Golgi apparatus

evidence_span

{"source_cache": "artifacts/inositol-research/19607714.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8b8bd010f44dd8b055efc345c57791e88547114b0a2f27d782183674fc53f984", "start_char": 0, "end_char": 1332, "text_sha256": "8b8bd010f44dd8b055efc345c57791e88547114b0a2f27d782183674fc53f984"}

experimental_model

Immunolocalization, neuronal electrophysiology and knockout

exposure

Native localization and HMIT-null comparisons

limitations

Native localization qualifies earlier heterologous uptake findings; it is an explained context difference, not evidence that one experiment is false.

nutrient_topic

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

organism

Rat and human brain; mouse knockout

plain_language

A transporter that works at an artificial cell surface may normally function inside the cell.

primary_references

[ino-p19607714] Evaluation of expression and function of the H+/myo-inositol transporter HMIT. (2009). https://pubmed.ncbi.nlm.nih.gov/19607714/ DOI: 10.1186/1471-2121-10-54

tissue_or_cell_type

Brain neurons and cultured neurons

Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 379–390

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

### ino-hmit-golgi HMIT localized to the Golgi apparatus in primary cultured neurons; HMIT-mediated currents were not detected in rat neurons or brain slices. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A transporter that works at an artificial cell surface may normally function inside the cell. organism: Rat and human brain; mouse knockout tissue_or_cell_type: Brain neurons and cultured neurons experimental_model: Immunolocalization, neuronal electrophysiology and knockout limitations: Native localization qualifies earlier heterologous uptake findings; it is an explained context difference, not evidence that one experiment is false. exposure: Native localization and HMIT-null comparisons evidence_span: {"source_cache": "artifacts/inositol-research/19607714.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8b8bd010f44dd8b055efc345c57791e88547114b0a2f27d782183674fc53f984", "start_char": 0, "end_char": 1332, "text_sha256": "8b8bd010f44dd8b055efc345c57791e88547114b0a2f27d782183674fc53f984"} [ino-p19607714] Evaluation of expression and function of the H+/myo-inositol transporter HMIT. (2009). https://pubmed.ncbi.nlm.nih.gov/19607714/ DOI: 10.1186/1471-2121-10-54

cross_nutrient

calcium ion (transported_ion); Manganese(II) ion (alternative_ion); Adenosine triphosphate (energy_substrate); Golgi apparatus (destination)

evidence_span

{"source_cache": "artifacts/manganese-glycosylation-sources/spca2023.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "start_char": 0, "end_char": 1276, "text_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "text_characters": 1276}

experimental_model

Cryo-EM of purified human SPCA1a with ATP and divalent ions

exposure

ATP/Ca2+, ATP/Mn2+ and phosphorylated metal-free structural states.

limitations

Structural states explain the transport cycle but do not supply a dietary requirement or prove that calcium supplementation impairs manganese delivery.

nutrient_topic

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

organism

Homo sapiens

plain_language

The same pump handles calcium and manganese through a shared site.

primary_references

[mn-gly-spca2023] Cryo-EM structures of human SPCA1a reveal the mechanism of Ca²⁺/Mn²⁺ transport into the Golgi apparatus. (2023). https://pubmed.ncbi.nlm.nih.gov/36867705/ DOI: 10.1126/sciadv.add9742

tissue_or_cell_type

Golgi membrane transport protein

transport_effect

raises The object already names import into the Golgi lumen.

transport_pool

the Golgi lumen The object already names import into the Golgi lumen.

Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 712–724

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM of purified human SPCA1a with ATP and divalent ions · source_derived_draft · unverified_draft

### mn-gly-spca-calcium Human SPCA1a also transports calcium; calcium and manganese occupy the same transmembrane pocket in the respective structures. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same pump handles calcium and manganese through a shared site. organism: Homo sapiens tissue_or_cell_type: Golgi membrane transport protein experimental_model: Cryo-EM of purified human SPCA1a with ATP and divalent ions limitations: Structural states explain the transport cycle but do not supply a dietary requirement or prove that calcium supplementation impairs manganese delivery. exposure: ATP/Ca2+, ATP/Mn2+ and phosphorylated metal-free structural states. cross_nutrient: calcium ion (transported_ion); Manganese(II) ion (alternative_ion); Adenosine triphosphate (energy_substrate); Golgi apparatus (destination) evidence_span: {"source_cache": "artifacts/manganese-glycosylation-sources/spca2023.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "start_char": 0, "end_char": 1276, "text_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "text_characters": 1276} [mn-gly-spca2023] Cryo-EM structures of human SPCA1a reveal the mechanism of Ca²⁺/Mn²⁺ transport into the Golgi apparatus. (2023). https://pubmed.ncbi.nlm.nih.gov/36867705/ DOI: 10.1126/sciadv.add9742

cross_nutrient

Secretory pathway calcium/manganese ATPase 1 (parent_protein); Manganese(II) ion (transported_ion); Adenosine triphosphate (energy_substrate); Golgi apparatus (destination)

evidence_span

{"source_cache": "artifacts/manganese-glycosylation-sources/spca2023.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "start_char": 0, "end_char": 1276, "text_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "text_characters": 1276}

experimental_model

Cryo-EM of purified human SPCA1a with ATP and divalent ions

exposure

ATP/Ca2+, ATP/Mn2+ and phosphorylated metal-free structural states.

limitations

Structural states explain the transport cycle but do not supply a dietary requirement or prove that calcium supplementation impairs manganese delivery.

nutrient_topic

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

organism

Homo sapiens

plain_language

An ATP-powered pump delivers manganese to the Golgi.

primary_references

[mn-gly-spca2023] Cryo-EM structures of human SPCA1a reveal the mechanism of Ca²⁺/Mn²⁺ transport into the Golgi apparatus. (2023). https://pubmed.ncbi.nlm.nih.gov/36867705/ DOI: 10.1126/sciadv.add9742

tissue_or_cell_type

Golgi membrane transport protein

transport_effect

raises Recorded as manganese movement from cytosol into the Golgi lumen.

transport_pool

the Golgi lumen Recorded as manganese movement from cytosol into the Golgi lumen.

Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 698–710

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cryo-EM of purified human SPCA1a with ATP and divalent ions · source_derived_draft · unverified_draft

### mn-gly-spca-manganese Human SPCA1a couples its ATPase cycle to manganese movement from cytosol into the Golgi lumen. Condition category: normal nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: An ATP-powered pump delivers manganese to the Golgi. organism: Homo sapiens tissue_or_cell_type: Golgi membrane transport protein experimental_model: Cryo-EM of purified human SPCA1a with ATP and divalent ions limitations: Structural states explain the transport cycle but do not supply a dietary requirement or prove that calcium supplementation impairs manganese delivery. exposure: ATP/Ca2+, ATP/Mn2+ and phosphorylated metal-free structural states. cross_nutrient: Secretory pathway calcium/manganese ATPase 1 (parent_protein); Manganese(II) ion (transported_ion); Adenosine triphosphate (energy_substrate); Golgi apparatus (destination) evidence_span: {"source_cache": "artifacts/manganese-glycosylation-sources/spca2023.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "start_char": 0, "end_char": 1276, "text_sha256": "06a3eac4cc4e989b9195bdb14847c868ddaa68935a12f2d5c5f50a1a47259fb8", "text_characters": 1276} [mn-gly-spca2023] Cryo-EM structures of human SPCA1a reveal the mechanism of Ca²⁺/Mn²⁺ transport into the Golgi apparatus. (2023). https://pubmed.ncbi.nlm.nih.gov/36867705/ DOI: 10.1126/sciadv.add9742

availability_state

machinery_impairment Imported condition classification; unverified.

cross_nutrient

TMEM165 Golgi cation-homeostasis protein (affected_protein); Golgi apparatus (affected_compartment)

evidence_span

{"source_cache": "artifacts/manganese-glycosylation-sources/potelle2016.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "e1845bfbdbb15370fd1375534464f61aa6e5674cc4129b6f0992d9a022882cc3", "start_char": 0, "end_char": 1190, "text_sha256": "e1845bfbdbb15370fd1375534464f61aa6e5674cc4129b6f0992d9a022882cc3", "text_characters": 1190}

experimental_model

TMEM165-depleted mammalian cells and separate yeast Gdt1 loss experiments

exposure

Mn2+ supplementation of depleted cells.

limitations

These records describe the mammalian-cell arm. The indexed abstract does not specify every line, dose or treatment duration; rescue supports a homeostasis role rather than establishing a transport stoichiometry.

nutrient_topic

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

organism

Mammalian cell model; yeast comparison

plain_language

More available manganese could compensate for this Golgi-handling defect in cells.

primary_references

[mn-gly-potelle2016] Glycosylation abnormalities in Gdt1p/TMEM165 deficient cells result from a defect in Golgi manganese homeostasis. (2016). https://pubmed.ncbi.nlm.nih.gov/27008884/ DOI: 10.1093/hmg/ddw026

tissue_or_cell_type

Golgi glycosylation

trigger_kind

machinery_impairment Imported condition classification; unverified.

Manganese: enzyme cofactors, glycosylation, transport and nutrient interactions (2026-09-17) · lines 740–752

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · TMEM165-depleted mammalian cells and separate yeast Gdt1 loss experiments · source_derived_draft · unverified_draft

### mn-gly-tmem165-mn-rescue Manganese supplementation restored glycosylation in the TMEM165-depleted mammalian-cell experiments. Condition category: machinery_impairment nutrient_topic: Manganese research collection; topical membership is not evidence of a direct dietary effect. plain_language: More available manganese could compensate for this Golgi-handling defect in cells. organism: Mammalian cell model; yeast comparison tissue_or_cell_type: Golgi glycosylation experimental_model: TMEM165-depleted mammalian cells and separate yeast Gdt1 loss experiments limitations: These records describe the mammalian-cell arm. The indexed abstract does not specify every line, dose or treatment duration; rescue supports a homeostasis role rather than establishing a transport stoichiometry. exposure: Mn2+ supplementation of depleted cells. cross_nutrient: TMEM165 Golgi cation-homeostasis protein (affected_protein); Golgi apparatus (affected_compartment) evidence_span: {"source_cache": "artifacts/manganese-glycosylation-sources/potelle2016.abstract.txt", "locator": "Indexed primary abstract", "file_sha256": "e1845bfbdbb15370fd1375534464f61aa6e5674cc4129b6f0992d9a022882cc3", "start_char": 0, "end_char": 1190, "text_sha256": "e1845bfbdbb15370fd1375534464f61aa6e5674cc4129b6f0992d9a022882cc3", "text_characters": 1190} [mn-gly-potelle2016] Glycosylation abnormalities in Gdt1p/TMEM165 deficient cells result from a defect in Golgi manganese homeostasis. (2016). https://pubmed.ncbi.nlm.nih.gov/27008884/ DOI: 10.1093/hmg/ddw026

evidence_span

{"source_cache": "artifacts/mebendazole-research/1117352.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7cf1916636fe33e5b6ce6c22d84d2550adfd392b30b1b940f4c794b3069066f", "start_char": 0, "end_char": 1554, "text_sha256": "e7cf1916636fe33e5b6ce6c22d84d2550adfd392b30b1b940f4c794b3069066f"}

experimental_model

Ultrastructural and cytochemical examination of Ascaris suum intestine from pigs fed medicated food

exposure

Mebendazole at 30 parts per million in pig feed, with parasites collected 6, 9, 15 and 24 hours after feeding began

limitations

The earliest mechanistic record here and still the clearest picture of the consequence. It predates the tubulin work and describes exactly what blocking microtubule-based transport would produce.

nutrient_topic

Mebendazole research collection; topical membership is not evidence of a direct clinical effect, and mebendazole is recorded separately from albendazole, from the benzimidazole class and from its own crystal forms. · Mebendazole

organism

Nematode

plain_language

The cargo piles up where it is made and never arrives where it is needed.

primary_references

[mbz-p1117352] Ultrastructural changes in Ascaris suum intestine after mebendazole treatment in vivo. (1975). https://pubmed.ncbi.nlm.nih.gov/1117352/ DOI: 10.2307/3279120

tissue_or_cell_type

Ascaris suum intestine

Mebendazole: the tubulin it binds, why that is selective, the crystal form that decides whether any of it works, and the off-target that became an oncology programme (2026-09-22) · lines 186–197

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ultrastructural and cytochemical examination of Ascaris suum intestine from pigs fed medicated food · source_derived_draft · unverified_draft

### mbz-secretory-transport-fails After 6 and 9 hours of treatment the characteristic changes in Ascaris suum intestinal cells were absence of secretory granules in the terminal web, accumulation of secretory granules in the Golgi region, formation of autophagic vacuoles in the apical cell part, and loss of glycogen, and cytochemistry revealed that the accumulated granules in the Golgi area contained glycoproteins or polysaccharides. Condition category: normal nutrient_topic: Mebendazole research collection; topical membership is not evidence of a direct clinical effect, and mebendazole is recorded separately from albendazole, from the benzimidazole class and from its own crystal forms. plain_language: The cargo piles up where it is made and never arrives where it is needed. organism: Nematode tissue_or_cell_type: Ascaris suum intestine experimental_model: Ultrastructural and cytochemical examination of Ascaris suum intestine from pigs fed medicated food limitations: The earliest mechanistic record here and still the clearest picture of the consequence. It predates the tubulin work and describes exactly what blocking microtubule-based transport would produce. exposure: Mebendazole at 30 parts per million in pig feed, with parasites collected 6, 9, 15 and 24 hours after feeding began evidence_span: {"source_cache": "artifacts/mebendazole-research/1117352.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e7cf1916636fe33e5b6ce6c22d84d2550adfd392b30b1b940f4c794b3069066f", "start_char": 0, "end_char": 1554, "text_sha256": "e7cf1916636fe33e5b6ce6c22d84d2550adfd392b30b1b940f4c794b3069066f"} [mbz-p1117352] Ultrastructural changes in Ascaris suum intestine after mebendazole treatment in vivo. (1975). https://pubmed.ncbi.nlm.nih.gov/1117352/ DOI: 10.2307/3279120