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Found evidence for kidney and liver cystic phenotypes in the Carney complex, a tumoral syndrome caused by mutations in PRKAR1A (zeige PRKAR1A ELISA Kits).
Data suggest that introduction of cGMP-specific (zeige PDE6A ELISA Kits) residues using site-directed mutagenesis reduces selectivity of cyclic nucleotide-binding domain (CNBD) of PRKAR1A (zeige PRKAR1A ELISA Kits); combination of two mutations (G316R/A336T) results in a cGMP-selective binding site in the C-terminal CNBD; introduction of corresponding mutations (T192R/A212T) into the N-terminal CNBD results in a highly cGMP-selective binding site.
Data show that ELOVL7 (zeige ELOVL7 ELISA Kits), SOCS3 (zeige SOCS3 ELISA Kits), ACSL4 (zeige ACSL4 ELISA Kits) and CLU (zeige CLU ELISA Kits) were upregulated while PRKAR1A (zeige PRKAR1A ELISA Kits) and ABCG1 (zeige ABCG1 ELISA Kits) were downregulated in the phlegm-dampness group.
Electrostatic interactions are mediators in the allosteric activation of protein kinase A RIalpha (zeige PRKAR1A ELISA Kits).
the present study reported for the first time an intronic splice site mutation in the PRKAR1A (zeige PRKAR1A ELISA Kits) gene of a Chinese family with Carney complex, which probably caused skin pigmentation observed in affected family members.
This study reports a novel point mutation of the PRKAR1A (zeige PRKAR1A ELISA Kits) gene in a patient with Carney complex who presented with significant osteoporosis and fractures.
a significant association between PKR2 rs6053283 polymorphism and Recurrent pregnancy loss (RPL)(P=0.003), whereas no association was observed between PKR1 rs4627609 polymorphism and RPL (P=0.929) in the Chinese Han population.
Letter/Case Report: novel PRKAR1A (zeige PRKAR1A ELISA Kits) mutation resulting in a splicing variant in a case of Carney complex.
Data suggest that prokineticins (PROK1 (zeige Prok1 ELISA Kits) and PROK2 (zeige PROK2 ELISA Kits)) and prokineticin receptors (PROKR1 and PROKR2 (zeige PROKR2 ELISA Kits)) act as main regulators of physiological functions of ovary, uterus, placenta, and testis. [REVIEW]
EG-VEGF (zeige Prok1 ELISA Kits) and its receptor PKR1 might play a role in the pathogenesis of adrenocortical tumors and could serve as prognostic markers for this rare malignant disease.
These results establish PKR1 via NFATc3 (zeige NFATC3 ELISA Kits) as a crucial modifier of mesenchymal-epithelial transition processing to the development of nephron.
show that MRAP2 significantly and specifically inhibits PKR1 signaling.
Data show that the prokineticins and their receptors PROK2 (zeige PROK2 ELISA Kits), PKR1 and PKR2 (zeige PROKR2 ELISA Kits) contributes to altered sensitivity in diabetic neuropathy and its inhibition blocked both allodynia and inflammatory events underlying disease.
These results suggest PKR1 to be a crucial player in the preadipocyte proliferation and differentiation.
Loss of PKR1 causes renal and cardiac structural and functional changes because of deficits in survival signaling, mitochondrial, and progenitor cell functions in found both organs.
The functional characteristics of coronary endothelial cells depend on the expression of PKR1 and PKR2 (zeige PROKR2 ELISA Kits) levels and the divergent signaling pathways used by these receptors.
Identification and molecular characterization of two closely related G protein-coupled receptors (prokineticin receptor)
PKR1 protein was localised to the labyrinth layer and showed the same pattern of expression as EG-VEGF (zeige Prok1 ELISA Kits) in mouse placenta.
Cardiomyocyte-PKR1 signaling upregulates its own ligand prokineticin-2 (zeige PROK2 ELISA Kits) that acts as a paracrine factor, triggering epicardial-derived progenitor cell proliferation/differentiation.
Data show that the inflammation-induced up-regulation of PK2 (zeige PROK2 ELISA Kits) was significantly less in pkr1 null mice than in WT and pkr2 (zeige PROKR2 ELISA Kits) null mice, demonstrating a role of PKR1 in setting PK2 (zeige PROK2 ELISA Kits) levels during inflammation.
PROK1 (zeige Prok1 ELISA Kits), acting via PROKR1, may be involved in the recruitment of monocytes to regressing CL and atretic follicles and their consequent activation therein.
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. This gene encodes one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Mutations in this gene cause Carney complex (CNC). This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). Several alternatively spliced transcript variants encoding two different isoforms have been observed.
prokineticin receptor 1
, G protein-coupled receptor 73
, prokineticin receptor 1-like
, G protein-coupled receptor ZAQ
, G-protein coupled receptor 73
, G-protein coupled receptor ZAQ
, cAMP-dependent protein kinase regulatory subunit RIalpha
, cAMP-dependent protein kinase type I-alpha regulatory chain
, cAMP-dependent protein kinase type I-alpha regulatory subunit
, protein kinase A type 1a regulatory subunit
, tissue-specific extinguisher 1