Hydrogen ion

cross_nutrient

false

experimental_model

In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice

exposure

In vitro pH manipulation

limitations

Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract.

nutrient_topic

Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)

organism

Homo sapiens

plain_language

Acid enabled release and capture of B12 from this food model.

primary_references

[carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i

tissue_or_cell_type

Gastric luminal digestion model

Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 88–99

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice · source_derived_draft · unverified_draft

### b12-abs-food-acid In the egg-yolk/human saliva model, acidification to pH 1.5 permitted limited cobalamin transfer to R binder; virtually none occurred above pH 2 despite pepsin. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Acid enabled release and capture of B12 from this food model. organism: Homo sapiens tissue_or_cell_type: Gastric luminal digestion model experimental_model: In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice limitations: Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract. exposure: In vitro pH manipulation cross_nutrient: false [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i

evidence_span

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experimental_model

Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression

exposure

Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5

limitations

Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established.

nutrient_topic

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

organism

Homo sapiens proteins and HEK cells

plain_language

Acidity changed the reaction rate in this assay.

primary_references

[mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177

tissue_or_cell_type

Purified redox system and human cell model

Molybdenum: cofactor assembly, sulfur metabolism and nutrient interactions (2026-09-17) · lines 1054–1065

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression · source_derived_draft · unverified_draft

### mo-marc-ph Lowering assay pH from 7.5 to 6.5 increased the reported mARC NO-formation rate by nearly threefold. Condition category: normal nutrient_topic: Molybdenum research collection; topical membership is not evidence of a direct dietary effect. plain_language: Acidity changed the reaction rate in this assay. organism: Homo sapiens proteins and HEK cells tissue_or_cell_type: Purified redox system and human cell model experimental_model: Recombinant human mARC1/mARC2, active-site mutation, tungsten replacement and HEK expression limitations: Shows nitrite-reducing capacity; its share of NO production in normal people and response to mineral intake are not established. exposure: Reduced enzyme, nitrite, NADH/CYB5/CYB5R; pH 7.5 versus 6.5 evidence_span: {"source_cache": "artifacts/molybdenum-research/24500710.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b", "start_char": 0, "end_char": 1585, "text_sha256": "e4c2ab41c945d420266290d0241752039d7de2cb6223f9c64c7d0525c5688d9b"} [mo-p24500710] Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2. (2014). https://pubmed.ncbi.nlm.nih.gov/24500710/ DOI: 10.1074/jbc.m114.555177

evidence_access

Primary full text, methods and protonation results

experimental_model

Purified dipeptides at 310.15 K and 0.15 M ionic strength.

limitations

Chemical buffering does not establish how much a supplement changes exercising muscle pH.

nutrient_topic

Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine

plain_language

Reversible proton binding gives the molecule buffering capacity.

primary_references

Species-specific acid-base characterization of carnosine and homocarnosine using nuclear magnetic resonance · 2022 · https://doi.org/10.1016/j.cplett.2022.140128 · DOI 10.1016/j.cplett.2022.140128

Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 180–186

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified dipeptides at 310.15 K and 0.15 M ionic strength. · source_derived_draft · unverified_draft

## carnosine-proton-buffer Reversible proton binding gives the molecule buffering capacity. NMR and potentiometric titration measured reversible protonation of carnosine, including its imidazole site near physiological pH. Model: Purified dipeptides at 310.15 K and 0.15 M ionic strength. Limitations: Chemical buffering does not establish how much a supplement changes exercising muscle pH. Evidence access: Primary full text, methods and protonation results Species-specific acid-base characterization of carnosine and homocarnosine using nuclear magnetic resonance · 2022 · https://doi.org/10.1016/j.cplett.2022.140128 · DOI 10.1016/j.cplett.2022.140128

endpoint

HCl infusion causing acute mineral acidemia raised plasma potassium in the conscious-dog experiment.

experimental-exposure

Experimental acute mineral acidemia with hyperkalemia; not potassium deficiency or excessive potassium intake.

experimental_model

Twelve conscious dogs with portal/hepatic/systemic sampling; beta-hydroxybutyric acid 7 mEq/kg or HCl 3 mEq/kg infused over 30 minutes; additional anesthetized and obstructed-urinary-tract studies.

limitations

Acute HCl infusion, not every acidosis; portal glucagon rose and direct H/K exchange was not isolated.

nutrient_topic

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

organism

Canis lupus familiaris

plain_language

Acid type affected the potassium response; a rise in blood potassium did not imply excess potassium intake.

primary_references

[adrogue-1985-acid-infusion] Role of the endocrine pancreas in the kalemic response to acute metabolic acidosis in conscious dogs (1985). https://www.jci.org/articles/view/111775 DOI: 10.1172/JCI111775

tissue_or_cell_type

systemic and splanchnic circulation

Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1151–1162

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Twelve conscious dogs with portal/hepatic/systemic sampling; beta-hydroxybutyric acid 7 mEq/kg or HCl 3 mEq/kg infused over 30 minutes; additional anesthetized and obstructed-urinary-tract studies. · source_derived_draft · unverified_draft

### hcl-acidemia-raises-plasma-k HCl infusion causing acute mineral acidemia raised plasma potassium in the conscious-dog experiment. Condition category: normal nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Acid type affected the potassium response; a rise in blood potassium did not imply excess potassium intake. organism: Canis lupus familiaris tissue_or_cell_type: systemic and splanchnic circulation experimental_model: Twelve conscious dogs with portal/hepatic/systemic sampling; beta-hydroxybutyric acid 7 mEq/kg or HCl 3 mEq/kg infused over 30 minutes; additional anesthetized and obstructed-urinary-tract studies. limitations: Acute HCl infusion, not every acidosis; portal glucagon rose and direct H/K exchange was not isolated. experimental-exposure: Experimental acute mineral acidemia with hyperkalemia; not potassium deficiency or excessive potassium intake. endpoint: HCl infusion causing acute mineral acidemia raised plasma potassium in the conscious-dog experiment. [adrogue-1985-acid-infusion] Role of the endocrine pancreas in the kalemic response to acute metabolic acidosis in conscious dogs (1985). https://www.jci.org/articles/view/111775 DOI: 10.1172/JCI111775

availability_state

nutrient_deficiency Imported condition classification; unverified.

endpoint

Luminal omeprazole abolished net total-CO2 flux used to measure acidification in collecting ducts from potassium-restricted rabbits.

experimental-exposure

Microperfused inner-stripe outer medullary collecting ducts from rabbits fed 0.55% potassium diet for 7-14 days; luminal omeprazole 0.1 mM.

experimental_model

Microperfused inner-stripe outer medullary collecting ducts from rabbits fed 0.55% potassium diet for 7-14 days; luminal omeprazole 0.1 mM.

limitations

Pharmacological activity assignment; the experiment does not isolate ATP4A versus ATP12A. Total-CO2 flux is an acidification surrogate.

nutrient_topic

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

organism

Oryctolagus cuniculus

plain_language

An H/K-pump-compatible activity supported acid secretion in the isolated duct.

primary_references

[wingo-1989-hka] Active proton secretion and potassium absorption in the rabbit outer medullary collecting duct. Functional evidence for proton-potassium-activated adenosine triphosphatase (1989). https://pubmed.ncbi.nlm.nih.gov/2544629/ DOI: 10.1172/JCI114165

tissue_or_cell_type

inner-stripe outer medullary collecting duct

transport_direction

potassium: tubular lumen toward blood; protons: cell toward tubular lumen

trigger_kind

nutrient_deficiency Imported condition classification; unverified.

Potassium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1096–1108

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Microperfused inner-stripe outer medullary collecting ducts from rabbits fed 0.55% potassium diet for 7-14 days; luminal omeprazole 0.1 mM. · source_derived_draft · unverified_draft

### hka-sensitive-proton-secretion Luminal omeprazole abolished net total-CO2 flux used to measure acidification in collecting ducts from potassium-restricted rabbits. Condition category: nutrient_deficiency nutrient_topic: Potassium research collection; topical membership is not evidence of a direct dietary effect. plain_language: An H/K-pump-compatible activity supported acid secretion in the isolated duct. organism: Oryctolagus cuniculus tissue_or_cell_type: inner-stripe outer medullary collecting duct experimental_model: Microperfused inner-stripe outer medullary collecting ducts from rabbits fed 0.55% potassium diet for 7-14 days; luminal omeprazole 0.1 mM. limitations: Pharmacological activity assignment; the experiment does not isolate ATP4A versus ATP12A. Total-CO2 flux is an acidification surrogate. transport_direction: potassium: tubular lumen toward blood; protons: cell toward tubular lumen experimental-exposure: Microperfused inner-stripe outer medullary collecting ducts from rabbits fed 0.55% potassium diet for 7-14 days; luminal omeprazole 0.1 mM. endpoint: Luminal omeprazole abolished net total-CO2 flux used to measure acidification in collecting ducts from potassium-restricted rabbits. [wingo-1989-hka] Active proton secretion and potassium absorption in the rabbit outer medullary collecting duct. Functional evidence for proton-potassium-activated adenosine triphosphatase (1989). https://pubmed.ncbi.nlm.nih.gov/2544629/ DOI: 10.1172/JCI114165

cross_nutrient

false

experimental_model

In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice

exposure

Pepsin supplementation at acidic pH

limitations

Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract.

nutrient_topic

Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)

organism

Homo sapiens

plain_language

Pepsin helped haptocorrin capture food-bound B12.

primary_references

[carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i

tissue_or_cell_type

Gastric luminal digestion model

Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 101–112

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice · source_derived_draft · unverified_draft

### b12-abs-food-pepsin Adding pepsin at 1,200 U/mL under acidic conditions increased egg-yolk cobalamin transfer to human salivary or gastric R binders to 39-58%. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Pepsin helped haptocorrin capture food-bound B12. organism: Homo sapiens tissue_or_cell_type: Gastric luminal digestion model experimental_model: In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice limitations: Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract. exposure: Pepsin supplementation at acidic pH cross_nutrient: false [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i

evidence_span

{"source_cache": "artifacts/niacin-redox-sources/nnt-structure-2019.abstract.txt", "locator": "Indexed abstract, reaction and structural mechanism", "start_char": 199, "end_char": 1759, "file_sha256": "edb35c2cdf2f57d604cb86da48665e5742d398f43c50f3e1622d161564c78a83", "text_sha256": "aa5063e57c35097c2fa2557ed9a7d61c3a411d90d0ded9b947525012520a5712"}

experimental_model

Cryo-EM of intact ovine NNT in different nucleotide states

exposure

Nucleotide-bound conformational states

limitations

Structural mechanism supported in ovine protein; forward flux is context dependent and not equivalent to adding phosphate to NAD. No human intake inference.

nutrient_topic

Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)

organism

Ovis aries

plain_language

NNT links the NADH and NADPH redox systems through membrane-coupled chemistry.

primary_references

[nnt-structure-2019] Structure and mechanism of mitochondrial proton-translocating transhydrogenase. (2019). https://pubmed.ncbi.nlm.nih.gov/31462775/ DOI: 10.1038/s41586-019-1519-2

tissue_or_cell_type

Purified mitochondrial protein

Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 1003–1014

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM of intact ovine NNT in different nucleotide states · source_derived_draft · unverified_draft

### b3-redox-nnt-coupling Structural analysis of mammalian NNT supported coupling of NADH-to-NADP+ hydride transfer to proton translocation across the mitochondrial membrane. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: NNT links the NADH and NADPH redox systems through membrane-coupled chemistry. organism: Ovis aries tissue_or_cell_type: Purified mitochondrial protein experimental_model: Cryo-EM of intact ovine NNT in different nucleotide states limitations: Structural mechanism supported in ovine protein; forward flux is context dependent and not equivalent to adding phosphate to NAD. No human intake inference. exposure: Nucleotide-bound conformational states evidence_span: {"source_cache": "artifacts/niacin-redox-sources/nnt-structure-2019.abstract.txt", "locator": "Indexed abstract, reaction and structural mechanism", "start_char": 199, "end_char": 1759, "file_sha256": "edb35c2cdf2f57d604cb86da48665e5742d398f43c50f3e1622d161564c78a83", "text_sha256": "aa5063e57c35097c2fa2557ed9a7d61c3a411d90d0ded9b947525012520a5712"} [nnt-structure-2019] Structure and mechanism of mitochondrial proton-translocating transhydrogenase. (2019). https://pubmed.ncbi.nlm.nih.gov/31462775/ DOI: 10.1038/s41586-019-1519-2

evidence_access

Primary abstract

experimental_model

Purified recombinant protein.

limitations

Do not assume CNDP2 is an equally active carnosinase at normal cytosolic pH.

nutrient_topic

Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine

plain_language

The similarly named enzyme behaved differently.

primary_references

Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200

Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 52–58

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified recombinant protein. · source_derived_draft · unverified_draft

## carnosine-cndp2-ph The similarly named enzyme behaved differently. Human CNDP2 hydrolyzed carnosine only under alkaline assay conditions, with an optimum near pH 9.5. Model: Purified recombinant protein. Limitations: Do not assume CNDP2 is an equally active carnosinase at normal cytosolic pH. Evidence access: Primary abstract Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12473676/ · DOI 10.1074/jbc.M209764200

evidence_access

Primary abstract

experimental_model

Buffered chemical reactions; adducts also detected in oxidized rat muscle homogenate.

limitations

Reaction chemistry does not measure clinical protection.

nutrient_topic

Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine

plain_language

The peptide can chemically trap a lipid-derived aldehyde.

primary_references

Carnosine is a quencher of 4-hydroxy-nonenal: through what mechanism of reaction? · 2002 · https://pubmed.ncbi.nlm.nih.gov/12419310/ · DOI 10.1016/s0006-291x(02)02545-7

Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 236–242

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Buffered chemical reactions; adducts also detected in oxidized rat muscle homogenate. · source_derived_draft · unverified_draft

## carnosine-hne-adduction The peptide can chemically trap a lipid-derived aldehyde. Carnosine reacted with HNE to form a stabilized Michael adduct and an imine macrocycle in a pH-dependent equilibrium. Model: Buffered chemical reactions; adducts also detected in oxidized rat muscle homogenate. Limitations: Reaction chemistry does not measure clinical protection. Evidence access: Primary abstract Carnosine is a quencher of 4-hydroxy-nonenal: through what mechanism of reaction? · 2002 · https://pubmed.ncbi.nlm.nih.gov/12419310/ · DOI 10.1016/s0006-291x(02)02545-7

evidence_access

Primary abstract

experimental_model

Human transporter expressed in Xenopus oocytes.

limitations

Transporter expression system, not whole-body bioavailability.

nutrient_topic

Carnosine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnosine / beta-alanyl-L-histidine

plain_language

A peptide transporter can carry intact carnosine.

primary_references

The bioactive dipeptide anserine is transported by human proton-coupled peptide transporters. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20067523/ · DOI 10.1111/j.1742-4658.2009.07528.x

transport_effect

raises Applying carnosine produced electrogenic proton-coupled inward transport currents.

transport_pool

the expressing cell Applying carnosine produced electrogenic proton-coupled inward transport currents.

Carnosine: synthesis, transport, carbonyl chemistry and nutrient interactions (2026-09-19) · lines 68–74

AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human transporter expressed in Xenopus oocytes. · source_derived_draft · unverified_draft

## carnosine-pept1 A peptide transporter can carry intact carnosine. Applying carnosine to oocytes expressing human PEPT1 produced electrogenic proton-coupled transport currents. Model: Human transporter expressed in Xenopus oocytes. Limitations: Transporter expression system, not whole-body bioavailability. Evidence access: Primary abstract The bioactive dipeptide anserine is transported by human proton-coupled peptide transporters. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20067523/ · DOI 10.1111/j.1742-4658.2009.07528.x

evidence_span

{"source_cache": "artifacts/inositol-research/11500374.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fb9efd53bbc0fae1bf1ada1525cdb7d10a4e700d3309bfba4e3a598c4a9c74b9", "start_char": 0, "end_char": 1270, "text_sha256": "fb9efd53bbc0fae1bf1ada1525cdb7d10a4e700d3309bfba4e3a598c4a9c74b9"}

experimental_model

Transporter expression and electrophysiology

exposure

Extracellular pH manipulation

limitations

Transport capacity after heterologous expression does not establish a neuronal plasma-membrane role in vivo.

nutrient_topic

Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)

organism

Rat brain transporter studied in Xenopus oocytes

plain_language

A different transporter can use a proton gradient, particularly in acidic experimental conditions.

primary_references

[ino-p11500374] Identification of a mammalian H(+)-myo-inositol symporter expressed predominantly in the brain. (2001). https://pubmed.ncbi.nlm.nih.gov/11500374/ DOI: 10.1093/emboj/20.16.4467

tissue_or_cell_type

Heterologous membranes and rat brain

transport_effect

raises Electrogenic proton-coupled myo-inositol uptake rising as pH fell.

transport_pool

the expressing cell Electrogenic proton-coupled myo-inositol uptake rising as pH fell.

Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 366–377

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Transporter expression and electrophysiology · source_derived_draft · unverified_draft

### ino-hmit-acid HMIT expressed in Xenopus oocytes mediated electrogenic proton-coupled myo-inositol uptake that increased as pH fell, with maximal tested activity near pH 5. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A different transporter can use a proton gradient, particularly in acidic experimental conditions. organism: Rat brain transporter studied in Xenopus oocytes tissue_or_cell_type: Heterologous membranes and rat brain experimental_model: Transporter expression and electrophysiology limitations: Transport capacity after heterologous expression does not establish a neuronal plasma-membrane role in vivo. exposure: Extracellular pH manipulation evidence_span: {"source_cache": "artifacts/inositol-research/11500374.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "fb9efd53bbc0fae1bf1ada1525cdb7d10a4e700d3309bfba4e3a598c4a9c74b9", "start_char": 0, "end_char": 1270, "text_sha256": "fb9efd53bbc0fae1bf1ada1525cdb7d10a4e700d3309bfba4e3a598c4a9c74b9"} [ino-p11500374] Identification of a mammalian H(+)-myo-inositol symporter expressed predominantly in the brain. (2001). https://pubmed.ncbi.nlm.nih.gov/11500374/ DOI: 10.1093/emboj/20.16.4467