نتایج جستجو برای: 60 hsp60

تعداد نتایج: 301710  

2017
Jose A. Mendoza Kevin K. Weinberger Matthew J. Swan

The heat shock protein, Hsp60, is one of the most abundant proteins in Helicobacter pylori. Given its sequence homology to the Escherichia coli Hsp60 or GroEL, Hsp60 from H. pylori would be expected to function as a molecular chaperone in this organism. H. pylori is an organism that grows on the gastric epithelium, where the pH can fluctuate between neutral and 4.5 and the intracellular pH can ...

Journal: :BMC Blood Disorders 2004
Chengfeng Xiao Sheng Chen Mingchun Yuan Fuyue Ding Dongliang Yang Ruibo Wang Jianxin Li Robert M Tanguay Tangchun Wu

BACKGROUND Immune thrombocytopenic purpura (ITP) is an autoimmune disease characterized by platelet destruction resulting from autoantibodies against platelet proteins, particularly platelet glycoprotein IIb/IIIa. Heat shock proteins (Hsp) have been shown to be major antigenic determinants in some autoimmune diseases. Antibodies to Hsps have also been reported to be associated with a number of ...

Journal: :Journal of cell science 2005
Gerald Pfister Cordula M Stroh Hannes Perschinka Michaela Kind Michael Knoflach Peter Hinterdorfer Georg Wick

The highly conserved and ubiquitous heat shock proteins (HSP) are essential for the cellular homeostasis and efficiently trigger cellular responses to stress conditions. Both microbial and human HSP act as dominant antigens in numerous infectious and autoimmune diseases such as atherosclerosis, inducing a strong immune-inflammatory response. In the present study, the surface localization of HSP...

Journal: :The Journal of biological chemistry 2011
Yan Li Rui Si Yan Feng Howard H Chen Lin Zou E Wang Ming Zhang H Shaw Warren David E Sosnovik Wei Chao

Innate immune response after transient ischemia is the most common cause of myocardial inflammation and may contribute to injury, yet the detailed signaling mechanisms leading to such a response are not well understood. Herein we tested the hypothesis that myocardial ischemia activates interleukin receptor-associated kinase-1 (IRAK-1), a kinase critical for the innate immune signaling such as t...

Journal: :Investigative ophthalmology & visual science 1995
R G Rank C Dascher A K Bowlin P M Bavoil

PURPOSE To determine whether immunization with recombinant Hsp60 would exacerbate ocular pathology on challenge with viable chlamydial elementary bodies. METHODS Guinea pigs were immunized either subcutaneously with recombinant Hsp60 or both subcutaneously with recombinant Hsp60 and ocularly with attenuated Salmonella typhimurium expressing the guinea pig inclusion conjunctivitis (GPIC) Hsp60...

2002
S. R. Kirchhoff S. Gupta A. A. Knowlton

Background—Heat shock proteins (HSPs) are well known for their ability to " protect " the structure and function of native macromolecules, particularly as they traffic across membranes. Considering the role of key mitochondrial proteins in apoptosis and the known antiapoptotic effects of HSP27 and HSP72, we postulated that HSP60, primarily a mitochondrial protein, also exerts an antiapoptotic e...

Journal: :The Journal of Experimental Medicine 1992
C J Boog E R de Graeff-Meeder M A Lucassen R van der Zee M M Voorhorst-Ogink P J van Kooten H J Geuze W van Eden

Heat-shock proteins have been shown to be critical antigens in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development was seen to coincide with development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homologue. We have developed murine monoclonal antibodies after immunization ...

2018
Ryuichi Ishida Tomoya Okamoto Fumihiro Motojima Hiroshi Kubota Hiroki Takahashi Masako Tanabe Toshihiko Oka Akira Kitamura Masataka Kinjo Masasuke Yoshida Michiro Otaka Ewa Grave Hideaki Itoh

The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmetric complex, and GroEL exists as double rings regardless of the presence of adenosine triphosphate (ATP). Its mammalian chaperonin homolog, heat shock protein, HSP60, and co-chaperonin, HSP10, play an essential role in protein folding by capturing unfolded proteins in the HSP60/HSP10 complex. How...

Journal: :Circulation 2002
S R Kirchhoff S Gupta A A Knowlton

BACKGROUND Heat shock proteins (HSPs) are well known for their ability to "protect" the structure and function of native macromolecules, particularly as they traffic across membranes. Considering the role of key mitochondrial proteins in apoptosis and the known antiapoptotic effects of HSP27 and HSP72, we postulated that HSP60, primarily a mitochondrial protein, also exerts an antiapoptotic eff...

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