نتایج جستجو برای: chaperone

تعداد نتایج: 13493  

Journal: :The Journal of biological chemistry 2001
F Pirkl E Fischer S Modrow J Buchner

FKBP52, a multidomain peptidyl prolyl cis/trans-isomerase (PPIase), is found in complex with the chaperone Hsp90 and the co-chaperone p23. It displays both PPIase and chaperone activity in vitro. To localize these two activities to specific regions of the protein, we created and analyzed a set of fragments of FKBP52. The PPIase activity toward both peptides and proteins is confined entirely to ...

2015
Donald Wolfgeher Diana M. Dunn Mark R. Woodford Dimitra Bourboulia Gennady Bratslavsky Mehdi Mollapour Stephen J. Kron Andrew W. Truman

Heat Shock Protein 90 (Hsp90) is an essential chaperone that supports the function of a wide range of signaling molecules. Hsp90 binds to a suite of co-chaperone proteins that regulate Hsp90 function through alteration of intrinsic ATPase activity. Several studies have determined Aha1 to be an important co-chaperone whose binding to Hsp90 is modulated by phosphorylation, acetylation and SUMOyla...

Journal: :Molecular cell 2005
Jeffrey J Kovacs Patrick J M Murphy Stéphanie Gaillard Xuan Zhao June-Tai Wu Christopher V Nicchitta Minoru Yoshida David O Toft William B Pratt Tso-Pang Yao

The molecular chaperone heat shock protein 90 (Hsp90) and its accessory cochaperones function by facilitating the structural maturation and complex assembly of client proteins, including steroid hormone receptors and selected kinases. By promoting the activity and stability of these signaling proteins, Hsp90 has emerged as a critical modulator in cell signaling. Here, we present evidence that H...

Journal: :The Journal of Cell Biology 2008
Tongzhong Ju Rajindra P. Aryal Caleb J. Stowell Richard D. Cummings

Regulatory pathways for protein glycosylation are poorly understood, but expression of branchpoint enzymes is critical. A key branchpoint enzyme is the T-synthase, which directs synthesis of the common core 1 O-glycan structure (T-antigen), the precursor structure for most mucin-type O-glycans in a wide variety of glycoproteins. Formation of active T-synthase, which resides in the Golgi apparat...

Journal: :BMB reports 2009
Songmi Lee Ji Sun Kim Chul Ho Yun Ho Zoon Chae Kanghwa Kim

To screen chaperone proteins from Schizosaccharomyce pombe (S. pombe), we prepared recombinant citrate synthase of the fission yeast as a substrate of anti-aggregation assay. Purified recombinant citrate synthase showed citrate synthase activity and was suitable for the substrate of chaperone assay. Several heat stable proteins including aspartyl aminopeptidase (AAP) for candidates of chaperone...

2016
Mark R. Woodford Diana M. Dunn Adam R. Blanden Dante Capriotti David Loiselle Chrisostomos Prodromou Barry Panaretou Philip F. Hughes Aaron Smith Wendi Ackerman Timothy A. Haystead Stewart N. Loh Dimitra Bourboulia Laura S. Schmidt W. Marston Linehan Gennady Bratslavsky Mehdi Mollapour

Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and it is regulated by co-chaperones. Here we show that the tumour suppressor FLCN is an Hsp90 client protein and its binding partners FNIP1/FNIP2 f...

Journal: :The Journal of biological chemistry 2000
C Mayr K Richter H Lilie J Buchner

Hsp90 is an abundant cytosolic molecular chaperone. It controls the folding of target proteins including steroid hormone receptors and kinases in complex with several partner proteins. Prominent members of this protein family are large peptidyl prolyl cis/trans isomerases (PPIases), which catalyze the cis/trans isomerization of prolyl peptide bonds in proteins and possess chaperone activity. In...

Journal: :Oncology reports 2008
Lynne W Elmore Robert Forsythe Heidi Forsythe A Taylor Bright Suhail Nasim Kanendori Endo Shawn E Holt

Over 90% of prostate cancers express telomerase activity. In an experimental model, hsp90 and p23, which are necessary for telomerase assembly and function, dramatically increase during tumorigenic conversion. We immunohistochemically analyzed 60 prostate carcinomas, 50 prostatic intraepithelial neoplasias (PIN) and 25 benign prostatic tissues to determine whether hsp90/p23 expression correlate...

2017
Adrienne L. Edkins

Hsp90 is a molecular chaperone that regulates the function of numerous oncogenic transcription factors and signalling intermediates in the cell. Inhibition of Hsp90 is sufficient to induce the proteosomal degradation of many of these proteins, and as such, the Hsp90 chaperone has been regarded as a promising drug target. The appropriate functioning of the Hsp90 chaperone is dependent on its ATP...

Journal: :Microbiology and molecular biology reviews : MMBR 2007
Sean-Paul Nuccio Andreas J Bäumler

Many Proteobacteria use the chaperone/usher pathway to assemble proteinaceous filaments on the bacterial surface. These filaments can curl into fimbrial or nonfimbrial surface structures (e.g., a capsule or spore coat). This article reviews the phylogeny of operons belonging to the chaperone/usher assembly class to explore the utility of establishing a scheme for subdividing them into clades of...

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