Chemicals and Drugs

Nogo Proteins

Myelin proteins that are expressed as three isoforms: Nogo-A, Nogo-B, and Nogo-C. These share a C-terminal reticulon homology domain (RHD), consisting of two hydrophobic membrane domains flanking a 66 amino acid (Nogo-66) hydrophilic region. A long transmembrane region allows conformations that either span the entire membrane or fold into a hairpin conformation. Nogo inhibits NEURITE outgrowth and modulates wiring and the restriction of SYNAPTIC PLASTICITY in the adult central nervous system. It also regulates neurite fasciculation, branching, and extension in the developing nervous system.

National Library of MedicineMedical Subject Headings2026

Structured Summary

Abstract

Myelin proteins that are expressed as three isoforms: Nogo-A, Nogo-B, and Nogo-C. These share a C-terminal reticulon homology domain (RHD), consisting of two hydrophobic membrane domains flanking a 66 amino acid (Nogo-66) hydrophilic region. A long transmembrane region allows conformations that either span the entire membrane or fold into a hairpin conformation. Nogo inhibits NEURITE outgrowth and modulates wiring and the restriction of SYNAPTIC PLASTICITY in the adult central nervous system. It also regulates neurite fasciculation, branching, and extension in the developing nervous system.

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Classification

Broader headings

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MeSH Record

Synonyms

23 entry terms
  • Nogo Protein
  • Reticulon-4 Protein
  • Reticulon 4 Protein
  • NI-220 Protein
  • NI-250 Protein
  • NI-35 Protein
  • NI-35-250
  • Neurite Growth Inhibitor 35-350
  • Nogo-66 Protein
  • Nogo-A Protein
  • Nogo-B Protein
  • Nogo-C Protein
  • Reticulon 4-B Protein
  • NI 220 Protein
  • NI 250 Protein
  • NI 35 250
  • NI 35 Protein
  • Neurite Growth Inhibitor 35 350
  • Nogo 66 Protein
  • Nogo A Protein
  • Nogo B Protein
  • Nogo C Protein
  • Reticulon 4 B Protein

MeSH Record

Aspects Covered

30 allowable subheadings

Indexed with the subheadings administration & dosage, adverse effects, agonists, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.

MeSH Record

History Note

2017 (2000)

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Tree Numbers

AMA Style

References

  1. National Library of Medicine. Nogo Proteins. Medical Subject Headings (MeSH). 2026. Unique ID D000070798. http://id.nlm.nih.gov/mesh/2026/D000070798
  2. Nogo Proteins. In: Wikidata. https://www.wikidata.org/wiki/Q76626642