نتایج جستجو برای: heat shock

تعداد نتایج: 279169  

2010
P. Ginet K. Montagne S. Akiyama Y. Sakai T. Fujii D. Fourmy S. Volz B. J. Kim

In this work we describe a new way to investigate the effect of heating on the synthesis of heat-shock proteins (HSP) in mammalian cells by using gold microheaters in liquid chamber. We have successfully fabricated and thermally calibrated gold microheaters on which we could grow a monolayer of mammalian cells and heat-shock only a few of them by controlling temperature distribution over the de...

2015
Diana M. Dunn Mark R. Woodford Andrew W. Truman Sandra M. Jensen Jacqualyn Schulman Tiffany Caza Taylor C. Remillard David Loiselle Donald Wolfgeher Brian S.J. Blagg Lucas Franco Timothy A. Haystead Soumya Daturpalli Matthias P. Mayer Jane B. Trepel Rhodri M.L. Morgan Chrisostomos Prodromou Stephen J. Kron Barry Panaretou William G. Stetler-Stevenson Steve K. Landas Len Neckers Gennady Bratslavsky Dimitra Bourboulia Mehdi Mollapour

The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity, tailoring the chaperone function to specific "client" proteins. The intracellular signaling mechanisms directly regulating Aha1 association with Hsp90 remain unknown. Here, we show that c-Abl kinase phosphorylates Y223 in human Aha1 (hAha...

Journal: :Communications in agricultural and applied biological sciences 2013
K Baruah P Norouzitallab P Sorgeloos P Bossier

Journal: :Infection and immunity 2004
Gerd Haug Klaus Aktories Holger Barth

The heat shock protein Hsp90 is essential for uptake of the binary actin ADP-ribosylating toxins Clostridium perfringens iota-toxin and Clostridium difficile transferase into eukaryotic cells. Inhibition of Hsp90 by its specific inhibitor radicicol delayed intoxication of Vero cells by these toxins. A common Hsp90-dependent mechanism for their translocation is discussed.

Journal: :Biochimica et biophysica acta 1994
L F Peruski F C Neidhardt

Protein D48.5 was recognized as a heat-inducible protein of Escherichia coli during the screening of a group of random, temperature-inducible Mud-Lac fusion mutants. Physiological and genetic analysis demonstrated that (i) the structural gene for this protein, designated htpI, is a member of the sigma 32-dependent heat shock regulon, (ii) at 37 degrees C the synthesis of protein D48.5 is nearly...

2012
Mahavir Singh Joseph J. Lucas Yeong Jeong Joanne Domenico Yi Jia Junyan Han Yoo Seob Shin Katsuyuki Takeda Yoshiki Shiraishi Yi Yeong Jeong Ralf Spallek Erwin W. Gelfand

Journal: :Cell stress & chaperones 1999
R A Krebs

Heat shock proteins (Hsps) and other molecular chaperones perform diverse physiological roles. One is to facilitate, in part, organismal thermotolerance, of which the functional consequences depend on Hsp70 concentration and developmental stage in Drosophila melanogaster. To test whether an Hsp70-thermotolerance relationship is a general phenomenon within Drosophila, I assayed Hsp70 concentrati...

Journal: :cell journal 0
parvaneh mohammadi marzieh ebrahimi hossein baharvand

background: the aim of this study is to create an ex vivo model to examine the expression of two heat shock protein 70 (hsp70) family members, heat shock protein 72 (hsp72) and heat shock constitute protein 70 (hsc70), at the mrna and protein levels in differentiating corneal cells from air exposed limbal stem cells. materials and methods: limbal biopsies were cultured as explants on a cellular...

Journal: :The Journal of biological chemistry 1997
R Carranco C Almoguera J Jordano

A small heat shock protein (sHSP) gene from sunflower, Ha hsp17.6 G1, showed expression patterns that differ from what is known for members of this gene family. The mRNAs of this gene accumulated in seeds during late desiccation stages of zygotic embryogenesis but not in response to heat shock in vegetative tissues. The failure to respond to heat shock was independent of the developmental stage...

2011
Barbara Baldo Andreas Weiss Christian N. Parker Miriam Bibel Paolo Paganetti Klemens Kaupmann

Background: Molecular chaperones assist in the folding of metastable proteins implicated in neurodegenerative diseases. Results: Huntingtin is a heat shock protein 90 (Hsp90) client protein Conclusion: Hsp90 inhibition mediated degradation of soluble mutant huntingtin is independent of a cellular heat shock response Significance: Mechanisms targeting Hsp90 chaperone function may provide new tre...

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