 src Homology Domains
"src Homology Domains" 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.
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.
| Descriptor ID |
D018909
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| MeSH Number(s) |
G02.111.570.790.709.610.640.750
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| Concept/Terms |
src Homology Domains- src Homology Domains
- Homology Domain, src
- Homology Domains, src
- src Homology Domain
- SH Domains
- SH Domain
SH2 Domain- SH2 Domain
- SH2 Domains
- src Homology Region 2 Domain
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Below are MeSH descriptors whose meaning is more general than "src Homology Domains".
Below are MeSH descriptors whose meaning is more specific than "src Homology Domains".
This graph shows the total number of publications written about "src Homology Domains" by people in this website by year, and whether "src Homology Domains" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1996 | 0 | 1 | 1 | | 1997 | 2 | 3 | 5 | | 1998 | 1 | 2 | 3 | | 1999 | 1 | 1 | 2 | | 2000 | 1 | 1 | 2 | | 2001 | 2 | 1 | 3 | | 2002 | 0 | 2 | 2 | | 2003 | 0 | 1 | 1 | | 2004 | 0 | 1 | 1 | | 2005 | 0 | 2 | 2 | | 2006 | 1 | 2 | 3 | | 2009 | 0 | 1 | 1 | | 2010 | 2 | 1 | 3 | | 2011 | 0 | 1 | 1 | | 2012 | 1 | 1 | 2 | | 2014 | 2 | 0 | 2 | | 2016 | 0 | 2 | 2 | | 2017 | 1 | 0 | 1 |
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Below are the most recent publications written about "src Homology Domains" by people in Profiles.
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Kükenshöner T, Schmit NE, Bouda E, Sha F, Pojer F, Koide A, Seeliger M, Koide S, Hantschel O. Selective Targeting of SH2 Domain-Phosphotyrosine Interactions of Src Family Tyrosine Kinases with Monobodies. J Mol Biol. 2017 05 05; 429(9):1364-1380.
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Ciaccio MF, Jones RB. Microwestern Arrays for Systems-Level Analysis of SH2 Domain-Containing Proteins. Methods Mol Biol. 2017; 1555:453-473.
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Sharma S, Galanina N, Guo A, Lee J, Kadri S, Van Slambrouck C, Long B, Wang W, Ming M, Furtado LV, Segal JP, Stock W, Venkataraman G, Tang WJ, Lu P, Wang YL. Identification of a structurally novel BTK mutation that drives ibrutinib resistance in CLL. Oncotarget. 2016 Oct 18; 7(42):68833-68841.
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Zhang Y, Wang X, Matakatsu H, Fehon R, Blair SS. The novel SH3 domain protein Dlish/CG10933 mediates fat signaling in Drosophila by binding and regulating Dachs. Elife. 2016 10 03; 5.
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Wojcik J, Lamontanara AJ, Grabe G, Koide A, Akin L, Gerig B, Hantschel O, Koide S. Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface. J Biol Chem. 2016 Apr 15; 291(16):8836-47.
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Bartelt RR, Light J, Vacaflores A, Butcher A, Pandian M, Nash P, Houtman JC. Regions outside of conserved PxxPxR motifs drive the high affinity interaction of GRB2 with SH3 domain ligands. Biochim Biophys Acta. 2015 Oct; 1853(10 Pt A):2560-9.
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Engelmann BW, Kim Y, Wang M, Peters B, Rock RS, Nash PD. The development and application of a quantitative peptide microarray based approach to protein interaction domain specificity space. Mol Cell Proteomics. 2014 Dec; 13(12):3647-62.
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Leung KK, Hause RJ, Barkinge JL, Ciaccio MF, Chuu CP, Jones RB. Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome. Mol Cell Proteomics. 2014 Jul; 13(7):1705-23.
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Sha F, Gencer EB, Georgeon S, Koide A, Yasui N, Koide S, Hantschel O. Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains. Proc Natl Acad Sci U S A. 2013 Sep 10; 110(37):14924-9.
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Chung S, Suzuki H, Miyamoto T, Takamatsu N, Tatsuguchi A, Ueda K, Kijima K, Nakamura Y, Matsuo Y. Development of an orally-administrative MELK-targeting inhibitor that suppresses the growth of various types of human cancer. Oncotarget. 2012 Dec; 3(12):1629-40.
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