Component
Drosophila SARM1 ARM domain residues 307–678
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 acts on it
NAD+ bound the same Drosophila SARM1 ARM-domain regulatory site with approximately 54.2 micromolar dissociation constant; competition assays supported opposing occupancy by NAD+ and NMN.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Drosophila-domain ITC and NMR competition.
- limitations
- Species/domain-specific affinity; separate from catalytic-site kinetics.
- nutrient_topic
- NAD+ collection; molecular form, preparation, species, exposure and manipulation remain explicit. · NAD+
- plain_language
- NAD can help restrain the switch at a regulatory site while also being its substrate.
- primary_references
- SARM1 is a metabolic sensor activated by an increased NMN/NAD+ ratio to trigger axon degeneration. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33657413/ · DOI 10.1016/j.neuron.2021.02.009
NAD+: compartmental supply, consumption and cross-nutrient mechanisms (2026-09-19) · lines 92–98
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Drosophila-domain ITC and NMR competition. · source_derived_draft · unverified_draft
## nad-plus-sarm-nad-binding NAD can help restrain the switch at a regulatory site while also being its substrate. NAD+ bound the same Drosophila SARM1 ARM-domain regulatory site with approximately 54.2 micromolar dissociation constant; competition assays supported opposing occupancy by NAD+ and NMN. Model: Drosophila-domain ITC and NMR competition. Limitations: Species/domain-specific affinity; separate from catalytic-site kinetics. Evidence access: Primary full text SARM1 is a metabolic sensor activated by an increased NMN/NAD+ ratio to trigger axon degeneration. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33657413/ · DOI 10.1016/j.neuron.2021.02.009
Complete structured claim and evidenceNMN bound the purified Drosophila SARM1 ARM domain at approximately 6.39 micromolar dissociation constant, with one ligand per domain.
Experimental context and source evidence
- evidence_access
- Primary full text
- experimental_model
- Drosophila-domain ITC and structural experiments.
- limitations
- The binding affinity is for a fly domain, not a full-length human protein or a human toxicity threshold.
- nutrient_topic
- NAD+ collection; molecular form, preparation, species, exposure and manipulation remain explicit. · NAD+
- plain_language
- The activating precursor has a directly measured binding site.
- primary_references
- SARM1 is a metabolic sensor activated by an increased NMN/NAD+ ratio to trigger axon degeneration. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33657413/ · DOI 10.1016/j.neuron.2021.02.009
NAD+: compartmental supply, consumption and cross-nutrient mechanisms (2026-09-19) · lines 84–90
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Drosophila-domain ITC and structural experiments. · source_derived_draft · unverified_draft
## nad-plus-sarm-nmn-binding The activating precursor has a directly measured binding site. NMN bound the purified Drosophila SARM1 ARM domain at approximately 6.39 micromolar dissociation constant, with one ligand per domain. Model: Drosophila-domain ITC and structural experiments. Limitations: The binding affinity is for a fly domain, not a full-length human protein or a human toxicity threshold. Evidence access: Primary full text SARM1 is a metabolic sensor activated by an increased NMN/NAD+ ratio to trigger axon degeneration. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33657413/ · DOI 10.1016/j.neuron.2021.02.009
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.