Component
Human cytosolic histidyl-tRNA synthetase / HARS1
Context-specific entity; species, compartment and exposure are stated on each claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
HARS1 ligates histidine to its cognate tRNA for protein synthesis.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Established enzymatic role in a primary HARS variant study.
- limitations
- Background chemistry rather than a new dietary intervention.
- nutrient_topic
- L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
- plain_language
- A charging enzyme connects free histidine to the protein-building machinery.
- primary_references
- A loss-of-function variant in the human histidyl-tRNA synthetase (HARS) gene is neurotoxic in vivo. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22930593/ · DOI 10.1002/humu.22210
L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 458–464
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Established enzymatic role in a primary HARS variant study. · source_derived_draft · unverified_draft
## histidine-hars-charging A charging enzyme connects free histidine to the protein-building machinery. HARS1 ligates histidine to its cognate tRNA for protein synthesis. Model: Established enzymatic role in a primary HARS variant study. Limitations: Background chemistry rather than a new dietary intervention. Evidence access: Primary full text A loss-of-function variant in the human histidyl-tRNA synthetase (HARS) gene is neurotoxic in vivo. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22930593/ · DOI 10.1002/humu.22210
Complete structured claim and evidence
What acts on it
HARS1 Arg137Gln identified in a neuropathy screen showed loss of function in yeast complementation and neuronal toxicity in a worm expression model.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- evidence_access
- Primary full text
- experimental_model
- Human variant discovery, orthologous yeast complementation and C. elegans functional assays.
- limitations
- The variant also occurred in additional sequenced people; functional findings do not establish penetrance or an effective histidine treatment.
- nutrient_topic
- L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
- plain_language
- A defective histidine-using enzyme can cause cellular problems that substrate alone has not been shown to fix.
- primary_references
- A loss-of-function variant in the human histidyl-tRNA synthetase (HARS) gene is neurotoxic in vivo. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22930593/ · DOI 10.1002/humu.22210
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 466–472
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human variant discovery, orthologous yeast complementation and C. elegans functional assays. · source_derived_draft · unverified_draft
## histidine-hars-variant A defective histidine-using enzyme can cause cellular problems that substrate alone has not been shown to fix. HARS1 Arg137Gln identified in a neuropathy screen showed loss of function in yeast complementation and neuronal toxicity in a worm expression model. Model: Human variant discovery, orthologous yeast complementation and C. elegans functional assays. Limitations: The variant also occurred in additional sequenced people; functional findings do not establish penetrance or an effective histidine treatment. Evidence access: Primary full text A loss-of-function variant in the human histidyl-tRNA synthetase (HARS) gene is neurotoxic in vivo. · 2013 · https://pubmed.ncbi.nlm.nih.gov/22930593/ · DOI 10.1002/humu.22210
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.