Ethanol

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

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experimental_model

Chronic ethanol exposure in rodents and human Caco-2 cells

exposure

Chronic ethanol feeding or culture exposure

limitations

Animal feeding and human cell experiments are separate; no human dietary depletion threshold was established.

nutrient_topic

Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin

organism

Homo sapiens

plain_language

Alcohol exposure reduced the cell signals that produce the shared vitamin transporter.

primary_references

[b7-p21148397] Inhibition of intestinal biotin absorption by chronic alcohol feeding: cellular and molecular mechanisms. (2011). https://pubmed.ncbi.nlm.nih.gov/21148397/ DOI: 10.1152/ajpgi.00465.2010

tissue_or_cell_type

Caco-2 intestinal epithelial cells

trigger_kind

machinery_impairment Imported condition classification; unverified.

Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 221–232

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chronic ethanol exposure in rodents and human Caco-2 cells · source_derived_draft · unverified_draft

### b7-alcohol-promoters Chronic ethanol exposure reduced activity of both SLC5A6 promoters P1 and P2 in human Caco-2 cells. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Alcohol exposure reduced the cell signals that produce the shared vitamin transporter. organism: Homo sapiens tissue_or_cell_type: Caco-2 intestinal epithelial cells experimental_model: Chronic ethanol exposure in rodents and human Caco-2 cells limitations: Animal feeding and human cell experiments are separate; no human dietary depletion threshold was established. exposure: Chronic ethanol feeding or culture exposure evidence_span: {"source_cache": "artifacts/biotin-research/21148397.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2398f4926e678d4650eba6488cab945c2d651a7c8e6c2f8fd00794c0ea891d4d", "start_char": 0, "end_char": 1829, "text_sha256": "2398f4926e678d4650eba6488cab945c2d651a7c8e6c2f8fd00794c0ea891d4d"} [b7-p21148397] Inhibition of intestinal biotin absorption by chronic alcohol feeding: cellular and molecular mechanisms. (2011). https://pubmed.ncbi.nlm.nih.gov/21148397/ DOI: 10.1152/ajpgi.00465.2010

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

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experimental_model

Chronic ethanol exposure in rodents and human Caco-2 cells

exposure

Chronic ethanol feeding or culture exposure

limitations

Animal feeding and human cell experiments are separate; no human dietary depletion threshold was established.

nutrient_topic

Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin

organism

Rattus norvegicus

plain_language

In rats, chronic alcohol feeding impaired both measured sides of intestinal biotin transport.

primary_references

[b7-p21148397] Inhibition of intestinal biotin absorption by chronic alcohol feeding: cellular and molecular mechanisms. (2011). https://pubmed.ncbi.nlm.nih.gov/21148397/ DOI: 10.1152/ajpgi.00465.2010

tissue_or_cell_type

Rat jejunal membrane preparations

trigger_kind

machinery_impairment Imported condition classification; unverified.

Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 234–245

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chronic ethanol exposure in rodents and human Caco-2 cells · source_derived_draft · unverified_draft

### b7-alcohol-rat-uptake Chronic ethanol feeding reduced carrier-mediated biotin uptake across rat jejunal brush-border and basolateral membranes. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: In rats, chronic alcohol feeding impaired both measured sides of intestinal biotin transport. organism: Rattus norvegicus tissue_or_cell_type: Rat jejunal membrane preparations experimental_model: Chronic ethanol exposure in rodents and human Caco-2 cells limitations: Animal feeding and human cell experiments are separate; no human dietary depletion threshold was established. exposure: Chronic ethanol feeding or culture exposure evidence_span: {"source_cache": "artifacts/biotin-research/21148397.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "2398f4926e678d4650eba6488cab945c2d651a7c8e6c2f8fd00794c0ea891d4d", "start_char": 0, "end_char": 1829, "text_sha256": "2398f4926e678d4650eba6488cab945c2d651a7c8e6c2f8fd00794c0ea891d4d"} [b7-p21148397] Inhibition of intestinal biotin absorption by chronic alcohol feeding: cellular and molecular mechanisms. (2011). https://pubmed.ncbi.nlm.nih.gov/21148397/ DOI: 10.1152/ajpgi.00465.2010

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

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experimental_model

Chronic ethanol exposure in renal HK-2 cells and separate rodents

exposure

Chronic ethanol exposure

limitations

HK-2 uptake is a model of renal handling, not a measured whole-body biotin loss in people.

nutrient_topic

Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin

organism

Homo sapiens

plain_language

Reduced transporter production is one explanation for the impaired uptake.

primary_references

[b7-p21209005] Chronic alcohol exposure negatively impacts the physiological and molecular parameters of the renal biotin reabsorption process. (2011). https://pubmed.ncbi.nlm.nih.gov/21209005/ DOI: 10.1152/ajprenal.00707.2010

tissue_or_cell_type

Human HK-2 proximal-tubular epithelial cells

trigger_kind

machinery_impairment Imported condition classification; unverified.

Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 260–271

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chronic ethanol exposure in renal HK-2 cells and separate rodents · source_derived_draft · unverified_draft

### b7-kidney-alcohol-transcription Ethanol-exposed HK-2 cells showed reduced activity of the human SLC5A6 regulatory region. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reduced transporter production is one explanation for the impaired uptake. organism: Homo sapiens tissue_or_cell_type: Human HK-2 proximal-tubular epithelial cells experimental_model: Chronic ethanol exposure in renal HK-2 cells and separate rodents limitations: HK-2 uptake is a model of renal handling, not a measured whole-body biotin loss in people. exposure: Chronic ethanol exposure evidence_span: {"source_cache": "artifacts/biotin-research/21209005.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b42defcb27acffce0c264240e14b0535770f94627ee5a4836b284e4e0971b5a0", "start_char": 0, "end_char": 1797, "text_sha256": "b42defcb27acffce0c264240e14b0535770f94627ee5a4836b284e4e0971b5a0"} [b7-p21209005] Chronic alcohol exposure negatively impacts the physiological and molecular parameters of the renal biotin reabsorption process. (2011). https://pubmed.ncbi.nlm.nih.gov/21209005/ DOI: 10.1152/ajprenal.00707.2010

availability_state

machinery_impairment Imported condition classification; unverified.

evidence_span

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experimental_model

Chronic ethanol exposure in renal HK-2 cells and separate rodents

exposure

Chronic ethanol exposure

limitations

HK-2 uptake is a model of renal handling, not a measured whole-body biotin loss in people.

nutrient_topic

Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin

organism

Homo sapiens

plain_language

Kidney cells reclaimed less biotin in this alcohol-exposure model.

primary_references

[b7-p21209005] Chronic alcohol exposure negatively impacts the physiological and molecular parameters of the renal biotin reabsorption process. (2011). https://pubmed.ncbi.nlm.nih.gov/21209005/ DOI: 10.1152/ajprenal.00707.2010

tissue_or_cell_type

Human HK-2 proximal-tubular epithelial cells

trigger_kind

machinery_impairment Imported condition classification; unverified.

Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 247–258

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Chronic ethanol exposure in renal HK-2 cells and separate rodents · source_derived_draft · unverified_draft

### b7-kidney-alcohol-uptake Chronic ethanol exposure reduced carrier-mediated biotin uptake in human HK-2 cells. Condition category: machinery_impairment nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Kidney cells reclaimed less biotin in this alcohol-exposure model. organism: Homo sapiens tissue_or_cell_type: Human HK-2 proximal-tubular epithelial cells experimental_model: Chronic ethanol exposure in renal HK-2 cells and separate rodents limitations: HK-2 uptake is a model of renal handling, not a measured whole-body biotin loss in people. exposure: Chronic ethanol exposure evidence_span: {"source_cache": "artifacts/biotin-research/21209005.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b42defcb27acffce0c264240e14b0535770f94627ee5a4836b284e4e0971b5a0", "start_char": 0, "end_char": 1797, "text_sha256": "b42defcb27acffce0c264240e14b0535770f94627ee5a4836b284e4e0971b5a0"} [b7-p21209005] Chronic alcohol exposure negatively impacts the physiological and molecular parameters of the renal biotin reabsorption process. (2011). https://pubmed.ncbi.nlm.nih.gov/21209005/ DOI: 10.1152/ajprenal.00707.2010

availability_state

biomarker_context Imported condition classification; unverified.

evidence_span

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experimental_model

In vivo stable-isotope labelling in mice, with primary hippocampal neurons and behavioural testing

exposure

Labelled alcohol or heavy-labelled acetate administered in vivo, with ACSS2 inhibition and deletion

limitations

Isotope labelling traces the actual carbon atoms onto histones, which is stronger than correlating acetylation with exposure. A mouse study; the fetal result is a single reported exposure.

nutrient_topic

Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid

organism

Mouse

plain_language

The same atoms cross into the fetus and land on the chromatin of its developing brain.

primary_references

[acetate-p31645761] Alcohol metabolism contributes to brain histone acetylation. (2019). https://pubmed.ncbi.nlm.nih.gov/31645761/ DOI: 10.1038/s41586-019-1700-7

tissue_or_cell_type

Brain and gestating fetus

trigger_kind

biomarker_context Imported condition classification; unverified.

Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 628–639

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vivo stable-isotope labelling in mice, with primary hippocampal neurons and behavioural testing · source_derived_draft · unverified_draft

### acetate-maternal-alcohol-fetal-brain In a pregnant mouse, exposure to labelled alcohol resulted in the incorporation of labelled acetyl groups into gestating fetal brains. Condition category: biomarker_context nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: The same atoms cross into the fetus and land on the chromatin of its developing brain. organism: Mouse tissue_or_cell_type: Brain and gestating fetus experimental_model: In vivo stable-isotope labelling in mice, with primary hippocampal neurons and behavioural testing limitations: Isotope labelling traces the actual carbon atoms onto histones, which is stronger than correlating acetylation with exposure. A mouse study; the fetal result is a single reported exposure. exposure: Labelled alcohol or heavy-labelled acetate administered in vivo, with ACSS2 inhibition and deletion evidence_span: {"source_cache": "artifacts/acetate-research/31645761.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7a812a410fd8be3bad8512ab46d4b8a7fd3329d1552ee30965b66860eeb2b2f", "start_char": 0, "end_char": 1646, "text_sha256": "a7a812a410fd8be3bad8512ab46d4b8a7fd3329d1552ee30965b66860eeb2b2f"} [acetate-p31645761] Alcohol metabolism contributes to brain histone acetylation. (2019). https://pubmed.ncbi.nlm.nih.gov/31645761/ DOI: 10.1038/s41586-019-1700-7

evidence_span

{"source_cache": "artifacts/alcohol-research/3761194.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca", "start_char": 0, "end_char": 1539, "text_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca"}

experimental_model

In vivo microdialysis in freely moving rats

exposure

Ethanol administration with regional dopamine measurement

limitations

A reward-pathway measurement in freely moving animals. Dopamine release is a correlate of reinforcement, not a measure of liking or dependence.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat

plain_language

Alcohol raises dopamine in the brain region that marks things as worth repeating.

primary_references

[alcohol-p3761194] Preferential stimulation of dopamine release in the nucleus accumbens of freely moving rats by ethanol. (1986). https://pubmed.ncbi.nlm.nih.gov/3761194/ DOI: 10.1016/s0022-3565(25)23929-5

tissue_or_cell_type

Nucleus accumbens

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 423–434

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vivo microdialysis in freely moving rats · source_derived_draft · unverified_draft

### alcohol-accumbens-dopamine Ethanol preferentially stimulated dopamine release in the nucleus accumbens of freely moving rats. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol raises dopamine in the brain region that marks things as worth repeating. organism: Rat tissue_or_cell_type: Nucleus accumbens experimental_model: In vivo microdialysis in freely moving rats limitations: A reward-pathway measurement in freely moving animals. Dopamine release is a correlate of reinforcement, not a measure of liking or dependence. exposure: Ethanol administration with regional dopamine measurement evidence_span: {"source_cache": "artifacts/alcohol-research/3761194.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca", "start_char": 0, "end_char": 1539, "text_sha256": "98cf7c1ea1f6fbf3da6b89ab6beaed01a679ea1c8d4823f00952692a0c9203ca"} [alcohol-p3761194] Preferential stimulation of dopamine release in the nucleus accumbens of freely moving rats by ethanol. (1986). https://pubmed.ncbi.nlm.nih.gov/3761194/ DOI: 10.1016/s0022-3565(25)23929-5

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

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experimental_model

Pair-fed alcohol mice with regional permeability measurement and Caco-2 zinc deprivation

exposure

Four weeks of alcohol liquid diet; zinc deprivation in culture

limitations

The regional specificity and the separate zinc-deprivation arm are what make the nutrient claim interpretable. The exaggeration experiment is in cultured cells.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Mouse

plain_language

Alcohol drains zinc from one specific stretch of gut, and that is exactly where it leaks.

primary_references

[alcohol-p20167873] The role of zinc deficiency in alcohol-induced intestinal barrier dysfunction. (2010). https://pubmed.ncbi.nlm.nih.gov/20167873/ DOI: 10.1152/ajpgi.00350.2009

tissue_or_cell_type

Ileum and Caco-2 monolayers

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 761–772

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pair-fed alcohol mice with regional permeability measurement and Caco-2 zinc deprivation · source_derived_draft · unverified_draft

### alcohol-alcohol-ileal-zinc Alcohol exposure significantly reduced the ileal zinc concentration in association with accumulation of reactive oxygen species, and significantly increased permeability of the ileum without affecting the duodenum or jejunum. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol drains zinc from one specific stretch of gut, and that is exactly where it leaks. organism: Mouse tissue_or_cell_type: Ileum and Caco-2 monolayers experimental_model: Pair-fed alcohol mice with regional permeability measurement and Caco-2 zinc deprivation limitations: The regional specificity and the separate zinc-deprivation arm are what make the nutrient claim interpretable. The exaggeration experiment is in cultured cells. exposure: Four weeks of alcohol liquid diet; zinc deprivation in culture evidence_span: {"source_cache": "artifacts/alcohol-research/20167873.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "12b4bf025e28831a9d613fd7d6b62275f573f8a8999efb73d763bb8e8059b15e", "start_char": 0, "end_char": 1542, "text_sha256": "12b4bf025e28831a9d613fd7d6b62275f573f8a8999efb73d763bb8e8059b15e"} [alcohol-p20167873] The role of zinc deficiency in alcohol-induced intestinal barrier dysfunction. (2010). https://pubmed.ncbi.nlm.nih.gov/20167873/ DOI: 10.1152/ajpgi.00350.2009

evidence_span

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experimental_model

Structure-function mapping of the BK channel cytosolic gating ring

exposure

Alcohol applied to defined channel constructs

limitations

Identifies a discrete alcohol-sensing site. A site in a recombinant channel is not proof that occupancy explains an intact behaviour.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Recombinant channel

plain_language

Alcohol has a physical docking place on this potassium channel.

primary_references

[alcohol-p24927535] An alcohol-sensing site in the calcium- and voltage-gated, large conductance potassium (BK) channel. (2014). https://pubmed.ncbi.nlm.nih.gov/24927535/ DOI: 10.1073/pnas.1317363111

tissue_or_cell_type

BK channel

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 358–369

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Structure-function mapping of the BK channel cytosolic gating ring · source_derived_draft · unverified_draft

### alcohol-bk-alcohol-site An alcohol-sensing site was identified in the calcium- and voltage-gated large conductance potassium channel. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol has a physical docking place on this potassium channel. organism: Recombinant channel tissue_or_cell_type: BK channel experimental_model: Structure-function mapping of the BK channel cytosolic gating ring limitations: Identifies a discrete alcohol-sensing site. A site in a recombinant channel is not proof that occupancy explains an intact behaviour. exposure: Alcohol applied to defined channel constructs evidence_span: {"source_cache": "artifacts/alcohol-research/24927535.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "ef6f89212505affcd872cd85809dfd8f4036b04e6d3a86b2b24a3b5bdc33f706", "start_char": 0, "end_char": 1201, "text_sha256": "ef6f89212505affcd872cd85809dfd8f4036b04e6d3a86b2b24a3b5bdc33f706"} [alcohol-p24927535] An alcohol-sensing site in the calcium- and voltage-gated, large conductance potassium (BK) channel. (2014). https://pubmed.ncbi.nlm.nih.gov/24927535/ DOI: 10.1073/pnas.1317363111

evidence_span

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experimental_model

Ethanol treatment with ubiquitin conjugation and degradation assays

exposure

Ethanol exposure with measurement of CYP2E1 turnover

limitations

A protein-turnover mechanism rather than a transcriptional one. It explains why the second oxidation route appears quickly without new transcription.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat and cell systems

plain_language

Alcohol does not make more of this enzyme; it stops the cell destroying it.

primary_references

[alcohol-p8530344] Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1. (1995). https://pubmed.ncbi.nlm.nih.gov/8530344/ DOI: 10.1074/jbc.270.50.29632

tissue_or_cell_type

Hepatic microsomes

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 137–148

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ethanol treatment with ubiquitin conjugation and degradation assays · source_derived_draft · unverified_draft

### alcohol-cyp2e1-stabilisation Ethanol induces CYP2E1 by protein stabilisation, slowing the ubiquitin-conjugation-dependent rapid degradation of the enzyme rather than raising its synthesis. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol does not make more of this enzyme; it stops the cell destroying it. organism: Rat and cell systems tissue_or_cell_type: Hepatic microsomes experimental_model: Ethanol treatment with ubiquitin conjugation and degradation assays limitations: A protein-turnover mechanism rather than a transcriptional one. It explains why the second oxidation route appears quickly without new transcription. exposure: Ethanol exposure with measurement of CYP2E1 turnover evidence_span: {"source_cache": "artifacts/alcohol-research/8530344.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689", "start_char": 0, "end_char": 909, "text_sha256": "94e862c6432092ebcc448d94b25d00e1c2d9bd38197f2a7cd774202aeaebc689"} [alcohol-p8530344] Ethanol induces CYP2E1 by protein stabilization. Role of ubiquitin conjugation in the rapid degradation of CYP2E1. (1995). https://pubmed.ncbi.nlm.nih.gov/8530344/ DOI: 10.1074/jbc.270.50.29632

evidence_span

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experimental_model

Nucleoside transport and adenosine measurement in cultured cells during ethanol exposure

exposure

Ethanol exposure with adenosine uptake measurement

limitations

A transport mechanism for an indirect target: the effect is on adenosine handling, not on a receptor. Cultured cells.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Cultured cells

plain_language

Alcohol raises a natural sedative by blocking its reuptake.

primary_references

[alcohol-p2298733] Ethanol increases extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. (1990). https://pubmed.ncbi.nlm.nih.gov/2298733/ DOI: 10.1016/s0021-9258(19)39923-5

tissue_or_cell_type

Nucleoside transporter

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 410–421

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Nucleoside transport and adenosine measurement in cultured cells during ethanol exposure · source_derived_draft · unverified_draft

### alcohol-ent1-inhibition Ethanol increased extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol raises a natural sedative by blocking its reuptake. organism: Cultured cells tissue_or_cell_type: Nucleoside transporter experimental_model: Nucleoside transport and adenosine measurement in cultured cells during ethanol exposure limitations: A transport mechanism for an indirect target: the effect is on adenosine handling, not on a receptor. Cultured cells. exposure: Ethanol exposure with adenosine uptake measurement evidence_span: {"source_cache": "artifacts/alcohol-research/2298733.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "3933013c774b52112ebb838291e240d625dbf664faa2e94db35204bc38fb73d9", "start_char": 0, "end_char": 1419, "text_sha256": "3933013c774b52112ebb838291e240d625dbf664faa2e94db35204bc38fb73d9"} [alcohol-p2298733] Ethanol increases extracellular adenosine by inhibiting adenosine uptake via the nucleoside transporter. (1990). https://pubmed.ncbi.nlm.nih.gov/2298733/ DOI: 10.1016/s0021-9258(19)39923-5

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

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experimental_model

Review of folate transport systems in relation to alcoholism-induced malabsorption

exposure

Chronic ethanol ingestion against folate transport

limitations

A review, labelled as such, used for the enumeration of routes. The individual transport measurements are recorded from their own primary papers where available.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human and animal

plain_language

Alcohol attacks the vitamin at the doorway, in both gut and kidney.

primary_references

[alcohol-p19292860] New perspectives on folate transport in relation to alcoholism-induced folate malabsorption--association with epigenome stability and cancer development. (2009). https://pubmed.ncbi.nlm.nih.gov/19292860/ DOI: 10.1111/j.1742-4658.2009.06959.x

tissue_or_cell_type

Intestine, liver and kidney

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 683–694

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Review of folate transport systems in relation to alcoholism-induced malabsorption · source_derived_draft · unverified_draft

### alcohol-ethanol-folate-transport Ethanol reduces intestinal and renal uptake of folate by altering the binding and transport kinetics of folate transport systems and by reducing the expression of folate transporters, with ethanol ingestion described as the major contributor to folate deficiency. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol attacks the vitamin at the doorway, in both gut and kidney. organism: Human and animal tissue_or_cell_type: Intestine, liver and kidney experimental_model: Review of folate transport systems in relation to alcoholism-induced malabsorption limitations: A review, labelled as such, used for the enumeration of routes. The individual transport measurements are recorded from their own primary papers where available. exposure: Chronic ethanol ingestion against folate transport evidence_span: {"source_cache": "artifacts/alcohol-research/19292860.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "596af06cee715270d990c6fd6f421a3cf4efe2448193da3e58a35d74c2949e30", "start_char": 0, "end_char": 2909, "text_sha256": "596af06cee715270d990c6fd6f421a3cf4efe2448193da3e58a35d74c2949e30"} [alcohol-p19292860] New perspectives on folate transport in relation to alcoholism-induced folate malabsorption--association with epigenome stability and cancer development. (2009). https://pubmed.ncbi.nlm.nih.gov/19292860/ DOI: 10.1111/j.1742-4658.2009.06959.x

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

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experimental_model

Hepatic PLP metabolism during ethanol oxidation

exposure

Ethanol oxidation with hepatic PLP measurement

limitations

Extends the mechanism to liver. Part of the same series as the erythrocyte work, so the records share a laboratory lineage.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human and animal liver

plain_language

The same loss shows up in the organ that does the oxidising.

primary_references

[alcohol-p1168205] Vitamin B6 metabolism in chronic alcohol abuse The effect of ethanol oxidation on hepatic pyridoxal 5'-phosphate metabolism. (1975). https://pubmed.ncbi.nlm.nih.gov/1168205/ DOI: 10.1172/jci108003

tissue_or_cell_type

Liver

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 670–681

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Hepatic PLP metabolism during ethanol oxidation · source_derived_draft · unverified_draft

### alcohol-ethanol-oxidation-hepatic-plp The effect of ethanol oxidation on hepatic pyridoxal 5-phosphate metabolism accompanied the plasma changes seen in chronic alcohol abuse. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The same loss shows up in the organ that does the oxidising. organism: Human and animal liver tissue_or_cell_type: Liver experimental_model: Hepatic PLP metabolism during ethanol oxidation limitations: Extends the mechanism to liver. Part of the same series as the erythrocyte work, so the records share a laboratory lineage. exposure: Ethanol oxidation with hepatic PLP measurement evidence_span: {"source_cache": "artifacts/alcohol-research/1168205.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "b436a7e8353028a5eb7cf608b2a272b39968ee2af717dbae8fb03a39cb77180d", "start_char": 0, "end_char": 1391, "text_sha256": "b436a7e8353028a5eb7cf608b2a272b39968ee2af717dbae8fb03a39cb77180d"} [alcohol-p1168205] Vitamin B6 metabolism in chronic alcohol abuse The effect of ethanol oxidation on hepatic pyridoxal 5'-phosphate metabolism. (1975). https://pubmed.ncbi.nlm.nih.gov/1168205/ DOI: 10.1172/jci108003

evidence_span

{"source_cache": "artifacts/alcohol-research/17159992.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fbee66c99566521e71ae6b95b34c77426888dd791b27b2e3dad3a215a12441f7", "start_char": 0, "end_char": 1048, "text_sha256": "fbee66c99566521e71ae6b95b34c77426888dd791b27b2e3dad3a215a12441f7"}

experimental_model

Recombinant GABA-A receptor subunit combinations tested for ethanol sensitivity

exposure

Ethanol at low millimolar concentrations on defined subunit partnerships

limitations

Identifies a subunit combination sensitive at drinking-relevant concentrations, which had been the main objection to GABA-A as a direct target.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Recombinant human and rodent subunits

plain_language

A specific combination of receptor parts responds to alcohol at the concentrations drinking produces.

primary_references

[alcohol-p17159992] A new naturally occurring GABA(A) receptor subunit partnership with high sensitivity to ethanol. (2007). https://pubmed.ncbi.nlm.nih.gov/17159992/ DOI: 10.1038/nn1813

tissue_or_cell_type

Extrasynaptic GABA-A receptors

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 319–330

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant GABA-A receptor subunit combinations tested for ethanol sensitivity · source_derived_draft · unverified_draft

### alcohol-gaba-subunit-sensitivity A naturally occurring GABA-A receptor subunit partnership was identified with high sensitivity to ethanol. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: A specific combination of receptor parts responds to alcohol at the concentrations drinking produces. organism: Recombinant human and rodent subunits tissue_or_cell_type: Extrasynaptic GABA-A receptors experimental_model: Recombinant GABA-A receptor subunit combinations tested for ethanol sensitivity limitations: Identifies a subunit combination sensitive at drinking-relevant concentrations, which had been the main objection to GABA-A as a direct target. exposure: Ethanol at low millimolar concentrations on defined subunit partnerships evidence_span: {"source_cache": "artifacts/alcohol-research/17159992.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fbee66c99566521e71ae6b95b34c77426888dd791b27b2e3dad3a215a12441f7", "start_char": 0, "end_char": 1048, "text_sha256": "fbee66c99566521e71ae6b95b34c77426888dd791b27b2e3dad3a215a12441f7"} [alcohol-p17159992] A new naturally occurring GABA(A) receptor subunit partnership with high sensitivity to ethanol. (2007). https://pubmed.ncbi.nlm.nih.gov/17159992/ DOI: 10.1038/nn1813

evidence_span

{"source_cache": "artifacts/alcohol-research/19561601.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6aa4c10bd615439d1b5e008da1031a4ed244aeef6a0be4764930a7f183778428", "start_char": 0, "end_char": 1103, "text_sha256": "6aa4c10bd615439d1b5e008da1031a4ed244aeef6a0be4764930a7f183778428"}

experimental_model

Mutagenesis and structural mapping of the GIRK cytoplasmic domain

exposure

Alcohol binding to a defined hydrophobic pocket

limitations

Locates the site to a discrete pocket, which supports direct binding over a bulk membrane effect.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Recombinant channels

plain_language

The same picture again: a specific pocket, not a general softening of the membrane.

primary_references

[alcohol-p19561601] A discrete alcohol pocket involved in GIRK channel activation. (2009). https://pubmed.ncbi.nlm.nih.gov/19561601/ DOI: 10.1038/nn.2358

tissue_or_cell_type

GIRK cytoplasmic domain

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 397–408

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mutagenesis and structural mapping of the GIRK cytoplasmic domain · source_derived_draft · unverified_draft

### alcohol-girk-pocket A discrete alcohol pocket in the channel cytoplasmic domain was shown to be involved in GIRK channel activation. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The same picture again: a specific pocket, not a general softening of the membrane. organism: Recombinant channels tissue_or_cell_type: GIRK cytoplasmic domain experimental_model: Mutagenesis and structural mapping of the GIRK cytoplasmic domain limitations: Locates the site to a discrete pocket, which supports direct binding over a bulk membrane effect. exposure: Alcohol binding to a defined hydrophobic pocket evidence_span: {"source_cache": "artifacts/alcohol-research/19561601.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "6aa4c10bd615439d1b5e008da1031a4ed244aeef6a0be4764930a7f183778428", "start_char": 0, "end_char": 1103, "text_sha256": "6aa4c10bd615439d1b5e008da1031a4ed244aeef6a0be4764930a7f183778428"} [alcohol-p19561601] A discrete alcohol pocket involved in GIRK channel activation. (2009). https://pubmed.ncbi.nlm.nih.gov/19561601/ DOI: 10.1038/nn.2358

evidence_span

{"source_cache": "artifacts/alcohol-research/10570485.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "42da0b6588f0ec74c04be8d7a13a0aec3d34ed9e01b92af9cfad92eb3e79714b", "start_char": 0, "end_char": 827, "text_sha256": "42da0b6588f0ec74c04be8d7a13a0aec3d34ed9e01b92af9cfad92eb3e79714b"}

experimental_model

Heterologous expression of GIRK channels with alcohol application

exposure

Intoxicating alcohol concentrations

limitations

Establishes the channel family as a direct target. Recombinant expression, not native neurons.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Recombinant channels

plain_language

Alcohol opens a potassium channel that quietens neurons.

primary_references

[alcohol-p10570485] G-protein-coupled inwardly rectifying potassium channels are targets of alcohol action. (1999). https://pubmed.ncbi.nlm.nih.gov/10570485/ DOI: 10.1038/16012

tissue_or_cell_type

Neuronal potassium channels

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 384–395

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Heterologous expression of GIRK channels with alcohol application · source_derived_draft · unverified_draft

### alcohol-girk-target G-protein-gated inwardly rectifying potassium channels are targets of alcohol action, activated at intoxicating concentrations. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol opens a potassium channel that quietens neurons. organism: Recombinant channels tissue_or_cell_type: Neuronal potassium channels experimental_model: Heterologous expression of GIRK channels with alcohol application limitations: Establishes the channel family as a direct target. Recombinant expression, not native neurons. exposure: Intoxicating alcohol concentrations evidence_span: {"source_cache": "artifacts/alcohol-research/10570485.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "42da0b6588f0ec74c04be8d7a13a0aec3d34ed9e01b92af9cfad92eb3e79714b", "start_char": 0, "end_char": 827, "text_sha256": "42da0b6588f0ec74c04be8d7a13a0aec3d34ed9e01b92af9cfad92eb3e79714b"} [alcohol-p10570485] G-protein-coupled inwardly rectifying potassium channels are targets of alcohol action. (1999). https://pubmed.ncbi.nlm.nih.gov/10570485/ DOI: 10.1038/16012

evidence_span

{"source_cache": "artifacts/alcohol-research/9452448.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec", "start_char": 0, "end_char": 1618, "text_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec"}

experimental_model

Site-directed mutagenesis of glycine receptor position alpha267 with alcohols of differing size

exposure

A series of alcohols against residue volume at alpha267

limitations

A volume-series experiment that argues for a discrete binding pocket rather than a membrane-disordering effect. It is recombinant receptor electrophysiology.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Recombinant receptor

plain_language

Make the pocket smaller and alcohol works less, which is what a real binding site looks like.

primary_references

[alcohol-p9452448] Enhancement of glycine receptor function by ethanol is inversely correlated with molecular volume at position alpha267. (1998). https://pubmed.ncbi.nlm.nih.gov/9452448/ DOI: 10.1074/jbc.273.6.3314

tissue_or_cell_type

Glycine receptor

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 345–356

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Site-directed mutagenesis of glycine receptor position alpha267 with alcohols of differing size · source_derived_draft · unverified_draft

### alcohol-glycine-receptor-pocket Enhancement of glycine receptor function by ethanol was inversely correlated with the molecular volume at position alpha267, implying a size-limited site rather than a general membrane effect. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Make the pocket smaller and alcohol works less, which is what a real binding site looks like. organism: Recombinant receptor tissue_or_cell_type: Glycine receptor experimental_model: Site-directed mutagenesis of glycine receptor position alpha267 with alcohols of differing size limitations: A volume-series experiment that argues for a discrete binding pocket rather than a membrane-disordering effect. It is recombinant receptor electrophysiology. exposure: A series of alcohols against residue volume at alpha267 evidence_span: {"source_cache": "artifacts/alcohol-research/9452448.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec", "start_char": 0, "end_char": 1618, "text_sha256": "e1dd90423748e82a02cec583a8bbfcfd2ee9dcf8da9c126ddf5c5198011820ec"} [alcohol-p9452448] Enhancement of glycine receptor function by ethanol is inversely correlated with molecular volume at position alpha267. (1998). https://pubmed.ncbi.nlm.nih.gov/9452448/ DOI: 10.1074/jbc.273.6.3314

evidence_span

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experimental_model

Ethanol-fed mice with hepatic AMPK and SREBP-1 measurement

exposure

Chronic ethanol feeding

limitations

A signalling route to steatosis measured in mice. It sits alongside, not instead of, the redox explanation for fatty liver.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Mouse

plain_language

Alcohol rewires the liver’s fat-building programme through the energy sensor.

primary_references

[alcohol-p21953514] Regulation of hepatic lipin-1 by ethanol: role of AMP-activated protein kinase/sterol regulatory element-binding protein 1 signaling in mice. (2012). https://pubmed.ncbi.nlm.nih.gov/21953514/ DOI: 10.1002/hep.24708

tissue_or_cell_type

Liver

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 436–447

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ethanol-fed mice with hepatic AMPK and SREBP-1 measurement · source_derived_draft · unverified_draft

### alcohol-lipin1-srebp Ethanol regulated hepatic lipin-1 through AMP-activated protein kinase and sterol regulatory element-binding protein 1 signalling in mice. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol rewires the liver’s fat-building programme through the energy sensor. organism: Mouse tissue_or_cell_type: Liver experimental_model: Ethanol-fed mice with hepatic AMPK and SREBP-1 measurement limitations: A signalling route to steatosis measured in mice. It sits alongside, not instead of, the redox explanation for fatty liver. exposure: Chronic ethanol feeding evidence_span: {"source_cache": "artifacts/alcohol-research/21953514.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "acfcd2656e45aab9abcf367ed27e447001ddaa55ac143e9cc2f24b0958ea15a7", "start_char": 0, "end_char": 1626, "text_sha256": "acfcd2656e45aab9abcf367ed27e447001ddaa55ac143e9cc2f24b0958ea15a7"} [alcohol-p21953514] Regulation of hepatic lipin-1 by ethanol: role of AMP-activated protein kinase/sterol regulatory element-binding protein 1 signaling in mice. (2012). https://pubmed.ncbi.nlm.nih.gov/21953514/ DOI: 10.1002/hep.24708

evidence_span

{"source_cache": "artifacts/alcohol-research/4342558.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d", "start_char": 0, "end_char": 959, "text_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d"}

experimental_model

Freeze-clamped liver metabolite measurement in starved rats after ethanol

exposure

Single ethanol dose, sampled over 30 minutes in fed and starved animals

limitations

The classic redox measurement. Metabolite ratios are calculated from near-equilibrium assumptions rather than measured directly, which the authors state.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat

plain_language

Two other energy ratios move as well, and they recover on different timescales.

primary_references

[alcohol-p4342558] The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver. (1972). https://pubmed.ncbi.nlm.nih.gov/4342558/ DOI: 10.1042/bj1270387

tissue_or_cell_type

Liver

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 111–122

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Freeze-clamped liver metabolite measurement in starved rats after ethanol · source_derived_draft · unverified_draft

### alcohol-nadp-and-phosphorylation The free cytosolic NADP+/NADPH ratio fell immediately and returned nearly to control by 15 minutes, while the cytosolic ATP/ADP phosphate ratio was elevated at 15 minutes in starved rats. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Two other energy ratios move as well, and they recover on different timescales. organism: Rat tissue_or_cell_type: Liver experimental_model: Freeze-clamped liver metabolite measurement in starved rats after ethanol limitations: The classic redox measurement. Metabolite ratios are calculated from near-equilibrium assumptions rather than measured directly, which the authors state. exposure: Single ethanol dose, sampled over 30 minutes in fed and starved animals evidence_span: {"source_cache": "artifacts/alcohol-research/4342558.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d", "start_char": 0, "end_char": 959, "text_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d"} [alcohol-p4342558] The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver. (1972). https://pubmed.ncbi.nlm.nih.gov/4342558/ DOI: 10.1042/bj1270387

evidence_span

{"source_cache": "artifacts/alcohol-research/2467382.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c968c9a63cb2826e3986e1fd13f83fdf231adc1d46e0bc9aa73882cce6f0dca1", "start_char": 0, "end_char": 844, "text_sha256": "c968c9a63cb2826e3986e1fd13f83fdf231adc1d46e0bc9aa73882cce6f0dca1"}

experimental_model

Whole-cell recording from dissociated hippocampal neurons

exposure

Ethanol at intoxicating concentrations applied to NMDA-activated current

limitations

The founding electrophysiology result for this target. Concentrations are in the intoxicating range, which is what makes it relevant to drinking.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat

plain_language

Alcohol shuts down the brain’s main excitatory receptor at the doses people actually drink.

primary_references

[alcohol-p2467382] Ethanol inhibits NMDA-activated ion current in hippocampal neurons. (1989). https://pubmed.ncbi.nlm.nih.gov/2467382/ DOI: 10.1126/science.2467382

tissue_or_cell_type

Hippocampal neurons

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 280–291

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Whole-cell recording from dissociated hippocampal neurons · source_derived_draft · unverified_draft

### alcohol-nmda-inhibition Ethanol inhibited NMDA-activated ion current in hippocampal neurons at concentrations reached during intoxication. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol shuts down the brain’s main excitatory receptor at the doses people actually drink. organism: Rat tissue_or_cell_type: Hippocampal neurons experimental_model: Whole-cell recording from dissociated hippocampal neurons limitations: The founding electrophysiology result for this target. Concentrations are in the intoxicating range, which is what makes it relevant to drinking. exposure: Ethanol at intoxicating concentrations applied to NMDA-activated current evidence_span: {"source_cache": "artifacts/alcohol-research/2467382.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c968c9a63cb2826e3986e1fd13f83fdf231adc1d46e0bc9aa73882cce6f0dca1", "start_char": 0, "end_char": 844, "text_sha256": "c968c9a63cb2826e3986e1fd13f83fdf231adc1d46e0bc9aa73882cce6f0dca1"} [alcohol-p2467382] Ethanol inhibits NMDA-activated ion current in hippocampal neurons. (1989). https://pubmed.ncbi.nlm.nih.gov/2467382/ DOI: 10.1126/science.2467382

evidence_span

{"source_cache": "artifacts/alcohol-research/2158533.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "62f29619272239be27b46fe08d9e439abb782cfe87fdb17351d50bfc0e22aa92", "start_char": 0, "end_char": 1708, "text_sha256": "62f29619272239be27b46fe08d9e439abb782cfe87fdb17351d50bfc0e22aa92"}

experimental_model

Extracellular recording in adult rat hippocampal slice

exposure

Ethanol applied to synaptic responses

limitations

Shows the inhibition is selective for the NMDA component rather than general synaptic depression.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat

plain_language

It is that one receptor being blocked, not the whole synapse being quietened.

primary_references

[alcohol-p2158533] NMDA receptor-mediated synaptic excitation selectively inhibited by ethanol in hippocampal slice from adult rat. (1990). https://pubmed.ncbi.nlm.nih.gov/2158533/ DOI: 10.1523/jneurosci.10-04-01372.1990

tissue_or_cell_type

Hippocampus

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 293–304

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Extracellular recording in adult rat hippocampal slice · source_derived_draft · unverified_draft

### alcohol-nmda-selective NMDA receptor-mediated synaptic excitation was selectively inhibited by ethanol in hippocampal slices from adult rats. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: It is that one receptor being blocked, not the whole synapse being quietened. organism: Rat tissue_or_cell_type: Hippocampus experimental_model: Extracellular recording in adult rat hippocampal slice limitations: Shows the inhibition is selective for the NMDA component rather than general synaptic depression. exposure: Ethanol applied to synaptic responses evidence_span: {"source_cache": "artifacts/alcohol-research/2158533.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "62f29619272239be27b46fe08d9e439abb782cfe87fdb17351d50bfc0e22aa92", "start_char": 0, "end_char": 1708, "text_sha256": "62f29619272239be27b46fe08d9e439abb782cfe87fdb17351d50bfc0e22aa92"} [alcohol-p2158533] NMDA receptor-mediated synaptic excitation selectively inhibited by ethanol in hippocampal slice from adult rat. (1990). https://pubmed.ncbi.nlm.nih.gov/2158533/ DOI: 10.1523/jneurosci.10-04-01372.1990

evidence_span

{"source_cache": "artifacts/alcohol-research/4342558.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d", "start_char": 0, "end_char": 959, "text_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d"}

experimental_model

Freeze-clamped liver metabolite measurement in starved rats after ethanol

exposure

Single ethanol dose, sampled over 30 minutes in fed and starved animals

limitations

The classic redox measurement. Metabolite ratios are calculated from near-equilibrium assumptions rather than measured directly, which the authors state.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat

plain_language

Burning alcohol floods the cell with the reduced form of the carrier that every other pathway needs oxidised.

primary_references

[alcohol-p4342558] The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver. (1972). https://pubmed.ncbi.nlm.nih.gov/4342558/ DOI: 10.1042/bj1270387

tissue_or_cell_type

Liver

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 98–109

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Freeze-clamped liver metabolite measurement in starved rats after ethanol · source_derived_draft · unverified_draft

### alcohol-redox-shift Ethanol administration caused an immediate decrease in the NAD+/NADH ratio of both cytoplasm and mitochondria, which persisted over the 30 minutes studied. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Burning alcohol floods the cell with the reduced form of the carrier that every other pathway needs oxidised. organism: Rat tissue_or_cell_type: Liver experimental_model: Freeze-clamped liver metabolite measurement in starved rats after ethanol limitations: The classic redox measurement. Metabolite ratios are calculated from near-equilibrium assumptions rather than measured directly, which the authors state. exposure: Single ethanol dose, sampled over 30 minutes in fed and starved animals evidence_span: {"source_cache": "artifacts/alcohol-research/4342558.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d", "start_char": 0, "end_char": 959, "text_sha256": "dce57aa8128b432a841f087e3c4e70963b8fe318e462df980e6cdd66ed4af79d"} [alcohol-p4342558] The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver. (1972). https://pubmed.ncbi.nlm.nih.gov/4342558/ DOI: 10.1042/bj1270387

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/18005257.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1987e526f06b05a8f98b20048b73a9d01941fae9f69a718cc2fe134992b4a25b", "start_char": 0, "end_char": 2252, "text_sha256": "1987e526f06b05a8f98b20048b73a9d01941fae9f69a718cc2fe134992b4a25b"}

experimental_model

Experimental alcoholism model with intestinal brush border membrane transport measurement

exposure

Chronic ethanol feeding with reduced folate carrier measurement

limitations

Assigns the malabsorption to a named carrier. It is an animal model of chronic alcoholism.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Rat

plain_language

The specific carrier is made in smaller amounts.

primary_references

[alcohol-p18005257] Down-regulation of reduced folate carrier may result in folate malabsorption across intestinal brush border membrane during experimental alcoholism. (2007). https://pubmed.ncbi.nlm.nih.gov/18005257/ DOI: 10.1111/j.1742-4658.2007.06150.x

tissue_or_cell_type

Intestinal brush border

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 696–707

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Experimental alcoholism model with intestinal brush border membrane transport measurement · source_derived_draft · unverified_draft

### alcohol-rfc-downregulation Down-regulation of the reduced folate carrier may result in folate malabsorption across the intestinal brush border membrane during experimental alcoholism. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The specific carrier is made in smaller amounts. organism: Rat tissue_or_cell_type: Intestinal brush border experimental_model: Experimental alcoholism model with intestinal brush border membrane transport measurement limitations: Assigns the malabsorption to a named carrier. It is an animal model of chronic alcoholism. exposure: Chronic ethanol feeding with reduced folate carrier measurement evidence_span: {"source_cache": "artifacts/alcohol-research/18005257.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1987e526f06b05a8f98b20048b73a9d01941fae9f69a718cc2fe134992b4a25b", "start_char": 0, "end_char": 2252, "text_sha256": "1987e526f06b05a8f98b20048b73a9d01941fae9f69a718cc2fe134992b4a25b"} [alcohol-p18005257] Down-regulation of reduced folate carrier may result in folate malabsorption across intestinal brush border membrane during experimental alcoholism. (2007). https://pubmed.ncbi.nlm.nih.gov/18005257/ DOI: 10.1111/j.1742-4658.2007.06150.x

dose

6 ppm capsaicin rinse twice daily

duration

17 days

evidence_access

Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.

evidence_scope

literature_reviewed; model-specific source-derived curation

experimental_model

Healthy human volunteers

limitations

The result shows selective sensory adaptation, not shared binding to one receptor for every stimulus.

nutrient_topic

Capsaicin chapter; interacting nutrients, drugs, peptides and proteins retain their experimental settings. · Capsaicin

organism

Healthy human volunteers

plain_language

Repeated capsaicin rinsing reduced burn from vanillyl butyl ether, cinnamaldehyde and ethanol, while menthol cooling and sucrose sweetness did not change.

primary_references

Inducible desensitization to capsaicin with repeated low-dose exposure in human volunteers. (2024). https://pubmed.ncbi.nlm.nih.gov/38135109/ DOI: 10.1016/j.physbeh.2023.114447

route

Oral rinse

tissue

Cross-stimulus oral sensory ratings

Capsaicin: mechanism of action and interactions (2026-09-20) · lines 77–86

Original AI-assisted source-specific curation with primary-study citations, model, exposure, route, duration, negative findings and limitations preserved. Not publisher full text. · supports · Healthy human volunteers · source_derived_draft · unverified_draft

## capsaicin-human-cross-desensitization Repeated capsaicin rinsing reduced burn from vanillyl butyl ether, cinnamaldehyde and ethanol, while menthol cooling and sucrose sweetness did not change. Model/species: Healthy human volunteers Tissue/system: Cross-stimulus oral sensory ratings Exposure: 6 ppm capsaicin rinse twice daily Route: Oral rinse Duration: 17 days Limits: The result shows selective sensory adaptation, not shared binding to one receptor for every stimulus. Primary reference: Inducible desensitization to capsaicin with repeated low-dose exposure in human volunteers. (2024). https://pubmed.ncbi.nlm.nih.gov/38135109/ DOI: 10.1016/j.physbeh.2023.114447 Access: Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.

evidence_span

{"source_cache": "artifacts/acetate-research/31645761.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7a812a410fd8be3bad8512ab46d4b8a7fd3329d1552ee30965b66860eeb2b2f", "start_char": 0, "end_char": 1646, "text_sha256": "a7a812a410fd8be3bad8512ab46d4b8a7fd3329d1552ee30965b66860eeb2b2f"}

experimental_model

In vivo stable-isotope labelling in mice, with primary hippocampal neurons and behavioural testing

exposure

Labelled alcohol or heavy-labelled acetate administered in vivo, with ACSS2 inhibition and deletion

limitations

Isotope labelling traces the actual carbon atoms onto histones, which is stronger than correlating acetylation with exposure. A mouse study; the fetal result is a single reported exposure.

nutrient_topic

Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid

organism

Mouse

plain_language

Atoms from the drink end up on the proteins that package DNA in the brain.

primary_references

[acetate-p31645761] Alcohol metabolism contributes to brain histone acetylation. (2019). https://pubmed.ncbi.nlm.nih.gov/31645761/ DOI: 10.1038/s41586-019-1700-7

tissue_or_cell_type

Brain and gestating fetus

Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 615–626

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vivo stable-isotope labelling in mice, with primary hippocampal neurons and behavioural testing · source_derived_draft · unverified_draft

### acetate-alcohol-to-brain-histones Using in vivo stable-isotope labelling in mice, the metabolism of alcohol contributed to rapid acetylation of histones in the brain, in part through direct deposition of acetyl groups derived from alcohol onto histones in an ACSS2-dependent manner, and a similar direct deposition was observed when mice were injected with heavy-labelled acetate in vivo. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: Atoms from the drink end up on the proteins that package DNA in the brain. organism: Mouse tissue_or_cell_type: Brain and gestating fetus experimental_model: In vivo stable-isotope labelling in mice, with primary hippocampal neurons and behavioural testing limitations: Isotope labelling traces the actual carbon atoms onto histones, which is stronger than correlating acetylation with exposure. A mouse study; the fetal result is a single reported exposure. exposure: Labelled alcohol or heavy-labelled acetate administered in vivo, with ACSS2 inhibition and deletion evidence_span: {"source_cache": "artifacts/acetate-research/31645761.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a7a812a410fd8be3bad8512ab46d4b8a7fd3329d1552ee30965b66860eeb2b2f", "start_char": 0, "end_char": 1646, "text_sha256": "a7a812a410fd8be3bad8512ab46d4b8a7fd3329d1552ee30965b66860eeb2b2f"} [acetate-p31645761] Alcohol metabolism contributes to brain histone acetylation. (2019). https://pubmed.ncbi.nlm.nih.gov/31645761/ DOI: 10.1038/s41586-019-1700-7

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/4359937.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08", "start_char": 0, "end_char": 1650, "text_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08"}

experimental_model

Plasma PLP in 66 alcoholic subjects without liver abnormality, plus erythrocyte enzyme assays

exposure

Chronic alcohol abuse; acetaldehyde and ethanol applied to erythrocytes

limitations

Selecting subjects without abnormal liver function isolates the vitamin effect from liver disease. The phosphatase mechanism is shown in erythrocytes, not liver.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human

plain_language

It is the breakdown product that destroys the vitamin, and it works by exposing it to a phosphatase rather than by blocking its synthesis.

primary_references

[alcohol-p4359937] Vitamin B6 metabolism in chronic alcohol abuse. Pyridoxal phosphate levels in plasma and the effects of acetaldehyde on pyridoxal phosphate synthesis and degradation in human erythrocytes. (1974). https://pubmed.ncbi.nlm.nih.gov/4359937/ DOI: 10.1172/jci107607

tissue_or_cell_type

Plasma and erythrocytes

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 644–655

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Plasma PLP in 66 alcoholic subjects without liver abnormality, plus erythrocyte enzyme assays · source_derived_draft · unverified_draft

### alcohol-acetaldehyde-not-ethanol Acetaldehyde, but not ethanol, impaired net formation of PLP from pyridoxal, pyridoxine and pyridoxine phosphate by erythrocytes, and the effect was abolished when the B6-phosphate phosphatase was inhibited by 80 mM phosphate, while pyridoxal kinase and pyridoxine phosphate oxidase activities were not decreased. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: It is the breakdown product that destroys the vitamin, and it works by exposing it to a phosphatase rather than by blocking its synthesis. organism: Human tissue_or_cell_type: Plasma and erythrocytes experimental_model: Plasma PLP in 66 alcoholic subjects without liver abnormality, plus erythrocyte enzyme assays limitations: Selecting subjects without abnormal liver function isolates the vitamin effect from liver disease. The phosphatase mechanism is shown in erythrocytes, not liver. exposure: Chronic alcohol abuse; acetaldehyde and ethanol applied to erythrocytes evidence_span: {"source_cache": "artifacts/alcohol-research/4359937.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08", "start_char": 0, "end_char": 1650, "text_sha256": "1df4485150b1be55f3e5214c424f960ff627cfc317e643c86a0f6747efed8b08"} [alcohol-p4359937] Vitamin B6 metabolism in chronic alcohol abuse. Pyridoxal phosphate levels in plasma and the effects of acetaldehyde on pyridoxal phosphate synthesis and degradation in human erythrocytes. (1974). https://pubmed.ncbi.nlm.nih.gov/4359937/ DOI: 10.1172/jci107607

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/7596324.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30469341e3044e901ef2ebfa2e84bfb83b48044a455f1f0e415662eb2a9c6368", "start_char": 0, "end_char": 1186, "text_sha256": "30469341e3044e901ef2ebfa2e84bfb83b48044a455f1f0e415662eb2a9c6368"}

experimental_model

Review of alcoholic brain damage separating ethanol, thiamine deficiency and liver disease

exposure

Chronic alcohol exposure with and without thiamine deficiency

limitations

A review, labelled as such. Its value here is that it insists the three causes be separated rather than merged into one syndrome.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Human and animal

plain_language

The drinking and the missing vitamin do more damage together than either does alone.

primary_references

[alcohol-p7596324] Pathophysiology of alcoholic brain damage: synergistic effects of ethanol, thiamine deficiency and alcoholic liver disease. (1995). https://pubmed.ncbi.nlm.nih.gov/7596324/ DOI: 10.1007/bf01991777

tissue_or_cell_type

Brain

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 722–733

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Review of alcoholic brain damage separating ethanol, thiamine deficiency and liver disease · source_derived_draft · unverified_draft

### alcohol-thiamine-synergy The pathophysiology of alcoholic brain damage involves synergistic effects of ethanol, thiamine deficiency and alcoholic liver disease. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: The drinking and the missing vitamin do more damage together than either does alone. organism: Human and animal tissue_or_cell_type: Brain experimental_model: Review of alcoholic brain damage separating ethanol, thiamine deficiency and liver disease limitations: A review, labelled as such. Its value here is that it insists the three causes be separated rather than merged into one syndrome. exposure: Chronic alcohol exposure with and without thiamine deficiency evidence_span: {"source_cache": "artifacts/alcohol-research/7596324.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "30469341e3044e901ef2ebfa2e84bfb83b48044a455f1f0e415662eb2a9c6368", "start_char": 0, "end_char": 1186, "text_sha256": "30469341e3044e901ef2ebfa2e84bfb83b48044a455f1f0e415662eb2a9c6368"} [alcohol-p7596324] Pathophysiology of alcoholic brain damage: synergistic effects of ethanol, thiamine deficiency and alcoholic liver disease. (1995). https://pubmed.ncbi.nlm.nih.gov/7596324/ DOI: 10.1007/bf01991777

evidence_span

{"source_cache": "artifacts/alcohol-research/25157460.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20", "start_char": 0, "end_char": 1560, "text_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20"}

experimental_model

X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis

exposure

Coenzyme-bound closed and open subunit conformations

limitations

A yeast enzyme, used because its asymmetric tetramer captures two catalytic states. The zinc coordination chemistry is conserved, but kinetic numbers are yeast numbers.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Yeast enzyme

plain_language

Three amino acids hold the zinc, and a fourth swings in to hand over the alcohol.

primary_references

[alcohol-p25157460] Yeast alcohol dehydrogenase structure and catalysis. (2014). https://pubmed.ncbi.nlm.nih.gov/25157460/ DOI: 10.1021/bi5006442

tissue_or_cell_type

Purified homotetramer

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 72–83

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis · source_derived_draft · unverified_draft

### alcohol-zinc-coordination-chemistry In the closed subunits the catalytic zinc holds the substrate oxygen in classical tetrahedral coordination with Cys-43, Cys-153 and His-66, while in the open subunits the zinc takes an inverted coordination that adds the carboxylate of Glu-67, which may be an intermediate in displacing the zinc-bound water with the alcohol substrate. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Three amino acids hold the zinc, and a fourth swings in to hand over the alcohol. organism: Yeast enzyme tissue_or_cell_type: Purified homotetramer experimental_model: X-ray crystallography of yeast ADH1 at 2.4 angstrom with site-directed mutagenesis limitations: A yeast enzyme, used because its asymmetric tetramer captures two catalytic states. The zinc coordination chemistry is conserved, but kinetic numbers are yeast numbers. exposure: Coenzyme-bound closed and open subunit conformations evidence_span: {"source_cache": "artifacts/alcohol-research/25157460.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20", "start_char": 0, "end_char": 1560, "text_sha256": "c91a7069c53b4af61096bdc09ce952b0277d63d547a94e5d3870d2980aa31e20"} [alcohol-p25157460] Yeast alcohol dehydrogenase structure and catalysis. (2014). https://pubmed.ncbi.nlm.nih.gov/25157460/ DOI: 10.1021/bi5006442

availability_state

nutrient_deficiency Imported condition classification; unverified.

evidence_span

{"source_cache": "artifacts/alcohol-research/20167873.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "12b4bf025e28831a9d613fd7d6b62275f573f8a8999efb73d763bb8e8059b15e", "start_char": 0, "end_char": 1542, "text_sha256": "12b4bf025e28831a9d613fd7d6b62275f573f8a8999efb73d763bb8e8059b15e"}

experimental_model

Pair-fed alcohol mice with regional permeability measurement and Caco-2 zinc deprivation

exposure

Four weeks of alcohol liquid diet; zinc deprivation in culture

limitations

The regional specificity and the separate zinc-deprivation arm are what make the nutrient claim interpretable. The exaggeration experiment is in cultured cells.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Mouse and human cells

plain_language

Take zinc away and the seals between cells come apart, with or without alcohol.

primary_references

[alcohol-p20167873] The role of zinc deficiency in alcohol-induced intestinal barrier dysfunction. (2010). https://pubmed.ncbi.nlm.nih.gov/20167873/ DOI: 10.1152/ajpgi.00350.2009

tissue_or_cell_type

Ileum and Caco-2 monolayers

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 774–785

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Pair-fed alcohol mice with regional permeability measurement and Caco-2 zinc deprivation · source_derived_draft · unverified_draft

### alcohol-zinc-tight-junctions Zinc deprivation caused epithelial barrier disruption in association with disassembly of tight junction proteins in Caco-2 monolayers, and minor zinc deprivation exaggerated the deleterious effect of alcohol on the epithelial barrier. Condition category: nutrient_deficiency nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Take zinc away and the seals between cells come apart, with or without alcohol. organism: Mouse and human cells tissue_or_cell_type: Ileum and Caco-2 monolayers experimental_model: Pair-fed alcohol mice with regional permeability measurement and Caco-2 zinc deprivation limitations: The regional specificity and the separate zinc-deprivation arm are what make the nutrient claim interpretable. The exaggeration experiment is in cultured cells. exposure: Four weeks of alcohol liquid diet; zinc deprivation in culture evidence_span: {"source_cache": "artifacts/alcohol-research/20167873.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "12b4bf025e28831a9d613fd7d6b62275f573f8a8999efb73d763bb8e8059b15e", "start_char": 0, "end_char": 1542, "text_sha256": "12b4bf025e28831a9d613fd7d6b62275f573f8a8999efb73d763bb8e8059b15e"} [alcohol-p20167873] The role of zinc deficiency in alcohol-induced intestinal barrier dysfunction. (2010). https://pubmed.ncbi.nlm.nih.gov/20167873/ DOI: 10.1152/ajpgi.00350.2009