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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.
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