"GAP-43 Protein" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A nervous tissue specific protein which is highly expressed in NEURONS during development and NERVE REGENERATION. It has been implicated in neurite outgrowth, long-term potentiation, SIGNAL TRANSDUCTION, and NEUROTRANSMITTER release. (From Neurotoxicology 1994;15(1):41-7) It is also a substrate of PROTEIN KINASE C.
| Descriptor ID |
D019922
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| MeSH Number(s) |
D12.776.395.550.400 D12.776.543.550.400 D12.776.631.400
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| Concept/Terms |
GAP-43 Protein- GAP-43 Protein
- GAP 43 Protein
- Phosphoprotein B-50
- Phosphoprotein B 50
- GAP-43
- Neuromodulin
- Growth-Associated Protein 43
- Growth Associated Protein 43
- Phosphoprotein pp46
- B-50 Protein
- B 50 Protein
- GAP43 Protein
- Nerve Growth Cone Membrane Protein GAP-43
- Nerve Growth Cone Membrane Protein GAP 43
- Phosphoprotein F1
|
Below are MeSH descriptors whose meaning is more general than "GAP-43 Protein".
Below are MeSH descriptors whose meaning is more specific than "GAP-43 Protein".
This graph shows the total number of publications written about "GAP-43 Protein" by people in this website by year, and whether "GAP-43 Protein" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2005 | 0 | 2 | 2 |
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Below are the most recent publications written about "GAP-43 Protein" by people in Profiles.
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In vivo single branch axotomy induces GAP-43-dependent sprouting and synaptic remodeling in cerebellar cortex. Proc Natl Acad Sci U S A. 2013 Jun 25; 110(26):10824-9.
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Structural plasticity of climbing fibers and the growth-associated protein GAP-43. Front Neural Circuits. 2013; 7:25.
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Impaired sprouting and axonal atrophy in cerebellar climbing fibres following in vivo silencing of the growth-associated protein GAP-43. PLoS One. 2011; 6(6):e20791.
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Neurite extension and in vitro myelination within three-dimensional modified fibrin matrices. J Neurobiol. 2005 Apr; 63(1):1-14.
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Cross-talk between Schwann cells and neuroblasts influences the biology of neuroblastoma xenografts. Am J Pathol. 2005 Mar; 166(3):891-900.
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Selective decline in protein F1 phosphorylation in hippocampus of senescent rats. Neurobiol Aging. 1988 Jul-Aug; 9(4):393-8.
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Protein F1 and protein kinase C may regulate the persistence, not the initiation, of synaptic potentiation in the hippocampus. Adv Exp Med Biol. 1987; 221:313-30.
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Direct relation of long-term synaptic potentiation to phosphorylation of membrane protein F1, a substrate for membrane protein kinase C. Brain Res. 1986 Dec 10; 399(2):205-11.
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A selective increase in phosporylation of protein F1, a protein kinase C substrate, directly related to three day growth of long term synaptic enhancement. Brain Res. 1985 Sep 16; 343(1):137-43.