関: GAP-43、GAP-43 protein

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/25 00:29:10」(JST)

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Growth Associated Protein 43 also known as GAP43 is a protein that in humans is encoded by the GAP43 gene.^[1]

GAP43 has been termed a 'growth' or 'plasticity' protein because it is expressed at high levels in neuronal growth cones during development, during axonal regeneration and is phosphorylated after long-term potentiation (LTP) and after learning (reference needed). This protein is considered a crucial component of the axon and presynaptic terminal, its null mutation leading to death within days after birth due to axon pathfinding defects.^[2]

Synonyms

GAP43 is also referred to as:

protein F1
neuromodulin
neural phosphoprotein B-50
axonal membrane protein GAP-43
calmodulin-binding protein P-57
nerve growth-related peptide GAP43
neuron growth-associated protein 43

Function

GAP43, is a nervous tissue-specific cytoplasmic protein that can be attached to the membrane via a dual palmitoylation sequence on cysteines 3 and 4. This sequence targets GAP43 to lipid rafts. It is a major protein kinase C (PKC) substrate and is considered to play a key role in neurite formation, regeneration, and plasticity.^[3]^[4] The role of GAP-43 in CNS development is not limited to effects on axons: It is also a component of the centrosome, and differentiating neurons that do not express GAP-43 show mislocalization of the centrosome and mitotic spindles, particularly in neurogenic cell divisions. As a consequence, in the cerebellum, the neuronal precursor pool fails to expand normally and the cerebellum is significantly smaller.

Several different laboratories studying the same protein, now called GAP43, initially used different names. It was designated F1, then B-50, then GAP43, pp46, and finally neuromodulin, each name reflecting a different function of the same molecule.^[5] F1 was localized to synapses, and was increased in its phosphorylation one day after learning. However, F1 was not cAMP kinase dependent. B-50 was regulated by the pituitary peptide ACTH and was associated with grooming behavior. In the case of GAP-43, it was designated as a growth-associated protein because its synthesis was upregulated during axonal regeneration. Pp46 was concentrated in neuronal growth cones and was thus postulated to play an important role in brain development. In the case of neuromodulin, it was shown to bind calmodulin avidly.

GAP43, the consensus choice for its designation,^[5] is a nervous system-specific protein that is attached to the membrane via a dual palmitoylation sequence on cysteines 3 and 4, though it can exist in the non-bound form in the cytoplasm. This dual sequence enables the association of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] or PIP2, with actin, facilitating the latter’s polymerization thereby regulating neuronal structure. This can occur within a lipid raft so as to compartmentalize and localize motility of filopodia in growth cones in developing brains, and could also remodel presynaptic terminals in adults in an activity-dependent manner. GAP-43 is also a protein kinase C (PKC) substrate. Phosphorylation of serine-41 on GAP-43 by PKC regulates neurite formation, regeneration, and synaptic plasticity.^[3]

Because of the association and potential binding of GAP43 with a number of different molecules, including PKC, PIP2, actin, calmodulin, spectrin, palmitate, synaptophysin, amyloid and tau protein, it may be useful to think of GAP43 as an adaptor protein situated within the terminal in a supramolecular complex regulating presynaptic terminal functions, particularly bidirectional communication with the postsynaptic process. Its important role in memory and information storage is executed through its cell biological mechanisms of phosphorylation, palmitoylation, protein-protein interaction and structural remodeling via actin polymerization.

Clinical significance

Humans with a deletion in one allele of the GAP43 gene fail to form telencephalic commissures and are mentally retarded,.^[6]^[7]

Model organisms

*Gap43* knockout mouse phenotype
Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Abnormal
Haematology	Normal
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal^[8]
Citrobacter infection	Normal^[9]
All tests and analysis from^[10]^[11]

Model organisms have been used in the study of GAP43 function. A conditional knockout mouse line, called Gap43^{tm1a(EUCOMM)Wtsi}^[12]^[13] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.^[14]^[15]^[16] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[10]^[17] Twenty five tests were carried out on mutant mice and two significant abnormalities were observed. No homozygous mutant mice survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and increased IgG1 levels were observed in these animals.^[10]

Studies on another homozygous GAP43 knockout mouse line found it to be lethal days after birth because it plays a critical role in the development of the mammalian CNS.^[18] Telencephalic commissures fail to form,^[19] thalamocortical afferents are mistargeted, especially in somatosensory, particularly barrel, cortex.^[18] GAP43 is not only important for axon targeting during development but it has been shown to be important also for the maintenance of the structure and dynamics of axonal fibres and of their synaptic terminals in wild-type rodents both during normal conditions and during lesion-induced axonal sprouting.^[20]^[21]^[22] The cerebellum is also affected.^[23] GAP43 is also haploinsufficient for the cortical phenotypes and the severity of the axon targeting phenotype is directly related to the extent to which the affected axons are phosphorylated by PKC, suggesting that axons require a functional threshold of phosphorylated GAP43 for targeting to occur normally.^[19] Moreover, elevation above this threshold in GAP43 mice can enhance learning and also facilitate a physiological model of learning, long-term potentiation (LTP).^[24] However, further enrichment beyond a certain level can be devastating to cognitive functions.

References

^ Kosik KS, Orecchio LD, Bruns GA, Benowitz LI, MacDonald GP, Cox DR, Neve RL (Apr 1988). "Human GAP-43: its deduced amino acid sequence and chromosomal localization in mouse and human". Neuron 1 (2): 127–32. doi:10.1016/0896-6273(88)90196-1. PMID 3272162.
^ "Entrez Gene: GAP43 growth associated protein 43".
^ ^a ^b Benowitz LI, Routtenberg A (Feb 1997). "GAP-43: an intrinsic determinant of neuronal development and plasticity". Trends in Neurosciences 20 (2): 84–91. doi:10.1016/S0166-2236(96)10072-2. PMID 9023877.
^ Aarts LH, Schotman P, Verhaagen J, Schrama LH, Gispen WH (1998). "The role of the neural growth associated protein B-50/GAP-43 in morphogenesis". Advances in Experimental Medicine and Biology 446: 85–106. doi:10.1007/978-1-4615-4869-0_6. PMID 10079839.
^ ^a ^b Benowitz LI, Routtenberg A (1987). "A membrane phosphoprotein associated with neural development, axonal regeneration, phospholipid metabolism, and synaptic plasticity". Trends in Neurosciences 10 (12): 527–532. doi:10.1016/0166-2236(87)90135-4.
^ Genuardi M, Calvieri F, Tozzi C, Coslovi R, Neri G (Oct 1994). "A new case of interstitial deletion of chromosome 3q, del(3q)(q13.12q21.3), with agenesis of the corpus callosum". Clinical Dysmorphology 3 (4): 292–6. doi:10.1097/00019605-199410000-00003. PMID 7894733.
^ Mackie Ogilvie C, Rooney SC, Hodgson SV, Berry AC (Mar 1998). "Deletion of chromosome 3q proximal region gives rise to a variable phenotype". Clinical Genetics 53 (3): 220–2. doi:10.1111/j.1399-0004.1998.tb02681.x. PMID 9630079.
^ "Salmonella infection data for Gap43". Wellcome Trust Sanger Institute.
^ "Citrobacter infection data for Gap43". Wellcome Trust Sanger Institute.
^ ^a ^b ^c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
^ "International Knockout Mouse Consortium".
^ "Mouse Genome Informatics".
^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
^ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
^ ^a ^b Strittmatter SM, Fankhauser C, Huang PL, Mashimo H, Fishman MC (Feb 1995). "Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43". Cell 80 (3): 445–52. doi:10.1016/0092-8674(95)90495-6. PMID 7859286.
^ ^a ^b Shen Y, Mani S, Donovan SL, Schwob JE, Meiri KF (Jan 2002). "Growth-associated protein-43 is required for commissural axon guidance in the developing vertebrate nervous system". The Journal of Neuroscience 22 (1): 239–47. PMID 11756507.
^ Grasselli G, Mandolesi G, Strata P, Cesare P (June 2011). "Impaired sprouting and axonal atrophy in cerebellar climbing fibres following in vivo silencing of the growth-associated protein GAP-43". PLOS ONE 6 (6): e20791. doi:10.1371/journal.pone.0020791. PMC 3112224. PMID 21695168.
^ Grasselli G, Strata P (February 2013). "Structural plasticity of climbing fibers and the growth-associated protein GAP-43". Frontiers in Neural Circuits 7 (25): 25. doi:10.3389/fncir.2013.00025. PMC 3578352. PMID 23441024.
^ Allegra Mascaro AL, Cesare P, Sacconi L, Grasselli G, Mandolesi G, Maco B, Knott GW, Huang L, De Paola V, Strata P, Pavone FS (Jun 2013). "In vivo single branch axotomy induces GAP-43-dependent sprouting and synaptic remodeling in cerebellar cortex". Proceedings of the National Academy of Sciences of the United States of America 110 (26): 10824–9. doi:10.1073/pnas.1219256110. PMID 23754371.
^ Shen Y, Mishra R, Mani S, Meiri KF (2008). "Both cell-autonomous and cell non-autonomous functions of GAP-43 are required for normal patterning of the cerebellum in vivo". Cerebellum 7 (3): 451–66. doi:10.1007/s12311-008-0049-5. PMID 18777197.
^ Routtenberg A, Cantallops I, Zaffuto S, Serrano P, Namgung U (Jun 2000). "Enhanced learning after genetic overexpression of a brain growth protein". Proceedings of the National Academy of Sciences of the United States of America 97 (13): 7657–62. doi:10.1073/pnas.97.13.7657. PMC 16601. PMID 10861025.

External links

Gap-43 protein at the US National Library of Medicine Medical Subject Headings (MeSH)
ihop-net, Growth associated protein 43
NCBI

English Journal

Effects of neural stem cells on synaptic proteins and memory in a mouse model of Alzheimer's disease.

Zhang W, Wang GM, Wang PJ, Zhang Q, Sha SH.Author information Department of Medical Imaging, Tongji Hospital, Medical School of Tongji University, Shanghai, China.AbstractTransplanting neural stem cells (NSC) to the damaged brain has been regarded as a potential treatment for neurodegenerative diseases such as Alzheimer's disease (AD), a condition characterized by memory loss. We hypothesized that transplantation of NSC into the hippocampal regions of APP + PS1 transgenic (Tg) mice, a well-established model of AD, would enhance the expression of synaptic proteins, which may be helpful for improving cognitive function. Our results showed that NSC transplantation significantly improved spatial learning and memory function in Tg mice. The results obtained by real-time RT-PCR, immunofluorescence, and Western blot analyses demonstrated that the expression of synaptophysin (SYN) and that of growth-associated protein-43 (GAP-43) in Tg-NSC mice, 8 weeks after transplantation, were significantly improved compared with what was observed in Tg-Veh (control) mice. This finding was confirmed by the increase in the number of synapses in Tg-NSC mice as observed via electron microscopy. Our results suggest that NSC-induced changes can recover memory loss in APP + PS1 transgenic mice, possibly by establishing new neural circuits resulting from the engrafted NSC. © 2013 Wiley Periodicals, Inc.
Journal of neuroscience research.J Neurosci Res.2014 Feb;92(2):185-94. doi: 10.1002/jnr.23299. Epub 2013 Nov 21.
Transplanting neural stem cells (NSC) to the damaged brain has been regarded as a potential treatment for neurodegenerative diseases such as Alzheimer's disease (AD), a condition characterized by memory loss. We hypothesized that transplantation of NSC into the hippocampal regions of APP + PS1 t
PMID 24265160

Neuroprotective effect of chondroitinase ABC on primary and secondary brain injury after stroke in hypertensive rats.

Chen XR1, Liao SJ1, Ye LX1, Gong Q2, Ding Q1, Zeng JS1, Yu J3.Author information 1Department of Neurology, Guangdong Key Laboratory for Diagnosis and Treatment of Major Neurological Diseases, National Key Clinical Department, National Key Discipline, the First Affiliated Hospital of Sun Yat-sen University, Guangzhou 510080, China.2Department of Neurology, the Second People's Hospital of Guangdong Province, Guangzhou 510000, China.3Department of Neurology, Guangdong Key Laboratory for Diagnosis and Treatment of Major Neurological Diseases, National Key Clinical Department, National Key Discipline, the First Affiliated Hospital of Sun Yat-sen University, Guangzhou 510080, China. Electronic address: yujian21cn@163.com.AbstractFocal cerebral infarction causes secondary damage in the ipsilateral ventroposterior thalamic nucleus (VPN). Chondroitin sulfate proteoglycans (CSPGs) are a family of putative inhibitory components, and its degradation by chondroitinase ABC (ChABC) promotes post-injury neurogenesis. This study investigated the role of ChABC in the primary and secondary injury post stroke in hypertension. Renovascular hypertensive Sprague-Dawley rats underwent middle cerebral artery occlusion (MCAO), and were subjected to continuous intra-infarct infusion of ChABC (0.12U/d for 7 days) 24h later. Neurological function was evaluated by a modified neurologic severity score. Neurons were counted in the peri-infarct region and the ipsilateral VPN 8 and 14 days after MCAO by Nissl staining and NeuN labeling. The expressions of CSPGs, growth-associated protein-43 (GAP-43) and synaptophysin (SYN) were detected with immunofluorescence or Western blotting. The intra-infarct infusion of ChABC, by degrading accumulated CSPGs, rescued neuronal loss and increased the levels of GAP-43 and SYN in both the ipsilateral cortex and VPN, indicating enhancd neuron survival as well as augmented axonal growth and synaptic plasticity, eventually improving overall neurological function. The study demonstrated that intra-infarct ChABC infusion could salvage the brain from both primary and secondary injury by the intervention on the neuroinhibitory environment post focal cerebral infarction.
Brain research.Brain Res.2014 Jan 16;1543:324-33. doi: 10.1016/j.brainres.2013.12.002. Epub 2013 Dec 8.
Focal cerebral infarction causes secondary damage in the ipsilateral ventroposterior thalamic nucleus (VPN). Chondroitin sulfate proteoglycans (CSPGs) are a family of putative inhibitory components, and its degradation by chondroitinase ABC (ChABC) promotes post-injury neurogenesis. This study inves
PMID 24326094

The expression of vesicular glutamate transporter 3 and vesicular monoamine transporter 2 induced by brain-derived neurotrophic factor in dorsal root ganglion neurons in vitro.

Liu D1, Bi Y2, Liu Z3, Liu H4, Li Z5.Author information 1Department of Anatomy, Shandong University School of Medicine, Jinan 250012, China. Electronic address: cyyzld@gmail.com.2Department of Cardiosurgery, Shandong University Qilu Hospital, Jinan 250012, China. Electronic address: yanwenbi@126.com.3Department of Anatomy, Shandong University School of Medicine, Jinan 250012, China. Electronic address: zhen@sdu.edu.cn.4Department of Rheumatology, Shandong University Qilu Hospital, Jinan 250012, China. Electronic address: huaxiangliu@hotmail.com.5Department of Anatomy, Shandong University School of Medicine, Jinan 250012, China. Electronic address: zli@sdu.edu.cn.AbstractThe vesicular glutamate transporter 3 (VGLUT3) and the vesicular monoamine transporter 2 (VMAT2) are expressed in dorsal root ganglion (DRG) neurons and play an important role in packing the neurotransmitter into synaptic vesicles. Brain-derived neurotrophic factor (BDNF) is one of the most profound known regulators of survival in the developing peripheral nervous system (PNS). Whether BDNF regulates the expression of VGLUT3 and VMAT2 in DRG neurons is still unclear. In the present study, primary cultured rat DRG neurons were used to evaluate the effects of BDNF on VGLUT3 and VMAT2 expression. The signaling pathways of the extracellular signal-regulated protein kinase 1/2 (ERK1/2), the phosphatidylinositol 3-kinase (PI3K)/Akt, and the phospholipase C-gamma (PLC-γ) involved in these effects were also determined. DRG neurons at 48h post-culture were incubated with BDNF and/or ERK1/2 inhibitor PD98059, PI3K inhibitor LY294002, and PLC-γ inhibitor U73122 for an additional 24h. After that, the neurite growth and growth-associated protein 43 (GAP-43) expressions after different doses of BDNF treatment were determined by immunofluorescent labeling. The expression of mRNA and protein of VGLUT3 and VMAT2 in different experimental conditions was assessed by real-time PCR, immunoblotting, and immunofluorescent labeling, respectively. The results showed that BDNF exposure promoted neurite growth and GAP-43 expression in DRG neurons in a dose-dependent manner. BDNF induced VGLUT3 upregulation through activation of PLC-γ signaling pathway. Although BDNF administration did not elevate the levels of VMAT2, the block of the PI3K/Akt or PLC-γ signaling pathways could inhibit VMAT2 expression in DRG neurons in the presence of BDNF. The knockdown of VGLUT3 or VMAT2 gene by siRNA did not affect the BDNF's effects on GAP-43 upregulation and neurite growth. The upregulation of VGLUT3 induced by BDNF might be that BDNF improved neuronal outgrowth status by promoting GAP-43 expression to stimulate neurite elongation. The contribution of distinct VGLUT3 and VMAT2 transporter expression induced by BDNF might be one of the mechanisms that BDNF regulates neuropathic pain. These data imply that BDNF signaling system might be a potential target on modifying distinct transporter-mediated biological effects of primary sensory neurons.
Brain research bulletin.Brain Res Bull.2014 Jan;100:93-106. doi: 10.1016/j.brainresbull.2013.11.007. Epub 2013 Dec 5.
The vesicular glutamate transporter 3 (VGLUT3) and the vesicular monoamine transporter 2 (VMAT2) are expressed in dorsal root ganglion (DRG) neurons and play an important role in packing the neurotransmitter into synaptic vesicles. Brain-derived neurotrophic factor (BDNF) is one of the most profound
PMID 24316448

Japanese Journal

Quantification of Neuromodulin (GAP-43, B-50) and Synapsin I in Rat Striata

IWATA Shin-ichi,NOMOTO Masahiro,FUKUDA Takeo
日本神経精神薬理学雑誌 = Japanese journal of psychopharmacology 19(5), 261-266, 1999-12-25
NAID 10017039594

Enhanced dopamine release and phosphorylation of synapsin I and neuromodulin in striatal synaptosomes after repeated amphetamine

IWATA S.
J Pharmacol Exp Ther 283, 1445-1452, 1997
NAID 80010114638

Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain

MAEKAWA S.
Biochim. Biophys. Acta 1323, 1-5, 1997
NAID 80009421669

Related Pictures

★リンクテーブル★

リンク元	「GAP-43 protein」「ニューロモジュリン」

「GAP-43 protein」

Growth associated protein 43
Identifiers
Symbols	GAP43 ; B-50; PP46
External IDs	OMIM: 162060 MGI: 95639 HomoloGene: 1545 GeneCards: GAP43 Gene
Gene ontology
Molecular function	• phosphatidylserine binding; • protein binding; • calmodulin binding; • lysophosphatidic acid binding; • phosphatidylinositol phosphate binding;
Cellular component	• cytoplasm; • plasma membrane; • postsynaptic density; • cell junction; • axon; • filopodium membrane; • growth cone membrane; • neuronal postsynaptic density;
Biological process	• protein kinase C-activating G-protein coupled receptor signaling pathway; • response to wounding; • glial cell differentiation; • axon choice point recognition; • regulation of growth; • tissue regeneration; • cell fate commitment; • regulation of filopodium assembly;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

　　[★]

成長関連タンパク質-43

関: GAP-43、growth-associated protein-43、neuromodulin

「ニューロモジュリン」

　　[★]

英: neuromodulin
関: 成長関連タンパク質-43

[pmid3272162-1] Kosik KS, Orecchio LD, Bruns GA, Benowitz LI, MacDonald GP, Cox DR, Neve RL (Apr 1988). "Human GAP-43: its deduced amino acid sequence and chromosomal localization in mouse and human". Neuron 1 (2): 127–32. doi:10.1016/0896-6273(88)90196-1. PMID 3272162.

[entrez-2] "Entrez Gene: GAP43 growth associated protein 43".

[pmid9023877-3] Benowitz LI, Routtenberg A (Feb 1997). "GAP-43: an intrinsic determinant of neuronal development and plasticity". Trends in Neurosciences 20 (2): 84–91. doi:10.1016/S0166-2236(96)10072-2. PMID 9023877.

[pmid10079839-4] Aarts LH, Schotman P, Verhaagen J, Schrama LH, Gispen WH (1998). "The role of the neural growth associated protein B-50/GAP-43 in morphogenesis". Advances in Experimental Medicine and Biology 446: 85–106. doi:10.1007/978-1-4615-4869-0_6. PMID 10079839.

[Benowitz_1987-5] Benowitz LI, Routtenberg A (1987). "A membrane phosphoprotein associated with neural development, axonal regeneration, phospholipid metabolism, and synaptic plasticity". Trends in Neurosciences 10 (12): 527–532. doi:10.1016/0166-2236(87)90135-4.

[PMID7894733-6] Genuardi M, Calvieri F, Tozzi C, Coslovi R, Neri G (Oct 1994). "A new case of interstitial deletion of chromosome 3q, del(3q)(q13.12q21.3), with agenesis of the corpus callosum". Clinical Dysmorphology 3 (4): 292–6. doi:10.1097/00019605-199410000-00003. PMID 7894733.

[PMID9630079-7] Mackie Ogilvie C, Rooney SC, Hodgson SV, Berry AC (Mar 1998). "Deletion of chromosome 3q proximal region gives rise to a variable phenotype". Clinical Genetics 53 (3): 220–2. doi:10.1111/j.1399-0004.1998.tb02681.x. PMID 9630079.

[.27.27Salmonella.27.27_infection-8] "Salmonella infection data for Gap43". Wellcome Trust Sanger Institute.

[.27.27Citrobacter.27.27_infection-9] "Citrobacter infection data for Gap43". Wellcome Trust Sanger Institute.

[mgp_reference-10] Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.

[11] Mouse Resources Portal, Wellcome Trust Sanger Institute.

[allele_ref-12] "International Knockout Mouse Consortium".

[mgi_allele_ref-13] "Mouse Genome Informatics".

[pmid21677750-14] Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.

[mouse_library-15] Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.

[mouse_for_all_reasons-16] Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.

[pmid21722353-17] van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

[pmid7859286-18] Strittmatter SM, Fankhauser C, Huang PL, Mashimo H, Fishman MC (Feb 1995). "Neuronal pathfinding is abnormal in mice lacking the neuronal growth cone protein GAP-43". Cell 80 (3): 445–52. doi:10.1016/0092-8674(95)90495-6. PMID 7859286.

[pmid11756507-19] Shen Y, Mani S, Donovan SL, Schwob JE, Meiri KF (Jan 2002). "Growth-associated protein-43 is required for commissural axon guidance in the developing vertebrate nervous system". The Journal of Neuroscience 22 (1): 239–47. PMID 11756507.

[Grasselli_et_al..2C_2011-20] Grasselli G, Mandolesi G, Strata P, Cesare P (June 2011). "Impaired sprouting and axonal atrophy in cerebellar climbing fibres following in vivo silencing of the growth-associated protein GAP-43". PLOS ONE 6 (6): e20791. doi:10.1371/journal.pone.0020791. PMC 3112224. PMID 21695168.

[Grasselli_.26_Strata.2C_2013-21] Grasselli G, Strata P (February 2013). "Structural plasticity of climbing fibers and the growth-associated protein GAP-43". Frontiers in Neural Circuits 7 (25): 25. doi:10.3389/fncir.2013.00025. PMC 3578352. PMID 23441024.

[Allegra_Mascaro_et_al..2C_2013-22] Allegra Mascaro AL, Cesare P, Sacconi L, Grasselli G, Mandolesi G, Maco B, Knott GW, Huang L, De Paola V, Strata P, Pavone FS (Jun 2013). "In vivo single branch axotomy induces GAP-43-dependent sprouting and synaptic remodeling in cerebellar cortex". Proceedings of the National Academy of Sciences of the United States of America 110 (26): 10824–9. doi:10.1073/pnas.1219256110. PMID 23754371.

[pmid18777197-23] Shen Y, Mishra R, Mani S, Meiri KF (2008). "Both cell-autonomous and cell non-autonomous functions of GAP-43 are required for normal patterning of the cerebellum in vivo". Cerebellum 7 (3): 451–66. doi:10.1007/s12311-008-0049-5. PMID 18777197.

[pmid10861025-24] Routtenberg A, Cantallops I, Zaffuto S, Serrano P, Namgung U (Jun 2000). "Enhanced learning after genetic overexpression of a brain growth protein". Proceedings of the National Academy of Sciences of the United States of America 97 (13): 7657–62. doi:10.1073/pnas.97.13.7657. PMC 16601. PMID 10861025.

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案内

neuromodulin