 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) |
G02.111.570.820.709.610.640.750
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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 |
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| 1995 | 2 | 0 | 2 | | 1996 | 1 | 3 | 4 | | 1997 | 4 | 2 | 6 | | 1998 | 2 | 1 | 3 | | 1999 | 3 | 2 | 5 | | 2000 | 3 | 0 | 3 | | 2001 | 3 | 3 | 6 | | 2002 | 5 | 4 | 9 | | 2003 | 0 | 4 | 4 | | 2005 | 1 | 3 | 4 | | 2006 | 3 | 2 | 5 | | 2007 | 3 | 3 | 6 | | 2008 | 1 | 0 | 1 | | 2009 | 2 | 2 | 4 | | 2011 | 1 | 2 | 3 | | 2012 | 2 | 2 | 4 | | 2013 | 1 | 3 | 4 | | 2014 | 0 | 1 | 1 | | 2015 | 0 | 1 | 1 | | 2016 | 1 | 1 | 2 | | 2017 | 2 | 0 | 2 | | 2018 | 1 | 1 | 2 |
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Below are the most recent publications written about "src Homology Domains" by people in Profiles.
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Veggiani G, Huang H, Yates BP, Tong J, Kaneko T, Joshi R, Li SSC, Moran MF, Gish G, Sidhu SS. Engineered SH2 domains with tailored specificities and enhanced affinities for phosphoproteome analysis. Protein Sci. 2019 02; 28(2):403-413.
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Wasserman SS, Shteiman-Kotler A, Harris K, Iliadi KG, Persaud A, Zhong Y, Zhang Y, Fang X, Boulianne GL, Stewart B, Rotin D. Regulation of SH3PX1 by dNedd4-long at the Drosophila neuromuscular junction. J Biol Chem. 2019 02 01; 294(5):1739-1752.
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de Araujo ED, Manaswiyoungkul P, Israelian J, Park J, Yuen K, Farhangi S, Berger-Becvar A, Abu-Jazar L, Gunning PT. High-throughput thermofluor-based assays for inhibitor screening of STAT SH2 domains. J Pharm Biomed Anal. 2017 Sep 05; 143:159-167.
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Tong J, Cao B, Martyn GD, Krieger JR, Taylor P, Yates B, Sidhu SS, Li SS, Mao X, Moran MF. Protein-phosphotyrosine proteome profiling by superbinder-SH2 domain affinity purification mass spectrometry, sSH2-AP-MS. Proteomics. 2017 03; 17(6).
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Ishikawa Y, Ito S, Nagata K, Sakai LY, Bächinger HP. Intracellular mechanisms of molecular recognition and sorting for transport of large extracellular matrix molecules. Proc Natl Acad Sci U S A. 2016 10 11; 113(41):E6036-E6044.
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Mazouchi A, Zhang Z, Bahram A, Gomes GN, Lin H, Song J, Chan HS, Forman-Kay JD, Gradinaru CC. Conformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer Model. Biophys J. 2016 Apr 12; 110(7):1510-1522.
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Jin LL, Wybenga-Groot LE, Tong J, Taylor P, Minden MD, Trudel S, McGlade CJ, Moran MF. Tyrosine phosphorylation of the Lyn Src homology 2 (SH2) domain modulates its binding affinity and specificity. Mol Cell Proteomics. 2015 Mar; 14(3):695-706.
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Wybenga-Groot LE, McGlade CJ. RTK SLAP down: the emerging role of Src-like adaptor protein as a key player in receptor tyrosine kinase signaling. Cell Signal. 2015 Feb; 27(2):267-74.
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Bernstein A, Rossant J. Anthony James Pawson (1952-2013). Nature. 2013 Sep 12; 501(7466):168.
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Wybenga-Groot LE, McGlade CJ. Crystal structure of Src-like adaptor protein 2 reveals close association of SH3 and SH2 domains through ß-sheet formation. Cell Signal. 2013 Dec; 25(12):2702-8.
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