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

Docking protein 3

Dokl, Dok-3
Top mentioned proteins: Dok-1, CAN, ACID, POLYMERASE, ERK
Papers on Dokl
TRAF6-mediated degradation of DOK3 is required for production of IL-6 and TNFα in TLR9 signaling.
Peng et al., Changchun, China. In Mol Immunol, Dec 2015
Our previous study showed that the downstream of kinase 3 (DOK3) is degraded during macrophage stimulation with CpG.
Searching for candidate genes in familial BRCAX mutation carriers with prostate cancer.
Thorne et al., Melbourne, Australia. In Urol Oncol, Dec 2015
In addition, 3 truncating variants, CYP3A43, DOK3, and PLEKHH3, demonstrated complete segregation and 3 truncation mutations, HEATR5B, GPR124, and HKR1, demonstrated partial segregation with PC.
Integrated genomic approaches identify major pathways and upstream regulators in late onset Alzheimer's disease.
Scott et al., London, United Kingdom. In Sci Rep, 2014
Protein-protein interaction network analysis emphasised the role of NFKB; identified a key interaction of CLU with complement; and linked TYROBP, TREM2 and DOK3 to modulation of LPS signalling through TLR4 and to phosphatidylinositol metabolism.
Hypertensive renal injury is associated with gene variation affecting immune signaling.
Doris et al., Houston, United States. In Circ Cardiovasc Genet, 2014
METHODS AND RESULTS: We used next gen sequencing to detect natural allelic variation in 5 genes of the immunoreceptor signaling pathway (IgH, Dok3, Src, Syk, and JunD) that arise from different ancestors in the injury-prone SHR-A3 and the resistant SHR-B2 lines.
Adaptor protein DOK3 promotes plasma cell differentiation by regulating the expression of programmed cell death 1 ligands.
Lam et al., Singapore, Singapore. In Proc Natl Acad Sci U S A, 2014
Although DOK3 is dispensable for early B-cell development, its role in plasma cell (PC) differentiation is unknown.
DOK3 is required for IFN-β production by enabling TRAF3/TBK1 complex formation and IRF3 activation.
Lam et al., Singapore, Singapore. In J Immunol, 2014
In this study, we elucidated a novel role for DOK3 in IFN-β production.
A physical interaction between the adaptor proteins DOK3 and DAP12 is required to inhibit lipopolysaccharide signaling in macrophages.
Humphrey et al., Changchun, China. In Sci Signal, 2013
We show that inhibition of LPS responses by DAP12 is mediated by the adaptor protein DOK3 (downstream of kinase 3).
DOK3 negatively regulates LPS responses and endotoxin tolerance.
Humphrey et al., Oklahoma City, United States. In Plos One, 2011
We show here that DOK3 is a negative regulator of TLR signaling by limiting LPS-induced ERK activation and cytokine responses in macrophages.
B cell receptor-mediated antigen gathering requires ubiquitin ligase Cbl and adaptors Grb2 and Dok-3 to recruit dynein to the signaling microcluster.
Batista et al., London, United Kingdom. In Immunity, 2011
identify a surprising but pivotal role for dynein and the microtubule network alongside Grb2, Dok-3, and Cbl in antigen gathering during B cell activation
A gene expression signature for chemoradiosensitivity of colorectal cancer cells.
Grade et al., Göttingen, Germany. In Int J Radiat Oncol Biol Phys, 2010
These data have suggested a potential relevance of the insulin and Wnt signaling pathways for treatment response, and we identified STAT3, RASSF1, DOK3, and ERBB2 as potential therapeutic targets.
Identification of DOK genes as lung tumor suppressors.
Pandolfi et al., Boston, United States. In Nat Genet, 2010
Identification of DOK genes as lung tumor suppressors.
A novel nuclear marker, Pm-int9, for phylogenetic studies of Opisthorchis felineus, Opisthorchis viverrini, and Clonorchis sinensis (Opisthorchiidae, Trematoda).
Mordvinov et al., Novosibirsk, Russia. In Parasitol Res, 2009
Dokl Biochem Biophys 421:214-217, 2008) have provided evidence using ribosomal and mitochondrial sequences that O. viverrini, O. felineus, and C. sinensis are closely related.
Proteomic analysis of integrin alphaIIbbeta3 outside-in signaling reveals Src-kinase-independent phosphorylation of Dok-1 and Dok-3 leading to SHIP-1 interactions.
García et al., Birmingham, United Kingdom. In J Thromb Haemost, 2009
The novel platelet adapter Dok-3 is tyrosine phosphorylated in an Src kinase-independent manner downstream of alphaIIbbeta3 in human platelets, leading to an interaction with Grb2 and SHIP-1.
Dok-3 plays a nonredundant role in negative regulation of B-cell activation.
Lam et al., Singapore, Singapore. In Blood, 2007
In the absence of Dok-3, the localization of the inhibitory phosphatase SHIP-1 to the plasma membrane is intact while its phosphorylation is compromised, suggesting that Dok-3 could function to facilitate or sustain the activation of SHIP-1.
Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts the intensity of Ca2+ signaling in B cells.
Wienands et al., Göttingen, Germany. In Embo J, 2007
Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts the intensity of Ca2+ signaling in B cells.
[Oxidized glutathione induces activation of the epidermal growth factor receptor and MAP kinases ERK 1,2].
Nikol'skiĭ et al., In Tsitologiia, 2005
Recently, we showed transactivation of EGFR and activation of transcription factor STAT3, rather than STAT1, induced by glutathione disulfide (GSSG) and glutoxim in epidermoid carcinoma A431 cells (Burova et al., Dokl.
Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/DOK5.
Shoelson et al., Boston, United States. In J Biol Chem, 2003
Because the other known PH-PTB proteins (insulin receptor substrates: IRS-1, IRS-2, IRS-3, and IRS-4, and the downstream of kinases: DOK-1, DOK-2, and DOK-3) are substrates of insulin and insulin-like growth factor (IGF)-1 receptors, we asked whether these new proteins, termed IRS5/DOK4 and IRS6/DOK5, might also have roles in insulin and IGF-1 signaling.
DOK4 and DOK5: new Dok-related genes expressed in human T cells.
Nunès et al., Marseille, France. In Genes Immun, 2003
Based on analysis of phylogenetic trees and exon/intron structure of Dok family members, DOK4 and DOK5 define a subfamily within dok genes distinct from DOK1, DOK2 and DOK3.
The primary structure of papaya mosaic virus coat protein.
Davies et al., Norwich, United Kingdom. In Virology, 1986
V. Kozlov, J. G. Atabekov, and K. G. Skyabin, Dokl.
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