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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SH3 domain binding glutamic acid-rich protein like

Top mentioned proteins: ACID, Thioredoxin, Chordin, Rhodopsin, HMG-14
Papers on SH3BGR
Dual-faced SH3BGRL: oncogenic in mice, tumor suppressive in humans.
Zeng et al., Guangzhou, China. In Oncogene, Nov 2015
Here, we first report the discovery of Src homology 3 (SH3) domain-binding glutamic acid-rich-like protein (SH3BGRL), a novel c-Src activator in mice.
A thioredoxin fold protein Sh3bgr regulates Enah and is necessary for proper sarcomere formation.
Park et al., Ulsan, South Korea. In Dev Biol, Oct 2015
The sh3bgr (SH3 domain binding glutamate-rich) gene encodes a small protein containing a thioredoxin-like fold, SH3 binding domain, and glutamate-rich domain.
Prevalence of chromosomal rearrangements involving non-ETS genes in prostate cancer.
Minner et al., Hamburg, Germany. In Int J Oncol, Apr 2015
Recurrent breakage, often accompanied by partial deletion of the genes, was found for NCKAP5, SH3BGR and TTC3 in 3 (0.8%) tumors each, as well as for ARNTL2 and ENOX1 in 2 (0.5%) cancers each.
Comparative proteomic profiling of triple-negative breast cancer reveals that up-regulation of RhoGDI-2 is associated to the inhibition of caspase 3 and caspase 9.
López-Camarillo et al., Mexico. In J Proteomics, 2015
Proteomics profiling of TNBC and normal breast tissues through two-dimensional electrophoresis and ESI-MS/MS mass spectrometry revealed the existence of 16 proteins (RhoGDI-2, HSP27, SOD1, DJ1, UBE2N, PSME1, FTL, SH3BGRL, and eIF5A-1) with increased abundance in carcinomas.
Signal transducer and activator of transcription 2 (STAT2) metabolism coupling postmitotic outgrowth to visual and sound perception network in human left cerebrum by biocomputation.
Lin et al., Beijing, China. In J Mol Neurosci, 2012
Our result showed that upstream RECQL, PDIA2, ENOSF1, THBS4, RASGRP1, PER2, PDE8A, ORC2L, DCI, OGG1_2, SMA4, GPD1, etc. activated STAT2, and downstream STAT2-activated GSTM3_1, GOSR1, SH3BGR, OSBPL8, PHYH, SAPS2, C21orf33, PDIA2, TRAPPC6A, ENOSF1, CAMTA1, GTF2I_2, etc. in human left cerebrum.
Discovery, identification, and characterization of candidate pharmacodynamic markers of methionine aminopeptidase-2 inhibition.
Wang et al., United States. In J Proteome Res, 2008
The combination of these approaches led to the discovery of novel MetAP2-specific substrates including thioredoxin-1 (Trx-1), SH3 binding glutamic acid rich-like protein (SH3BGRL), and eukaryotic elongation factor-2 (eEF2).
Proteome analysis of human substantia nigra in Parkinson's disease.
Wolf et al., Aachen, Germany. In Proteome Sci, 2007
Identified differential proteins comprised elements of iron metabolism (H-ferritin) and glutathione-related redox metabolism (GST M3, GST P1, GST O1), including novel redox proteins (SH3BGRL).
The suppression of SH3BGRL is important for v-Rel-mediated transformation.
Bose et al., Austin, United States. In Oncogene, 2006
mutations in predicted EVH1-binding domain of SH3BGRL had a modest effect on suppression of v-Rel transformation. This study provides the first example of a gene that is downregulated in v-Rel-expressing cells also playng a role in v-Rel transformation
Crystal structure of human SH3BGRL protein: the first structure of the human SH3BGR family representing a novel class of thioredoxin fold proteins.
Wang et al., Beijing, China. In Proteins, 2005
h-SH3BGRL should present a novel class of the thioredoxin fold proteins
Expression, purification and crystallization of a human protein SH3BGRL at atomic resolution.
Wang et al., Beijing, China. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005
The protein SH3BGRL, containing both SH3-binding and Homer EVH1-binding motifs, has been crystallized using the hanging-drop vapour-diffusion method.
Heart morphogenesis is not affected by overexpression of the Sh3bgr gene mapping to the Down syndrome heart critical region.
Schiaffino et al., Padova, Italy. In Hum Genet, 2004
The SH3BGR gene maps to the DS-CHD region and is a potential candidate for the pathogenesis of CHD, since it is selectively expressed in cardiac and skeletal muscle.
The identification of a novel human homologue of the SH3 binding glutamic acid-rich (SH3BGR) gene establishes a new family of highly conserved small proteins related to Thioredoxin Superfamily.
Scartezzini et al., Genova, Italy. In Gene, 2002
SH3BGRL and SH3BGRL3 code for small proteins similar to the N-terminal region of the SH3BGR protein.
A novel human homologue of the SH3BGR gene encodes a small protein similar to Glutaredoxin 1 of Escherichia coli.
Scartezzini et al., Genova, Italy. In Biochem Biophys Res Commun, 2001
In this paper, we describe the identification and characterization of a new human homologue of the SH3BGR gene, named SH3BGRL3 (SH3 domain binding glutamic acid-rich protein like 3).
Developmental expression of the SH3BGR gene, mapping to the Down syndrome heart critical region.
Scartezzini et al., Padova, Italy. In Mech Dev, 2000
The SH3BGR gene has been recently isolated and mapped to chromosome 21 within the Down syndrome (DS) congenital heart disease (CHD) minimal region.
A contiguous 3-Mb sequence-ready map in the S3-MX region on 21q22.2 based on high- throughput nonisotopic library screenings.
Yaspo et al., Berlin, Germany. In Genome Res, 1999
Gene distribution in the region includes 9 known genes (c21-LRP, WRB, SH3BGR, HMG14, PCP4, DSCAM, MX2, MX1, and TMPRSS2) and 14 new additional gene signatures consisting of cDNA selection products and ESTs.
Identification and characterization of a new human gene encoding a small protein with high homology to the proline-rich region of the SH3BGR gene.
Scartezzini et al., Genova, Italy. In Biochem Biophys Res Commun, 1998
As part of an effort to identify genes potentially involved in the Down Syndrome pathogenesis, in this paper we report the identification and characterization of a new human gene (named SH3BGRL), which shows a high homology to the SH3BGR gene, previously mapped to the Down Syndrome region of chromosome 21.
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