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

Heat shock protein, alpha-crystallin-related, B6

P20, HSP20
may play a role in muscle contraction [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: PrP, CAN, ACID, caspase-3, HAD
Papers using P20 antibodies
WebGestalt: an integrated system for exploring gene sets in various biological contexts
Geisert Eldon E. et al., In Gene Regulation and Systems Biology, 2004
... on Alcoholism (U01AA13499, U24AA13513); a Human Brain Project funded jointly by the NIDA, NIMH, and NIAAA (P20-DA 21131); NCI MMHCC (U01CA105417); and Biomedical Informatics Research Network (BIRN), ...
The induction of antibody production by IL-6 is indirectly mediated by IL-21 produced by CD4+ T cells
Rincon Mercedes et al., In The Journal of Experimental Medicine, 2002
... Rincon) and the Vermont Genetics Network through grant P20 RR16462 from the IDeA Network of Biomedical Research Excellence program of ...
Shiga toxin-producing Escherichia coli strains from bovines: association of adhesion with carriage of eae and other genes.
Shields Malcolm S. et al., In Emerging Infectious Diseases, 1995
... This study was partially supported by National Institutes of Health grant P20 RR016454 from the Infrastructure Network of Biomedical Research Excellence Program of ...
Apoptosis in the pathogenesis and treatment of disease
Schönbeck Uwe et al., In The Journal of Experimental Medicine, 1994
... P20 antibody was provided by Santa Cruz biotechnology.
Papers on P20
The effect of electrical stimulation on post mortem myofibrillar protein degradation and small heat shock protein kinetics in bull beef.
Farouk et al., Piracicaba, Brazil. In Meat Sci, Mar 2016
Electrical stimulation significantly affected the variable levels of αβ-crystallin and HSP20 with higher concentrations of these sHSP in ES muscles at later ageing timepoints compared with NS muscles.
Characterization and expression analysis of a caspase-2 in an invertebrate echinoderm sea cumber Apostichopus japonicus.
Li et al., Dalian, China. In Fish Shellfish Immunol, Jan 2016
In addition, a p20 large subunit with a characteristic five-peptide motif (QACRG) and a p10 small subunit in C-terminal were identified in CASs domain.
HSP25 down-regulation enhanced p53 acetylation by dissociation of SIRT1 from p53 in doxorubicin-induced H9c2 cell apoptosis.
Xiao et al., Changsha, China. In Cell Stress Chaperones, Nov 2015
Subsequent studies found that HSP25, but not HSP90, HSP70, and HSP20, interacted with SIRT1.
Protecting against ischemic stroke in rats by HSP 20-mediated exercise.
Lin et al., Taipei, Taiwan. In Eur J Clin Invest, Nov 2015
METHOD: Adult male Sprague-Dawley rats (288 in number) were used to investigate the contribution of HSP20-containing neurons and HSP20-containing glial cells in the exercise-mediated neuroprotection in the stroke condition using middle cerebral artery occlusion.
Altered Gene Expression in the Schistosome-Transmitting Snail Biomphalaria glabrata following Exposure to Niclosamide, the Active Ingredient in the Widely Used Molluscicide Bayluscide.
Loker et al., Albuquerque, United States. In Plos Negl Trop Dis, Oct 2015
Specifically, six heat shock protein (HSP) genes from three super-families (HSP20, HSP40 and HSP70) were upregulated.
Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 (PKD1).
Baillie et al., Glasgow, United Kingdom. In Cell Biochem Funct, Oct 2015
Heat shock protein 20 (HSP20) has cardioprotective qualities, which are triggered by PKA phosphorylation.
Monocyte Caspase-1 Is Released in a Stable, Active High Molecular Weight Complex Distinct from the Unstable Cell Lysate-Activated Caspase-1.
Wewers et al., Columbus, United States. In Plos One, 2014
Size exclusion chromatography identified two antigenic forms of p20 caspase-1 in the activation induced released caspase-1: one at the predicted size of tetrameric, p20/p10 caspase-1 and the other at >200 kDa.
The cardioprotective role of small heat-shock protein 20.
Baillie et al., Glasgow, United Kingdom. In Biochem Soc Trans, 2014
The small HSP (heat-shock protein) HSP20 is a molecular chaperone that is transiently up-regulated in response to cellular stress/damage.
Emerging targets for novel therapy of asthma.
Camoretti-Mercado et al., Mobile, United States. In Curr Opin Pharmacol, 2013
The cAMP/PKA pathway continues to be a promising drug target with the emergence of new PDE inhibitors and a novel PKA target protein, HSP20, which mediates smooth muscle relaxation via actin depolymerization.
The A-kinase-anchoring protein AKAP-Lbc facilitates cardioprotective PKA phosphorylation of Hsp20 on Ser(16).
Baillie et al., Glasgow, United Kingdom. In Biochem J, 2012
the cytosolic protein AKAP-Lbc (AKAP13) as the anchoring protein responsible for directing PKA phosphorylation of Hsp20 on Ser(16)
Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20).
Gusev et al., Moscow, Russia. In Arch Biochem Biophys, 2012
cofilins 1 and 2 only weakly interact with 14-3-3 and therefore cannot directly compete with phosphorylated small heat shock protein HspB6 for its binding to 14-3-3
Hsp20 functions as a novel cardiokine in promoting angiogenesis via activation of VEGFR2.
Fan et al., Cincinnati, United States. In Plos One, 2011
Hsp20 serves as a novel cardiokine in regulating myocardial angiogenesis through activation of the VEGFR signaling cascade.
Properties of the monomeric form of human 14-3-3ζ protein and its interaction with tau and HspB6.
Gusev et al., Moscow, Russia. In Biochemistry, 2011
Properties of the monomeric form of 14-3-3zeta protein and its interaction with tau and HspB6. This interaction requires phosphorylation of tau protein and HspB6.
Large potentials of small heat shock proteins.
Gusev et al., Moscow, Russia. In Physiol Rev, 2011
HSPB6 (HSP20) also possesses chaperone-like activity, is involved in regulation of smooth muscle contraction, has pronounced cardioprotective activity, and seems to participate in insulin-dependent regulation of muscle metabolism.
Acetylation of heat shock protein 20 (Hsp20) regulates human myometrial activity.
Europe-Finner et al., Newcastle upon Tyne, United Kingdom. In J Biol Chem, 2011
A potential molecular mechanism by which Hsp20 acetylation can affect myometrial activity by liberating cofilin
The emerging role of HSP20 as a multifunctional protective agent.
Baillie et al., Glasgow, United Kingdom. In Cell Signal, 2011
Recently, one member of the sHSP family, HSP20 (HspB6), has been shown to be highly effective as a protective mediator against a number of debilitating pathological conditions, including cardiac hypertrophy and Alzheimer's disease.
The role of microRNA in modulating myocardial ischemia-reperfusion injury.
Birnbaum et al., Galveston, United States. In Physiol Genomics, 2011
By altering the expression of various key elements in cell survival and apoptosis [such as phosphoinositide 3-kinase (PI3K), phosphatase and tensin homolog deleted on chromosome 10 (PTEN), Bcl-2, Mcl-1, heat shock protein (HSP)60, HSP70, HSP20, programmed cell death 4 (Pdcd4), LRRFIP1, Fas ligand (FasL), Sirt-1, etc.], miRNAs alter the response to ischemia-reperfusion injury.
Granzyme B-induced apoptosis requires both direct caspase activation and relief of caspase inhibition.
Bleackley et al., Edmonton, Canada. In Immunity, 2003
Indeed, cleavage of caspase 3 to p20 still occurred in Bcl-2-transfectants but processing to p17 was blocked.
Crystal structure of Arp2/3 complex.
Pollard et al., Los Angeles, United States. In Science, 2001
Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-terminal alpha helices and have similarly folded amino-terminal alpha/beta domains.
Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer.
Hammill et al., Ludwigshafen am Rhein, Germany. In Cell, 1994
The crystal structure at 2.5 A resolution of a recombinant human ICE-tetrapeptide chloromethylketone complex reveals that the holoenzyme is a homodimer of catalytic domains, each of which contains a p20 and a p10 subunit.
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