GHR
GHR (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[23][24]
Искәрмәләр[үзгәртү | вики-текстны үзгәртү]
- ↑ 1,0 1,1 UniProt
- ↑ 2,0 2,1 2,2 M Sundström, T Lundqvist, J Rödin et al. Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1996. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.271.50.32197 — PMID:8943276
- ↑ 3,0 3,1 3,2 3,3 3,4 3,5 Sobrier M., MO S. A single amino acid substitution in the exoplasmic domain of the human growth hormone (GH) receptor confers familial GH resistance (Laron syndrome) with positive GH-binding activity by abolishing receptor homodimerization // EMBO J. — NPG, 1994. — ISSN 0261-4189; 1460-2075 — doi:10.1002/J.1460-2075.1994.TB06392.X — PMID:8137822
- ↑ 4,0 4,1 4,2 Vos A. M. d., M. Ultsch, Kossiakoff A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex // Science / H. Thorp — AAAS, 1992. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.1549776 — PMID:1549776
- ↑ 5,0 5,1 5,2 T Amit, T Bergman, F Dastot et al. A membrane-fixed, truncated isoform of the human growth hormone receptor // J. Clin. Endocrinol. Metab. / R. Paul Robertson — Endocrine Society, 1997. — ISSN 0021-972X; 1945-7197; 0096-7173; 0368-1610 — doi:10.1210/JC.82.11.3813 — PMID:9360546
- ↑ 6,0 6,1 T Clackson, Ultsch M. H., Wells J. A. et al. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity // Journal of Molecular Biology / P. Wright — Elsevier BV, 1998. — ISSN 0022-2836; 1089-8638 — doi:10.1006/JMBI.1998.1669 — PMID:9571026
- ↑ 7,0 7,1 M Sundström, T Lundqvist, J Rödin et al. Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1996. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.271.50.32197 — PMID:8943276
- ↑ 8,0 8,1 Vos A. M. d., M. Ultsch, Kossiakoff A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex // Science / H. Thorp — AAAS, 1992. — ISSN 0036-8075; 1095-9203 — doi:10.1126/SCIENCE.1549776 — PMID:1549776
- ↑ Filippakopoulos P., Savitsky P., Barr A. J. et al. Large-scale structural analysis of the classical human protein tyrosine phosphatome // Cell — Cell Press, Elsevier BV, 2009. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2008.11.038 — PMID:19167335
- ↑ Pasquali C., Rob Hooft van Huijsduijnen, Wälchli S. Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor // Molecular Endocrinology — Endocrine Society, OUP, 2003. — ISSN 0888-8809; 1944-9917 — doi:10.1210/ME.2003-0011 — PMID:12907755
- ↑ Chen T., Lin K., Chen C. et al. Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network // J. Proteome Res. / J. Yates — ACS, 2014. — ISSN 1535-3893; 1535-3907 — doi:10.1021/PR5002737 — PMID:25241761
- ↑ 12,00 12,01 12,02 12,03 12,04 12,05 12,06 12,07 12,08 12,09 12,10 12,11 12,12 GOA
- ↑ 13,0 13,1 13,2 13,3 Hammonds G., Henzel W. J., Barnard R. T. Growth hormone receptor and serum binding protein: purification, cloning and expression // Nature / M. Skipper — NPG, Springer Science+Business Media, 1987. — ISSN 1476-4687; 0028-0836 — doi:10.1038/330537A0 — PMID:2825030
- ↑ 14,00 14,01 14,02 14,03 14,04 14,05 14,06 14,07 14,08 14,09 14,10 14,11 14,12 14,13 14,14 14,15 14,16 14,17 14,18 14,19 GOA
- ↑ Pelekanos R. A., McKinstry W. J., Parker M. W. Model for growth hormone receptor activation based on subunit rotation within a receptor dimer // Nat. Struct. Mol. Biol. — USA: NPG, 2005. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB977 — PMID:16116438
- ↑ 16,00 16,01 16,02 16,03 16,04 16,05 16,06 16,07 16,08 16,09 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
- ↑ 17,0 17,1 T Clackson, Ultsch M. H., Wells J. A. et al. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity // Journal of Molecular Biology / P. Wright — Elsevier BV, 1998. — ISSN 0022-2836; 1089-8638 — doi:10.1006/JMBI.1998.1669 — PMID:9571026
- ↑ Sobrier M., MO S. A single amino acid substitution in the exoplasmic domain of the human growth hormone (GH) receptor confers familial GH resistance (Laron syndrome) with positive GH-binding activity by abolishing receptor homodimerization // EMBO J. — NPG, 1994. — ISSN 0261-4189; 1460-2075 — doi:10.1002/J.1460-2075.1994.TB06392.X — PMID:8137822
- ↑ 19,0 19,1 19,2 Carlsson L. Mutations of the growth hormone receptor in children with idiopathic short stature. The Growth Hormone Insensitivity Study Group // N. Engl. J. Med. / J. M. Drazen, F. J. Ingelfinger — MMS, 1995. — ISSN 0028-4793; 1533-4406 — doi:10.1056/NEJM199510263331701 — PMID:7565946
- ↑ Sjögren K., Low T. Estrogen inhibits GH signaling by suppressing GH-induced JAK2 phosphorylation, an effect mediated by SOCS-2 // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2003. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0337600100 — PMID:12552091
- ↑ Carlsson L. Mutations of the growth hormone receptor in children with idiopathic short stature. The Growth Hormone Insensitivity Study Group // N. Engl. J. Med. / J. M. Drazen, F. J. Ingelfinger — MMS, 1995. — ISSN 0028-4793; 1533-4406 — doi:10.1056/NEJM199510263331701 — PMID:7565946
- ↑ Godowski P. J., Leung D. W., Meacham L. R. et al. Characterization of the human growth hormone receptor gene and demonstration of a partial gene deletion in two patients with Laron-type dwarfism // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1989. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.86.20.8083 — PMID:2813379
- ↑ 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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