L1CAM
Внешний вид
L1CAM (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[21][22]
Искәрмәләр
[үзгәртү | вики-текстны үзгәртү]- ↑ 1,0 1,1 1,2 1,3 UniProt
- ↑ 2,0 2,1 Vinogradova O., Tyukhtenko S., Lemmon V. Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins // Biochemistry / A. Schepartz — ACS, 2008. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI702433Q — PMID:18321067
- ↑ 3,0 3,1 3,2 3,3 3,4 Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
- ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 4,12 4,13 4,14 4,15 GOA
- ↑ Waterman C. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
- ↑ Colombo F. L1CAM and its cell-surface mutants: new mechanisms and effects relevant to the physiology and pathology of neural cells // J. Neurochem. — Wiley-Blackwell, 2012. — ISSN 0022-3042; 1471-4159 — doi:10.1111/JNC.12015 — PMID:22973895
- ↑ Teckchandani A., Toida N., Goodchild J. et al. Quantitative proteomics identifies a Dab2/integrin module regulating cell migration // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2009. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200812160 — PMID:19581412
- ↑ 8,0 8,1 8,2 GOA
- ↑ 9,0 9,1 9,2 Schäfer M. K. E., Nam Y., Moumen A. et al. L1 syndrome mutations impair neuronal L1 function at different levels by divergent mechanisms // Neurobiol. Dis. — Elsevier BV, 2010. — ISSN 0969-9961; 1095-953X — doi:10.1016/J.NBD.2010.05.029 — PMID:20621658
- ↑ Mayr M., Iozzo R. V., Barallobre-Barreiro J. et al. Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation // Circulation — Lippincott Williams & Wilkins, 2016. — ISSN 0009-7322; 1524-4539 — doi:10.1161/CIRCULATIONAHA.115.016423 — PMID:27559042
- ↑ 11,0 11,1 11,2 11,3 Schäfer M. K. E., Nam Y., Moumen A. et al. L1 syndrome mutations impair neuronal L1 function at different levels by divergent mechanisms // Neurobiol. Dis. — Elsevier BV, 2010. — ISSN 0969-9961; 1095-953X — doi:10.1016/J.NBD.2010.05.029 — PMID:20621658
- ↑ Waterman C. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation // Nat. Cell Biol. — NPG, 2011. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB2216 — PMID:21423176
- ↑ 13,0 13,1 13,2 13,3 Colombo F. L1CAM and its cell-surface mutants: new mechanisms and effects relevant to the physiology and pathology of neural cells // J. Neurochem. — Wiley-Blackwell, 2012. — ISSN 0022-3042; 1471-4159 — doi:10.1111/JNC.12015 — PMID:22973895
- ↑ Teckchandani A., Toida N., Goodchild J. et al. Quantitative proteomics identifies a Dab2/integrin module regulating cell migration // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2009. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200812160 — PMID:19581412
- ↑ Mayr M., Iozzo R. V., Barallobre-Barreiro J. et al. Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation // Circulation — Lippincott Williams & Wilkins, 2016. — ISSN 0009-7322; 1524-4539 — doi:10.1161/CIRCULATIONAHA.115.016423 — PMID:27559042
- ↑ Lemmon V. P. Molecular structure and functional testing of human L1CAM: an interspecies comparison // Genomics / A. Engel — Academic Press, Elsevier BV, 1991. — ISSN 0888-7543; 1089-8646 — doi:10.1016/0888-7543(91)90150-D — PMID:1769655
- ↑ M Jouet, A Rosenthal, G Armstrong et al. X-linked spastic paraplegia (SPG1), MASA syndrome and X-linked hydrocephalus result from mutations in the L1 gene // Nature Genetics / M. Axton, T. Faial — NPG, 1994. — ISSN 1061-4036; 1546-1718 — doi:10.1038/NG0794-402 — PMID:7920659
- ↑ Zachary I. C., Frankel P., Evans I. M. et al. The role of neuropilins in cell signalling // Biochem. Soc. Trans. — Portland Press, 2009. — ISSN 0300-5127; 1470-8752 — doi:10.1042/BST0371171 — PMID:19909241
- ↑ 19,0 19,1 Godenschwege T. A. Differential effects of human L1CAM mutations on complementing guidance and synaptic defects in Drosophila melanogaster // PLOS ONE / PLOS ONE Editors — PLoS, 2013. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0076974 — PMID:24155914
- ↑ Godenschwege T. A. Differential effects of human L1CAM mutations on complementing guidance and synaptic defects in Drosophila melanogaster // PLOS ONE / PLOS ONE Editors — PLoS, 2013. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0076974 — PMID:24155914
- ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
- ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.
Чыганаклар
[үзгәртү | вики-текстны үзгәртү]- Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
- Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)
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