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Human Polyclonal PRKD1 Primary Antibody for IHC (p), WB - ABIN391011
Wu, Solaro: Protein kinase C zeta. A novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins. in The Journal of biological chemistry 2007
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Human Polyclonal PRKD1 Primary Antibody for ELISA, WB - ABIN562395
Sin, Martin, Wills, Currie, Baillie: Small heat shock protein 20 (Hsp20) facilitates nuclear import of protein kinase D 1 (PKD1) during cardiac hypertrophy. in Cell communication and signaling : CCS 2015
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Human Polyclonal PRKD1 Primary Antibody for ICC, IF - ABIN4345848
Weinreb, Piscuoglio, Martelotto, Waggott, Ng, Perez-Ordonez, Harding, Alfaro, Chu, Viale, Fusco, da Cruz Paula, Marchio, Sakr, Lim, Thompson, Chiosea, Seethala, Skalova, Stelow, Fonseca, Assaad, How et al.: Hotspot activating PRKD1 somatic mutations in polymorphous low-grade adenocarcinomas of the salivary glands. ... in Nature genetics 2014
cloning and expression analysis of a protein kinase C gene, PKCmu, and its regulation of the promoter region (PKCmu)
PKD1 contributes to the regulation of physiological angiogenesis and lymphangiogenesis during zebrafish development and is essential for tumor angiogenesis.
PKD1 not only regulates the hypoxic glycolytic metabolism of cancer cells via regulation of the expression of HIF-1alpha and glycolytic enzymes.
these results describe a novel mechanism governing PRKD1 gene expression in pancreatic ductal adenocarcinoma and provide a functional link between oncogenic KRas, NF-kappaB and expression of PRKD1.
p110alpha subunit of PI3K and PKD mediate YAP activation in response to insulin and neurotensin in pancreatic cancer cells. Inhibitors of PI3K or PKD disrupt crosstalk between insulin receptor and GPCR signaling systems by blocking YAP/TEAD-regulated gene expression in pancreatic cancer cells
High PRKD1 expression is associated with drug resistance in breast cancer.
Our findings directly associate the AR/NCOA1 complex with PRKD1 regulation and cellular migration and support the concept of therapeutic inhibition of NCOA1 in prostate cancer.
None of the Polymorphous low-grade adenocarcinoma (PLGA) lacking PRKD1 somatic mutations or PRKD gene family rearrangements harboured somatic mutations in the kinase domains of the PRKD2 or PRKD3 genes.
A single nucleotide polymorphism located within the fourth intron of PRKD1 (rs57803087) was strongly associated with DPP-4 inhibitor response in patients with type 2 diabetes
Mutation in PRKD1 gene is associated with congenital heart defects.
Bradykinin stimulates myofibroblast migration through protein kinase D-mediated activation of COX-2 and Hsp27.
Lysophosphatidic acid/PKD-1 signaling leads to nuclear accumulation of histone deacetylase 7, where it interacts with forkhead box protein O1 to suppress endothelial CD36 transcription and mediates silencing of antiangiogenic switch, resulting in proangiogenic and proarteriogenic reprogramming.
This study discovered and characterized a novel, highly conserved N-terminal domain, comprising 92 amino acids, which mediates dimerization of Protein Kinase D (PKD) isoforms, PKD1, PKD2, and PKD3 monomers.
MC stimulation by physical contact with T cells results in PKD activation, leading to the phosphorylation of p38, degranulation and release of cytokines. Understanding the molecular events associated with T cell-induced MC activation might lead to therapeutic approaches for controlling T cell-mediated inflammatory processes in which MC participate.
Data suggest the role of the phospholipase C epsilon-Protein kinase D-PEA15 protein-ribosomal S6 kinase-IkappaB-NF-kappa B pathway in facilitating inflammation and inflammation-associated carcinogenesis in the colon.
PRKD1 Mutation is not associated with Solid Tumors and Leukemias.
Knockdown of PKD1 did not affect NMDAR internalization but prevented the phosphorylation and inhibition of remaining surface NMDARs and NMDAR-mediated synaptic functions.
Studies indicate that the loss of protein kinase D PKD1 is thought to promote invasion and metastasis, while PKD2 and upregulated PKD3 to be positive regulators of proliferation.
it is highly possible that PKD1 plays a critical role in signal transduction from the PKC pathway to the tyrosine kinase pathway
Positional mapping of PRKD1, NRP1 and PRDM1 as novel candidate disease genes in truncus arteriosus
Protein kinase D is increased and activated in lung epithelial cells and macrophages in idiopathic pulmonary fibrosis.
a positive relationship between L1 and pPKD1 in both cultured cerebellar neurons and human cerebellar tissue, suggesting that L1 functions in the modulation of PKD1 phosphorylation.
these results suggest a potentially important role for PRKD1 in bone formation.
The study demonstrates an essential role for PKD1 in the beta-cell adaptive secretory response to high-fat feeding in mice.
These findings imply that PKD1 plays a critical regulatory role in Group B streptococci (GBS)-induced proinflammatory reactions and sepsis, and inhibition of PKD1 activation together with antibiotic treatment in GBS-infected neonates could be an effective way to control GBS diseases.
Our studies demonstrate that PKD1/2 is a key regulator of MVB maturation and exosome secretion, and constitutes a mediator of the DGK alpha effect on MVB secretory traffic.
Our results show that AKAP13-PKD1 signaling is critical for transcriptional regulation of key contractile, cell death, and metabolic pathways during the development of compensatory hypertrophy in vivo.
PKD1 acts downstream of TGFalpha and Kras, to mediate formation of ductal structures through activation of the Notch pathway.
Results reveal that whereas protein kinase D1 and protein kinase D2 are essential for neuronal polarity, there exists a functional redundancy between the two proteins.
we demonstrated that protein kinase D1 (PKD1) plays a survival role during the early stage of oxidative stress in dopaminergic neuronal cells
PKD controls synaptic plasticity and learning by regulating actin stability in dendritic spines.
regulatory kinase of eNOS in endothelial cells whose activity orchestrates mammalian vascular tone
Overexpression of constitutively active PKD1 in rodent heart results in dilated cardiomyopathy.
PKD1-deficient keratinocytes showed an increase in transglutaminase expression and activity, indicating an anti-differentiative role of PKD1. Furthermore, the PKD1-deficient keratinocytes exhibited decreased proliferation.
BTK and protein kinase C mu, that are involved in TLR7/9-triggered IFN-beta production in dendritic cells.
findings reveal a pathway initiated by GPCR agonist-induced RhoA activation, in which PLCepsilon signals to PKD1-mediated phosphorylation of cytoskeletal proteins
PKD1 mediates class IIa histone deacetylase phosphorylation and nuclear extrusion in intestinal epithelial cells.
Beta-adrenergic receptor signaling triggers local nuclear signaling and inhibits GqR-mediated PKD activation by preventing its intracellular translocation.
PKD1 has a critical role in epidermal adaptive responses, including wound healing and skin carcinogenesis
G protein-coupled receptor (GPR)40-dependent potentiation of insulin secretion in mouse islets is mediated by protein kinase D1.
AngII activates PKD via a mechanism involving Src family kinases and PKC, to underlie increased aldosterone production.
Data indicate that Ser738/742-to-glutamate protein kinase D mutant increased AngII-induced CREB protein and activating transcription factor 2 phosphorylation, and phospho-CREB binding to the steroidogenic acute regulatory protein promoter.
These results indicate that PKD is downstream of PLD and suggest that PKD is one of the mechanisms through which PLD promotes aldosterone production in response to AngII in adrenal glomerulosa cells.
PKD mediates acute AngII-induced aldosterone secretion.
Protein kinase D-HDAC5 pathway plays an important role in VEGF regulation of gene transcription and angiogenesis
PRKD1 is a serine/threonine kinase that regulates a variety of cellular functions, including membrane receptor signaling, transport at the Golgi, protection from oxidative stress at the mitochondria, gene transcription, and regulation of cell shape, motility, and adhesion (summary by Eiseler et al., 2009
protein kinase D1
, protein kinase C, mu
, serine/threonine-protein kinase D1-like
, protein kinase C mu type
, protein kinase D
, serine/threonine-protein kinase D1
, protein kinase C mu