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

Prostaglandin E synthase 3

cPGES, Hsp90 co-chaperone, cytosolic prostaglandin E2 synthase, cytosolic prostaglandin E synthase
Top mentioned proteins: Hsp90, mPGES-1, cyclooxygenase, mPGES-2, CAN
Papers using cPGES antibodies
Measurement of pH and ionic composition of pericellular sites
Jacques Claire et al., In Arthritis Research & Therapy, 1974
... Texas, USA); anti-mouse COX-1 polyclonal antibody; anti-mouse mPGES-1 polyclonal antibody; anti-mouse mPGES-2 polyclonal antibody; anti-mouse cPGES polyclonal antibody (Cayman from SPI-BIO, Massy, France); ...
Papers on cPGES
NudC regulates actin dynamics and ciliogenesis by stabilizing cofilin 1.
Zhou et al., Hangzhou, China. In Cell Res, Jan 2016
Here we find that nuclear distribution gene C (NudC), an Hsp90 co-chaperone, is required for actin organization and dynamics.
Nodal promotes functional luteolysis via downregulation of progesterone and prostaglandins E2 and promotion of PGF2 alpha synthetic pathways in mare corpus luteum.
Ferreira-Dias et al., Olsztyn, Poland. In Endocrinology, Jan 2016
Nodal treatment of luteal cells decreased progesterone (P4) and prostaglandin (PG) E2 concentrations in culture media (p<0.05), as well as mRNA and protein of secretory enzymes StAR, CYP11A1, cPGES and mPGES1 (p<0.05).
Prostaglandin E2 / cyclooxygenase pathway in human skeletal muscle: Influence of muscle fiber type and age.
Trappe et al., In J Appl Physiol, Dec 2015
PGE2/COX pathway proteins [COX enzymes (COX-1, COX-2), PGE2 synthases (cPGES, mPGES-1, mPGES-2), and PGE2 receptors (EP1, EP2, EP3, EP4)] were quantified via Western blot.
Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.
Sharma et al., Chandīgarh, India. In Plos Genet, Oct 2015
The requirement of Cpr7 is specific for [URE3] as its deletion does not antagonize both strong and weak variant of another yeast prion [PSI+], suggesting a distinct role of the Hsp90 co-chaperone with different yeast prions.
Lysophosphatidic acid modulates prostaglandin signalling in bovine steroidogenic luteal cells.
Woclawek-Potocka et al., Olsztyn, Poland. In Prostaglandins Other Lipid Mediat, Sep 2015
The aim of the present study was to determine the influence of LPA on PGE2 and PGF2α synthesis and on the expression of enzymes involved in PG biosynthesis (PTGS2, mPGES-1, cPGES, mPGES-2, PGFS and 9-KPR), prostaglandin transporter (PGT), and prostaglandin receptors (EP1, EP2, EP3, EP4 and FP) in bovine steroidogenic luteal cells.
Substrate recognition and function of the R2TP complex in response to cellular stress.
Macurek et al., Praha, Czech Republic. In Front Genet, 2014
The R2TP complex is a HSP90 co-chaperone, which consists of four subunits: PIH1D1, RPAP3, RUVBL1, and RUVBL2.
The FKBP51-Glucocorticoid Receptor Balance in Stress-Related Mental Disorders.
Rein et al., München, Germany. In Curr Mol Pharmacol, 2014
It was originally characterized as Hsp90 cochaperone and part of the receptor-chaperone heterocomplex that governs the activity of steroid receptors.
Targeting Hsp90 and its co-chaperones to treat Alzheimer's disease.
Dickey et al., Tampa, United States. In Expert Opin Ther Targets, 2014
The development of Hsp90/tau complex-specific inhibitors and further development of Hsp90 co-chaperone-specific drugs should yield more potent, less toxic therapeutics.
Tumor-intrinsic and tumor-extrinsic factors impacting hsp90- targeted therapy.
Trepel et al., Bethesda, United States. In Curr Mol Med, 2012
An additional area of recent progress in Hsp90 research is in studies of the posttranslational modifications of Hsp90 itself and Hsp90 co-chaperone proteins.
p23 co-chaperone protects the aryl hydrocarbon receptor from degradation in mouse and human cell lines.
Chan et al., Việt Trì, Vietnam. In Biochem Pharmacol, 2012
p23 co-chaperone protects the aryl hydrocarbon receptor from degradation
miRNA mediated up-regulation of cochaperone p23 acts as an anti-apoptotic factor in childhood acute lymphoblastic leukemia.
Zheng et al., Beijing, China. In Leuk Res, 2012
As an anti-apoptotic factor, p23 is able to be a potential target for anti-leukemic therapy.
Cytosolic Bax: does it require binding proteins to keep its pro-apoptotic activity in check?
Borner et al., Freiburg, Germany. In J Biol Chem, 2012
In cytosol only one protein called p23 hsp90 binds to Bax but the binding protein does not affect the subcellular localization and pro-apoptotic activity of Bax.
Research resource: enhanced genome-wide occupancy of estrogen receptor α by the cochaperone p23 in breast cancer cells.
Garabedian et al., New York City, United States. In Mol Endocrinol, 2012
a small increase in the expression of p23 amplifies ER-binding genome wide and, in combination with ER, elicits an invasive phenotype in breast cancer
Influenza virus infection induces the nuclear relocalization of the Hsp90 co-chaperone p23 and inhibits the glucocorticoid receptor response.
Naffakh et al., Paris, France. In Plos One, 2010
The p23 cochaperone of Hsp90, which plays a major role in glucocorticoid receptor folding and function, associates with influenza virus polymerase.
[Development of anti-inflammatory drugs targeted against prostaglandin-related molecules].
Yamano et al., Mariana, Brazil. In Nihon Rinsho, 2010
Prostaglandin E2 (PGE2) is a proinflammatory mediator that is synthesized by cyclooxygenases (COX-1 and COX-2) and prostaglandin E synthases (cPGES-1 and mPGES-1); PGE2 exerts its biological effects by binding to specific receptors.
Membrane prostaglandin E synthase-1: a novel therapeutic target.
Jakobsson et al., Stockholm, Sweden. In Pharmacol Rev, 2007
cytosolic PGE synthase (cPGES) and two membrane-bound PGE synthases, mPGES-1 and mPGES-2.
Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis.
Balch et al., Los Angeles, United States. In Cell, 2006
Cell-surface rescue of the most common disease variant that is restricted to the ER, DeltaF508, can be initiated by partial siRNA silencing of the Hsp90 cochaperone ATPase regulator Aha1.
Structure and mechanism of the Hsp90 molecular chaperone machinery.
Prodromou et al., London, United Kingdom. In Annu Rev Biochem, 2005
Additionally, we describe the roles of the plethora of cochaperones with which Hsp90 cooperates and growing insights into their biochemical mechanisms, which come from crystal structures of Hsp90 cochaperone complexes.
Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans.
Baumeister et al., München, Germany. In Cell, 2004
Caenorhabditis elegans UNC-45 facilitates this by functioning both as a chaperone and as a Hsp90 cochaperone for myosin during thick filament assembly.
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin.
Epstein et al., Houston, United States. In Science, 2002
Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans.
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