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Human Monoclonal PRKAR1A Primary Antibody for IF, IHC - ABIN2452637
Maleszewski, Larsen, Kip, Castonguay, Edwards, Carney, Kipp: PRKAR1A in the development of cardiac myxoma: a study of 110 cases including isolated and syndromic tumors. in The American journal of surgical pathology 2014
Show all 2 Pubmed References
Human Polyclonal PRKAR1A Primary Antibody for EIA, ICC - ABIN2729579
Cao, Xia, Zhou, Yang, Hao, Peng, Liu, Zhu: Methylcrotonoyl-CoA carboxylase 1 potentiates RLR-induced NF-κB signaling by targeting MAVS complex. in Scientific reports 2016
Human Polyclonal PRKAR1A Primary Antibody for WB - ABIN519180
Uys, Ramburan, Loos, Kinnear, Korkie, Mouton, Riedemann, Moolman-Smook: Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C. in BMC cell biology 2011
Results demonstrate that PKA activity regulated by Mys is indispensable for negative regulation of the Hh signaling pathway in Hh-responsive cells.
Kidney-specific loss of Prkar1a induced renal cystic disease and markedly aggravated cystogenesis in the Pkd1(RC) models.
data demonstrate that haploinsufficiency for either one of the type-II regulatory subunits improved the bone phenotype of mice haploinsufficient for Prkar1a
PRKAR1A gene and its locus are altered in mixed odontogenic tumors. Expression is decreased in a subset of tumors, and Prkar1a(+) (/) (-) mice do not show abnormalities, which indicates that additional genes play a role in this tumor's pathogenesis.
Prkar1a activation enhances beta-catenin (show CTNNB1 Antibodies) transcriptional activity through nuclear localization to PML (show PML Antibodies) bodies.
Loss of Prkar1a can only promote tumorigenesis when Prkar1a-mediated apoptosis is somehow countered.
Data show that mammary-specific loss of Prkar1a leads to elevated type-II PKA isozyme activation and this is sufficient to drive breast carcinogenesis.
Results show that mouse Prkar1a and human PRKAR2A (show PRKAR2A Antibodies) exhibited a dynamic spatio-temporal expression in tooth development, whereas neither human PRKAR1A nor mouse Prkar2a (show PRKAR2A Antibodies) showed their expression in odontogenesis.
Ablation of Prkar1a interferes with signaling pathways necessary for osteoblast differentiation.
hypoxia/reoxygenation (H/R)-mediated decrease in PKARIalpha protein levels leads to activation of RSK1 (show RPS6KA1 Antibodies), which via phosphorylation of NHE1 (show SLC9A1 Antibodies) induces cardiomyocyte apoptosis.
Prkar1a was found to play a critical role in peripheral nerve development.
Found evidence for kidney and liver cystic phenotypes in the Carney complex, a tumoral syndrome caused by mutations in PRKAR1A.
Data suggest that introduction of cGMP-specific (show PDE6A Antibodies) residues using site-directed mutagenesis reduces selectivity of cyclic nucleotide-binding domain (CNBD) of PRKAR1A; 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 (show ELOVL7 Antibodies), SOCS3 (show SOCS3 Antibodies), ACSL4 (show ACSL4 Antibodies) and CLU (show CLU Antibodies) were upregulated while PRKAR1A and ABCG1 (show ABCG1 Antibodies) were downregulated in the phlegm-dampness group.
Electrostatic interactions are mediators in the allosteric activation of protein kinase A RIalpha.
the present study reported for the first time an intronic splice site mutation in the PRKAR1A 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 gene in a patient with Carney complex who presented with significant osteoporosis and fractures.
Letter/Case Report: novel PRKAR1A mutation resulting in a splicing variant in a case of Carney complex.
P-Rex1 (show PREX1 Antibodies) contributes to the spatiotemporal localization of type I PKA, which tightly regulates this guanine exchange factor by a multistep mechanism.
In the absence of a PRKAR1A gene mutation, our Cushing's syndrome patients do not fit the criteria for Carney's complex
Case Report: although there was no family history of any of the Carney complex features and no mutations in the PRKAR1A gene were found, findings lead to the diagnosis of sporadic Carney complex.
ceramide activates plasma membrane Ca2+-ATPase from kidney-promixal tubule cells with protein kinase A as an intermediate
Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit)
Data suggest PRKAR1A contains two structurally homologous cAMP-binding domains that exhibit marked differences in dynamic profiles in activation/inhibition of Prkaca (show PRKACA Antibodies); conservation of structure does not necessarily imply conservation of dynamics.
Results describe the structures of the protein kinase A RIalpha subunit D/D domain alone and in complex with D-AKAP2 (show AKAP10 Antibodies).
Data show that RSK1 (show RPS6KA1 Antibodies) regulates PKAc activity in a cAMP-independent manner, and PKARIalpha by associating with RSK1 (show RPS6KA1 Antibodies) regulates its activation and its biological functions.
angle X-ray scattering studies indicate RIalpha, RIIalpha, and RIIbeta (show PRKAR2B Antibodies) homodimers differ markedly in overall shape despite extensive sequence homology and similar molecular masses;cAMP binding does not cause large conformational changes(Prkar1a, Prkar2a (show PRKAR2A Antibodies))
the PKA RIalpha subunit dynamic C helix mediates isoform-specific domain reorganization upon C subunit binding
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.
protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1)
, cAMP-dependent protein kinase type I-alpha regulatory subunit
, cAMP-dependent protein kinase regulatory subunit alpha 1
, cAMP-dependent protein kinase type I-alpha regulatory subunit-like
, protein kinase, cAMP dependent regulatory, type 1, alpha
, cAMP-dependent protein kinase regulatory subunit RIalpha
, cAMP-dependent protein kinase type I-alpha regulatory chain
, protein kinase A type 1a regulatory subunit
, tissue-specific extinguisher 1
, protein kinase, cAMP dependent regulatory, type I, alpha
, cAMP-dependent protein kinase type I regulatory subunit
, cAMP-dependent protein kinase, regulatory subunit alpha 1