Cited by 150Nerve injury and regenerationAxon Guidance and Neuronal SignalingNeurogenesis and neuroplasticity mechanisms

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Cloning of human GAP 43: Growth association and ischemic resurgence

Ng, Shi-Chung, de la Monte, Suzanne M., Conboy, Gary L., Karns, Larry R., Fishman, Mark C.·1988·Neuron

DOI 10.1016/0896-6273(88)90197-3

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Abstract

GAP-43 is a growth cone protein expressed in neurons especially during periods of axonal elongation. Poor repair in the adult mammalian CNS has been ascribed to restraints upon its expression. We have cloned human GAP-43 cDNA to investigate its potential involvement in neurological illness. Analysis of postmortem human brain tissue disclosed uniformly high expression of GAP-43 throughout the neonatal brain, whereas in the adult brain high levels of GAP-43 persist only in discrete regions. However, in the wake of ischemic injury in the adult brain, regions normally low in GAP-43 reexpress it at high levels, suggesting a role for GAP-43 in remodeling and repair of mature CNS neurons.

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DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
Feinberg, A. P., & Vogelstein, B. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90418-9 · Cited by 24,512
Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
Chirgwin, J. M., Przybyla, A., MacDonald, R. J., & Rutter, W. J. (1979) · Biochemistry · doi:10.1021/bi00591a005 · Cited by 21,460
Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
Melton, D. A., Krieg, P. A., Rebagliati, M. R., Maniatis, T., Zinn, K., & Green, M. R. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.18.7035 · Cited by 6,324
A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
Shaw, G. D., & Kamen, R. (1986) · Cell · doi:10.1016/0092-8674(86)90341-7 · Cited by 3,946
Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information
Zuker, M., & Stiegler, P. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.1.133 · Cited by 3,604
Degeneration and Regeneration of the Nervous System.
(1929) · JAMA · doi:10.1001/jama.1929.02710220063037 · Cited by 2,908
Pain and Its Effects in the Human Neonate and Fetus
Anand, K. J. S., & Hickey, P. R. (1987) · New England Journal of Medicine · doi:10.1056/nejm198711193172105 · Cited by 1,715
Greenfield's Neuropathology
Lantos, P. L. (1985) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.48.5.496 · Cited by 1,156
The long and the short of long–term memory—a molecular framework
Goelet, P., Castellucci, V. F., Schacher, S., & Kandel, E. R. (1986) · Nature · doi:10.1038/322419a0 · Cited by 1,034

Show all 41 references

Sorted by citations

Plasticity during stroke recovery: from synapse to behaviour
Murphy, T. H., & Corbett, D. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2735 · Cited by 1,938
Brain–computer interfaces in neurological rehabilitation
Daly, J. J., & Wolpaw, J. R. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70223-0 · Cited by 1,149
Axonal Growth-Associated Proteins
Skene, J. H. P. (1989) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.12.030189.001015 · Cited by 1,145
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Stroemer, R. P., Kent, T. A., & Hulsebosch, C. E. (1995) · Stroke · doi:10.1161/01.str.26.11.2135 · Cited by 514
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter, S. M., Valenzuela, D., Kennedy, T. E., Neer, E. J., & Fishman, M. C. (1990) · Nature · doi:10.1038/344836a0 · Cited by 420
Self-citation
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Carmichael, S. T. (2003) · The Neuroscientist · doi:10.1177/1073858402239592 · Cited by 378
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Nudo, R. J. (2006) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2006.10.004 · Cited by 332
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Doster, S. K., Lozano, A. M., Aguayo, A. J., & Willard, M. B. (1991) · Neuron · doi:10.1016/0896-6273(91)90066-9 · Cited by 315
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Oestreicher, A. B., Graan, P. N. E. D., Gispen, W. H., Verhaagen, J., & Schrama, L. H. (1997) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00043-9 · Cited by 291
Microstructural status of ipsilesional and contralesional corticospinal tract correlates with motor skill in chronic stroke patients
Schaechter, J. D., Fricker, Z. P., Perdue, K. L., Helmer, K. G., Vangel, M. G., Greve, D. N., & Makris, N. (2009) · Human Brain Mapping · doi:10.1002/hbm.20770 · Cited by 296
Patterns of aberrant sprouting in alzheimer's disease
Masliah, E., Mallory, M. E., Hansen, L. A., Alford, M. F., Albright, T., DeTeresa, R. M., Terry, R. D., Baudier, J., & Saitoh, T. (1991) · Neuron · doi:10.1016/0896-6273(91)90170-5 · Cited by 243
Regulation of free calmodulin levels by neuromodulin: neuron growth and regeneration
Liu, Y., & Storm, D. R. (1990) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(90)90195-e · Cited by 232
Expression of the potent vasoconstrictor endothelin in the human central nervous system.
Lee, M. E., de la Monte, S. M., Ng, S., Bloch, K. D., & Quertermous, T. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114677 · Cited by 228
Self-citation
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Liu, J. (1996) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(95)03706-3 · Cited by 225
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Hoffman, P. N. (1989) · Journal of Neuroscience · doi:10.1523/jneurosci.09-03-00893.1989 · Cited by 226
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Zuber, M. X., Goodman, D. W., Karns, L. R., & Fishman, M. C. (1989) · Science · doi:10.1126/science.2658062 · Cited by 218
Self-citation
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Gerendasy, D. D., & Sutcliffe, J. G. (1997) · Molecular Neurobiology · doi:10.1007/bf02740632 · Cited by 206
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Simon, R. P., Cho, H., Gwinn, R. P., & Lowenstein, D. H. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-03-00881.1991 · Cited by 204
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Mukaetova‐Ladinska, E. B., García‐Sierra, F., Hurt, J., Gertz, H.-J., Xuereb, J. H., Hills, R., Brayne, C., Huppert, F. A., Paykel, E. S., McGee, M. A., et al. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64573-7 · Cited by 189
GAP-43 gene expression during development: persistence in a distinctive set of neurons in the mature central nervous system
de la Monte, S. M., Federoff, H. J., Ng, S., Grabczyk, E., & Fishman, M. C. (1989) · Developmental Brain Research · doi:10.1016/0165-3806(89)90279-4 · Cited by 187
Self-citation
GAP‐43 as a plasticity protein in neuronal form and repair
Strittmatter, S. M., Vartanian, T. K., & Fishman, M. C. (1992) · Journal of Neurobiology · doi:10.1002/neu.480230506 · Cited by 185
Self-citation
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Li, S., Nie, E. H., Yin, Y., Benowitz, L. I., Tung, S., Vinters, H. V., Bahjat, F. R., Stenzel-Poore, M. P., Kawaguchi, R., Coppola, G., et al. (2015) · Nature Neuroscience · doi:10.1038/nn.4146 · Cited by 181
“In humans, the initial cloning studies of GAP43, the paradigmatic neuronal growth cone marker, showed that it is induced in peri-infarct cortex after stroke 39 and increases cortical thickness in regions of cortical map plasticity during recovery 7 .”
Dual regulation of GAP-43 gene expression by nerve growth factor and glucocorticoids.
Federoff, H. J., Grabczyk, E., & Fishman, M. C. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77633-9 · Cited by 181
Self-citation
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Tetzlaff, W., Zwiers, H., Lederis, K. P., Cassar, L., & Bisby, M. A. (1989) · Journal of Neuroscience · doi:10.1523/jneurosci.09-04-01303.1989 · Cited by 170
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Dani, J. W., Armstrong, D. M., & Benowitz, L. I. (1991) · Neuroscience · doi:10.1016/0306-4522(91)90190-y · Cited by 166
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Coggins, P. J., & Zwiers, H. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb11398.x · Cited by 163
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Li, S., & Carmichael, S. T. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.03.011 · Cited by 162
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Chamak, B., Morandi, V., & Mallat, M. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490380213 · Cited by 164
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Benowitz, L. I., Perrone-Bizzozero, N., Finklestein, S. P., & Bird, E. D. (1989) · Journal of Neuroscience · doi:10.1523/jneurosci.09-03-00990.1989 · Cited by 153
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Gispen, W. H., Nielander, H. B., Graan, P. N. E. D., Oestreicher, A. B., Schrama, L. H., & Schotman, P. (1991) · Molecular Neurobiology · doi:10.1007/bf02935540 · Cited by 153
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Yankner, B. A., Benowitz, L. I., Villa‐Komaroff, L., & Neve, R. L. (1990) · Molecular Brain Research · doi:10.1016/0169-328x(90)90071-k · Cited by 147
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MiR-17-92 enriched exosomes derived from multipotent mesenchymal stromal cells enhance axon-myelin remodeling and motor electrophysiological recovery after stroke
Xin, H., Liu, Z., Buller, B., Li, Y., Golembieski, W., Gan, X., Wang, F., Lü, M., Ali, M. M., Zhang, Z. G., et al. (2020) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x20950489 · Cited by 132
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Mostany, R., Chowdhury, T. G., Johnston, D. G., Portonovo, S. A., Carmichael, S. T., & Portera‐Cailliau, C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3908-10.2010 · Cited by 127
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Baetge, E. E., & Hammangt, J. P. (1991) · Neuron · doi:10.1016/0896-6273(91)90118-j · Cited by 116
Nerve growth factor-induced changes in the intracellular localization of the protein kinase C substrate B-50 in pheochromocytoma PC12 cells.
Hooff, C. O. M. V., Holthuis, J. C. M., Oestreicher, A. B., Boonstra, J., Graan, P. N. E. D., & Gispen, W. H. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.3.1115 · Cited by 115
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Biffo, S., Verhaagen, J., Schrama, L. H., Schotman, P., Danho, W., & Margolis, F. L. (1990) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1990.tb00440.x · Cited by 111
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Meberg, P. J., & Routtenberg, A. (1991) · Neuroscience · doi:10.1016/0306-4522(91)90284-u · Cited by 104
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Nahmani, M., & Turrigiano, G. G. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.04.029 · Cited by 97
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LaBate, M., & Skene, J. H. P. (1989) · Neuron · doi:10.1016/0896-6273(89)90254-7 · Cited by 96
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Carmichael, S. T. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0408-0 · Cited by 99
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Irwin, N. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.6.1281 · Cited by 86
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Emery, D. L., Royo, N. C., Fischer, I., Saatman, K. E., & McIntosh, T. K. (2003) · Journal of Neurotrauma · doi:10.1089/089771503322686085 · Cited by 82
Olutasidenib (FT-2102) in patients with relapsed or refractory IDH1 -mutant glioma: A multicenter, open-label, phase Ib/II trial
de la Fuente, M. I., Colman, H., Rosenthal, M. A., Tine, B. A. V., Levacic, D., Walbert, T., Gan, H. K., Vieito, M., Milhem, M. M., Lipford, K., et al. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac139 · Cited by 82
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Noh, M., Kwon, H. S., Kwon, M., Nahm, M., Jin, H. K., Bae, J., & Kim, S. H. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00867-4 · Cited by 94
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Callahan, L. M., & Coleman, P. D. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00035-d · Cited by 81
Regulated Binding of the Protein Kinase C Substrate GAP-43 to the V0/C2 Region of Protein Kinase C-δ
Dekker, L. V., & Parker, P. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12747 · Cited by 77
Acute increase in expression of growth associated protein GAP-43 following cortical ischemia in rat
Stroemer, R. P., Kent, T. A., & Hulsebosch, C. E. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90557-2 · Cited by 76
The Synaptic Pathology of Schizophrenia: Is Aberrant Neurodevelopment and Plasticity to Blame?
Eastwood, S. L. (2004) · International review of neurobiology · doi:10.1016/s0074-7742(04)59003-7 · Cited by 75
Neurochemical Correlates of Cortical Plasticity after Unilateral Elevated Intraocular Pressure in a Primate Model of Glaucoma
Lam, D. Y., Kaufman, P. L., Gabelt, B. T., To, E. C., & Matsubara, J. A. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.02-0779 · Cited by 74
Chapter 26 GAP-43 as a marker for structural plasticity in the mature CNS
Benowitz, L. I., Perrone‐Bizzozero, N. I., Neve, R. L., & Rodriguez, W. R. (1990) · Progress in brain research · doi:10.1016/s0079-6123(08)63187-8 · Cited by 72
GAP-43, a protein associated with axon growth, is phosphorylated at three sites in cultured neurons and rat brain.
Spencer, S. A., Schuh, S. M., Liu, W. S., & Willard, M. B. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50388-x · Cited by 71
Hippocampal and cortical growth-associated protein-43 messenger RNA in schizophrenia
Eastwood, S. L., & Harrison, P. J. (1998) · Neuroscience · doi:10.1016/s0306-4522(98)00040-2 · Cited by 70
Buyang Huanwu decoction facilitates neurorehabilitation through an improvement of synaptic plasticity in cerebral ischemic rats
Pan, R., Cai, J., Zhan, L., Guo, Y., Huang, R., Li, X., Zhou, M., Xu, D., Zhan, J., & Chen, H. (2017) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-017-1680-9 · Cited by 70
Aberrant GAP-43 gene expression in Alzheimer's disease.
de la Monte, S. M., Ng, S., & Hsu, D. (1995) · Europe PMC (PubMed Central) · Cited by 66
Self-citation
Gap-43 — What does it do in the growth cone?
Gordon‐Weeks, P. R. (1989) · Trends in Neurosciences · doi:10.1016/0166-2236(89)90073-8 · Cited by 64
Plasticity beyond peri-infarct cortex: Spinal up regulation of structural plasticity, neurotrophins, and inflammatory cytokines during recovery from cortical stroke
Sist, B., Fouad, K., & Winship, I. R. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.11.019 · Cited by 64
In situ hybridization histochemistry and the study of gene expression in the human brain
Harrison, P. J., & PEARSON, R. (1990) · Progress in Neurobiology · doi:10.1016/0301-0082(90)90007-4 · Cited by 61
Post-transcriptional regulation of GAP-43 rnRNA levels during neuronal differentiation and nerve regeneration
Perrone‐Bizzozero, N. I., Neve, R. L., Irwin, N., Lewis, S., Fischer, I., & Benowitz, L. I. (1991) · Molecular and Cellular Neuroscience · doi:10.1016/1044-7431(91)90027-l · Cited by 62
Elevated CSF GAP-43 is associated with accelerated tau accumulation and spread in Alzheimer’s disease
Franzmeier, N., Dehsarvi, A., Steward, A., Biel, D., Dewenter, A., Roemer, S. N., Wagner, F., Groß, M., Brendel, M., Moscoso, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44374-w · Cited by 63
Identification of two promoter regions in the rat B-50/GAP-43 gene
Eggen, B. J. L., Nielander, H. B., Rensen, M. G. A., Schotman, P., Gispen, W. H., & Schrama, L. H. (1994) · Molecular Brain Research · doi:10.1016/0169-328x(94)90229-1 · Cited by 60
The Relationship of GAP‐43 to the Development and Plasticity of Synaptic Connectionsa
Benowitz, L. I., & Perrone‐Bizzozero, N. I. (1991) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1991.tb25914.x · Cited by 59
Distribution of GAP-43 (B50/F1) mRNA in the adult rat brain by in situ hybridization using an alkaline phosphatase labeled probe
Yao, G. L., Kiyama, H., & Tohyama, M. (1993) · Molecular Brain Research · doi:10.1016/0169-328x(93)90168-o · Cited by 58
How is protein kinase C activated in CNS
Huang, K., & Huang, F. L. (1993) · Neurochemistry International · doi:10.1016/0197-0186(93)90037-6 · Cited by 57
An Imperfect Dopaminergic Error Signal Can Drive Temporal-Difference Learning
Potjans, W., Diesmann, M., & Morrison, A. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1001133 · Cited by 56
Alterations in GAP‐43 and Synapsin Immunoreactivity Provide Evidence for Synaptic Reorganization in Adult Cat Dorsal Lateral Geniculate Nucleus following Retinal Lesions
Baekelandt, V., Arckens, L., Annaert, W. G., Eysel, U. T., Orban, G. A., & Vandesande, F. (1994) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1994.tb00987.x · Cited by 53
Transcriptional regulation of neuromodulin (GAP-43) in mouse neuroblastoma clone N1E-115 as evaluated by the RT/PCR method
Robbins, M., & McKinney, M. (1992) · Molecular Brain Research · doi:10.1016/0169-328x(92)90047-f · Cited by 51
GAP-43 in the axons of mammalian CNS neurons regenerating into peripheral nerve grafts
Campbell, G., Anderson, P. N., Turmaine, M., & Lieberman, A. R. (1991) · Experimental Brain Research · doi:10.1007/bf00228507 · Cited by 50
Ultrastructural double localization of B-50/GAP43 and synaptophysin (p38) in the neonatal and adult rat hippocampus
Campagne, M. V. L., Oestreicher, A. B., Henegouwen, P. M. P. V. B. E., & Gispen, W. H. (1990) · Journal of Neurocytology · doi:10.1007/bf01186822 · Cited by 44
Regenerative and other responses to injury in the retinal stump of the optic nerve in adult albino rats: transection of the intracranial optic nerve.
Zeng, B., Anderson, P. N., Campbell, G., & Lieberman, A. R. (1994) · Europe PMC (PubMed Central) · Cited by 41
Chronic atropine administration up-regulates rat cortical muscarinic m1 receptor mRNA molecules: assessment with the RT/PCR
McKinney, M., & Robbins, M. (1992) · Molecular Brain Research · doi:10.1016/0169-328x(92)90066-k · Cited by 42
Reduced GAP-43 message levels are associated with increased neurofibrillary tangle density in the frontal association cortex (area 9) in Alzheimer's disease
Coleman, P. D., Kazee, A. M., Lapham, L. W., Eskin, T. A., & Rogers, K. E. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90085-c · Cited by 41
Chicken growth-associated protein (GAP)-43: primary structure and regulated expression of mRNA during embryogenesis
Baizer, L., Alkan, S., Stocker, K. M., & Ciment, G. (1990) · Molecular Brain Research · doi:10.1016/0169-328x(90)90074-n · Cited by 40
Cloning and Characterization of the Rat Gene Encoding GAP‐43
Grabczyk, E., Zuber, M. X., Federoff, H. J., Ng, S., Pack, A. M., & Fishman, M. C. (1990) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1990.tb00393.x · Cited by 39
Self-citation
Phosphorylation of GAP-43 T172 is a molecular marker of growing axons in a wide range of mammals including primates
Okada, M., Kawagoe, Y., Sato, Y., Nozumi, M., Ishikawa, Y., Tamada, A., Yamazaki, H., Sekino, Y., Kanemura, Y., Shinmyo, Y., et al. (2021) · Molecular Brain · doi:10.1186/s13041-021-00755-0 · Cited by 37
Pediatric Peripheral Neuroectodermal Tumors, Oncogenes, and Differentiation
Thiele, C. J. (1990) · Cancer Investigation · doi:10.3109/07357909009018932 · Cited by 36
Translating the frontiers of brain repair to treatments: Starting not to break the rules
Carmichael, S. T. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.005 · Cited by 35
Presynaptic phosphoprotein B-50/GAP-43 in neuronal and synaptic plasticity.
Biewenga, J. E., Schrama, L. H., & Gispen, W. H. (1996) · Acta Biochimica Polonica · doi:10.18388/abp.1996_4502 · Cited by 33
Development of GAP-43 mRNA in the macaque cerebral cortex
Oishi, T., Higo, N., Umino, Y., Matsuda, K., & Hayashi, M. (1998) · Developmental Brain Research · doi:10.1016/s0165-3806(98)00067-4 · Cited by 32
The NCAM‐derived P2 peptide facilitates recovery of cognitive and motor function and ameliorates neuropathology following traumatic brain injury
Klementiev, B., Novikova, T., Korshunova, I., Berezin, V., & Bock, E. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06245.x · Cited by 31
Transient expression of GAP-43 within the hippocampus after global brain ischemia in rat
Schmidt‐Kastner, R., Bedard, A. M., & Hakim, A. M. (1997) · Cell and Tissue Research · doi:10.1007/s004410050808 · Cited by 30
Cerebral venous thrombosis in nephrotic syndrome.
Akatsu, H., Vaysburd, M., Fervenza, F. C., Peterson, J., & Jacobs, M. B. (1997) · PubMed · Cited by 29
Differential expression of growth-associated protein (GAP-43) mRNA in rat primary sensory neurons after peripheral nerve lesion: a non-radioactive in situ hybridisation study
Wiese, U. H., Ruth, J. L., & Emson, P. C. (1992) · Brain Research · doi:10.1016/0006-8993(92)91669-6 · Cited by 29
Elevated expression of B‐50 (GAP‐43)‐mRNA in a subpopulation of olfactory bulb mitral cells following axotomy
Verhaagen, J., Zhang, Y., Hamers, F. P. T., & Gispen, W. H. (1993) · Journal of Neuroscience Research · doi:10.1002/jnr.490350206 · Cited by 28
Transient expression of GAP-43 in nonneuronal cells of the embryonic chicken limb
Stocker, K. M., Baizer, L., & Ciment, G. (1992) · Developmental Biology · doi:10.1016/0012-1606(92)90295-r · Cited by 27
Neocortex and hippocampus contain distinct distributions of calcium‐calmodulin protein kinase II and GAP43 mRNA
Jacobs, K., Neve, R., & Donoghue, J. P. (1993) · The Journal of comparative neurology · doi:10.1002/cne.903360112 · Cited by 28
S(+)-Ketamine Up-Regulates Neuronal Regeneration Associated Proteins Following Glutamate Injury in Cultured Rat Hippocampal Neurons
Himmelseher, S., Pfenninger, E. G., Kochs, E. F., & Auchter, M. (2000) · Journal of Neurosurgical Anesthesiology · doi:10.1097/00008506-200004000-00003 · Cited by 25
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de Groen, P. C., Eggen, B. J. L., Gispen, W. H., Schotman, P., & Schrama, L. H. (1995) · Journal of Molecular Neuroscience · doi:10.1007/bf02736770 · Cited by 24
Contrasting patterns of protein phosphorylation in human normal and Alzheimer brain: Focus on protein kinase C and protein F1GAP-43
Florez, J. C., Nelson, R. B., & Routtenberg, A. (1991) · Experimental Neurology · doi:10.1016/0014-4886(91)90126-w · Cited by 23
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Prévot, V., Bouret, S. G., Croix, D., Alonso, G., Jennes, L., Mitchell, V. A., Routtenberg, A., & Beauvillain, J. (2000) · Endocrinology · doi:10.1210/en.141.5.1648 · Cited by 22
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Tagaya, M., Matsuyama, T., Nakamura, H., Hata, R., Shimizu, S., Kiyama, H., Matsumoto, M., & Sugita, M. (1995) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1995.140 · Cited by 22
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Neve, R. L., Ivins, K. J., Benowitz, L. I., During, M. J., & Geller, A. I. (1991) · Molecular Neurobiology · doi:10.1007/bf02935542 · Cited by 22
Chapter 7 Neuronal plasticity in normal aging and deficient plasticity in Alzheimer's disease: a proposed intercellular signal cascade
Coleman, P. D., Rogers, K. E., & Flood, D. G. (1990) · Progress in brain research · doi:10.1016/s0079-6123(08)63168-4 · Cited by 21
Involvement of Growth‐Associated Protein‐43 with Irreversible Neurite Outgrowth by Dibutyryl Cyclic AMP and Phorbol Ester in NG108–15 Cells
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Authors: Ng, S.-C., de la Monte, S. M., Conboy, G. L., Karns, L. R., & Fishman, M. C.
Affiliations: Howard Hughes Medical Institute (US)
Harvard University (US)
ORCID: de la Monte, Suzanne M.
Fishman, Mark C.
Venue: Neuron
Publisher: Elsevier BV
Published: 1988-04
Volume: 1
Issue: 2
Pages: 133-139
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(88)90197-3
OpenAlex: W2054092941
Cited by: 150
References: 41
Citations by year: 2025: 4 · 2024: 1 · 2022: 1 · 2021: 9 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 2 · 2013: 4 · 2012: 1
FWCI: 6.85
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: Howard Hughes Medical Institute
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nerve injury and regeneration
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
Keywords: GAP-43, growth-associated protein, cDNA cloning, growth cones, axon elongation, CNS repair, ischemic injury, neuronal remodeling, postmortem brain, neonatal brain, neurological disorders
MeSH terms: Adolescent, Aging, Amino Acid Sequence, Base Sequence, Brain, Cerebral Infarction, DNA, Humans, Infant, Newborn, Membrane Glycoproteins, Middle Aged, Molecular Sequence Data, Nerve Tissue Proteins, GAP-43 Protein

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Cloning of human GAP 43: Growth association and ischemic resurgence

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