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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 protein 1

SH3 domain-binding protein, 3BP-1
Top mentioned proteins: Src, G3BP, GAP, ABL, CAN
Papers on SH3 domain-binding protein
The proline-rich region of glyceraldehyde-3-phosphate dehydrogenase from human sperm may bind SH3 domains, as revealed by a bioinformatic study of low-complexity protein segments.
Grynberg et al., Warsaw, Poland. In Mol Reprod Dev, Jan 2016
The putative binding partners of the proline-rich GAPDHS motif include SH3 domain-binding protein 4 (SH3BP4) and the IL2-inducible T-cell kinase/tyrosine-protein kinase ITK/TSK (ITK).
Overexpression of Ras-GTPase-activating protein SH3 domain-binding protein 1 correlates with poor prognosis in gastric cancer patients.
Gu et al., Shanghai, China. In Histopathology, Nov 2015
AIMS: Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is a downstream effector of Ras signalling, and is overexpressed in several types of human malignancy.
Involvement of Ras GTPase-activating protein SH3 domain-binding protein 1 in the epithelial-to-mesenchymal transition-induced metastasis of breast cancer cells via the Smad signaling pathway.
Shao et al., Beijing, China. In Oncotarget, Aug 2015
Ras GTPase-activating protein SH3 domain-binding protein 1 (G3BP1), an essential Ras mediator, has been implicated in cancer development, including cell growth, motility, invasion and apoptosis.
Resveratrol induces apoptosis by directly targeting Ras-GTPase-activating protein SH3 domain-binding protein 1.
Dong et al., Austin, United States. In Oncogene, Jun 2015
Here, the Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) was identified as a potential target of resveratrol, and in vitro binding assay results using resveratrol-conjugated Sepharose 4B beads confirmed their direct binding.
Loss of SH3 domain-binding protein 2 function suppresses bone destruction in tumor necrosis factor-driven and collagen-induced arthritis in mice.
Ueki et al., Kansas City, United States. In Arthritis Rheumatol, Mar 2015
OBJECTIVE: SH3 domain-binding protein 2 (SH3BP2) is a signaling adapter protein that regulates the immune and skeletal systems.
Apollon/Bruce is upregulated by Humanin.
Matsuoka et al., Tokyo, Japan. In Mol Cell Biochem, 2014
A previous study demonstrated that the Humanin-induced activation of the htHNR/JAK2/STAT3 signaling pathway leads to increased expression of SH3 domain-binding protein 5 (SH3BP5), which is an essential effector of Humanin's anti-cell death activity in some cultured neuronal cells.
Tyrosine phosphorylation of 3BP2 is indispensable for the interaction with VAV3 in chicken DT40 cells.
Sada et al., Fukui, Japan. In Exp Cell Res, 2014
Adaptor protein c-Abl SH3 domain-binding protein-2 (3BP2) is known to play regulatory roles in immunoreceptor-mediated signal transduction.
eEF2 and Ras-GAP SH3 domain-binding protein (G3BP1) modulate stress granule assembly during HIV-1 infection.
Mouland et al., Montréal, Canada. In Nat Commun, 2013
Here we show that HIV-1 Gag blocks SG assembly irrespective of eIF2α phosphorylation and even when SG assembly is forced by overexpression of Ras-GAP SH3 domain-binding protein (G3BP1) or TIAR.
SH3-binding protein 5 mediates the neuroprotective effect of the secreted bioactive peptide humanin by inhibiting c-Jun NH2-terminal kinase.
Matsuoka et al., Tokyo, Japan. In J Biol Chem, 2013
In the present study, Humanin increased the mRNA and protein expression of SH3 domain-binding protein 5 (SH3BP5), which has been known to be a JNK interactor, in neuronal cells.
[Syk inhibitors].
Sada et al., Fukui, Japan. In Nihon Rinsho, 2013
Furthermore, we will introduce our findings of the adaptor protein 3BP2 (c-Abl SH3 domain-binding protein-2), as a novel target of Syk.
Individual Src-family tyrosine kinases direct the degradation or protection of the clock protein Timeless via differential ubiquitylation.
Smithgall et al., Pittsburgh, United States. In Cell Signal, 2013
Here we report that mammalian Timeless is an SH3 domain-binding protein and substrate for several members of the Src protein-tyrosine kinase family, including Fyn, Hck, c-Src and c-Yes.
Deficiency of G3BP1, the stress granules assembly factor, results in abnormal synaptic plasticity and calcium homeostasis in neurons.
Tazi et al., Montpellier, France. In J Neurochem, 2013
Ras-GAP SH3-domain-binding protein, G3BP, is an important component in the assembly of stress granules (SGs), which are cytoplasmic aggregates assembled following translational stress.
Both G3BP1 and G3BP2 contribute to stress granule formation.
Fujii et al., Niigata, Japan. In Genes Cells, 2013
Ras-GTPase-activating protein SH3 domain-binding protein 1 (G3BP1) is a component of SGs that initiates the assembly of SGs by forming a multimer.
Epithelial junction formation requires confinement of Cdc42 activity by a novel SH3BP1 complex.
Balda et al., London, United Kingdom. In J Cell Biol, 2012
Epithelial junction formation and morphogenesis require a dual activity complex, containing SH3BP1 and CapZ, that is recruited to sites of active membrane remodeling to guide Cdc42 signaling and cytoskeletal dynamics.
The GTPase dynamin binds to and is activated by a subset of SH3 domains.
Booker et al., London, United Kingdom. In Cell, 1993
In this report, affinity purification techniques were used to identify the GTPase dynamin as an SH3 domain-binding protein.
Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.
Baltimore et al., New York City, United States. In Science, 1992
A complementary DNA was isolated that encoded a protein, 3BP-1, to which the SH3 region of Abl bound with high specificity and to which SH3 regions from other proteins bound differentially.
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