نتایج جستجو برای: chaperone

تعداد نتایج: 13493  

Journal: :Biochimica et biophysica acta 2004
Frederic G Sauer Han Remaut Scott J Hultgren Gabriel Waksman

Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence. The periplasmic chaperone facilitates the initial folding of fiber subunits but then traps them in activated folding transition states. Chaperone dissociation releases the folding energy that drives subunit incorporation into the fiber, which grows through a pore forme...

Journal: :RNA biology 2016
Scott Horowitz James C A Bardwell

Recently, we found that RNA is a remarkably powerful chaperone that can bind to unfolded proteins and transfer them to Hsp70 for refolding. Combined with past studies on RNA-chaperone interactions, we propose a model for how chaperone RNA activity may contribute to the cellular response to stress.

2016
Nikhil Sharma Aideen Kathleen Mary Walsh Sriram Rajagopalan

BACKGROUND The general medical council stipulate all intimate examinations should be chaperoned, and their identity documented within patients' notes. We decided to audit our surgical unit for compliance to these guidelines. METHODS A prospective audit before and after intervention was performed. Patients undergoing an intimate examination on the surgical assessment unit over five working day...

Journal: :Biochemistry 2009
Xin Hu Michael S Lee Anders Wallqvist

We describe an efficient approach to model the binding interaction of the disordered effector protein to its cognate chaperone in the type III secretion system (T3SS). Starting from de novo models, we generated ensembles of unfolded conformations of the Yersinia effector YopE using REMD simulations and docked them to the chaperone SycE using a multistep protein docking strategy. The predicted Y...

Journal: :BioEssays : news and reviews in molecular, cellular and developmental biology 2012
Shu Quan James C A Bardwell

Molecular chaperones assist de novo protein folding and facilitate the refolding of stress-denatured proteins. The molecular chaperone concept was coined nearly 35 years ago, and since then, tremendous strides have been made in understanding how these factors support protein folding. Here, we focus on how various chaperone proteins were first identified to play roles in protein folding. Example...

Journal: :The Journal of biological chemistry 2006
Ami Citri Daniel Harari Galit Shohat Parameswaran Ramakrishnan Judith Gan Sara Lavi Miriam Eisenstein Adi Kimchi David Wallach Shmuel Pietrokovski Yosef Yarden

Hsp90 is a highly abundant chaperone whose clientele includes hundreds of cellular proteins, many of which are central players in key signal transduction pathways and the majority of which are protein kinases. In light of the variety of Hsp90 clientele, the mechanism of selectivity of the chaperone toward its client proteins is a major open question. Focusing on human kinases, we have demonstra...

2016
Michael O. Daniyan Aileen Boshoff Earl Prinsloo Eva-Rachele Pesce Gregory L. Blatch Harm H Kampinga

Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chaperones of the heat shock protein (Hsp) family are prominent members of the exportome, including a number of Hsp40s and a Hsp70. PFA0660w, a type II Hsp40, has been shown ...

Journal: :Clinical cancer research : an official journal of the American Association for Cancer Research 2000
M Graner A Raymond D Romney L He L Whitesell E Katsanis

Although the use of tumor-derived heat shock/chaperone proteins (HSPs) as anticancer vaccines is gaining wider study and acceptance, there have thus far been no reports concerning chaperone antitumor activities against disseminated hematological malignancies. We have devised an efficient and effective method for purification of the chaperone proteins grp94/gp96, HSP90, HSP70, and calreticulin f...

Journal: :The Journal of biological chemistry 2005
Hemachand Tummala Cheolwha Jung Ashutosh Tiwari Cynthia M J Higgins Lawrence J Hayward Zuoshang Xu

Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by progressive motor neuron degeneration, paralysis, and death. Mutant Cu,Zn-superoxide dismutase (SOD1) causes a subset of ALS by an unidentified toxic property. Increasing evidence suggests that chaperone dysfunction plays a role in motor neuron degeneration in ALS. To investigate the relationship between mutant ...

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