Results 21 to 30 of about 270,723 (313)

Interaction of human heat shock protein 70 with tumor-associated peptides [PDF]

, 2009
Molecular chaperones of the heat shock protein 70 (Hsp70) family play a crucial role in the presentation of exogenous antigenic peptides by antigen-presenting cells (APCs).
Manzenrieder, Florian, Elfriede Noessner, Noessner, Elfriede, Bendz, H., Buchner, J., Bendz, Henriette, Johannes Buchner, Nößner, E., Issels, Rolf D., Florian Manzenrieder, Kessler, H., Rolf D. Issels, Pandya, M.J., Manzenrieder, F., Issels, R.D., Kessler, Horst, Pandya, Maya J., Henriette Bendz, Maya J. Pandya, Buchner, Johannes, Horst Kessler   +20 more
core   +1 more source

Expression of Hsp72 in Lymphocytes in Patients with Febrile Convulsion

Kaohsiung Journal of Medical Sciences, 2005
The pathophysiology of febrile convulsion, the most common childhood neurologic disease, remains unclear. In this study, we investigated what role a heat shock protein plays in this disease.
Lung-Chang Lin
doaj   +1 more source

Heat shock induces expression of OSTC/DC2, a novel subunit of oligosaccharyltransferase, in vitro and in vivo

Kaohsiung Journal of Medical Sciences, 2014
Mammalian oligosaccharyltransferase complex subunit OSTC/DC2 protein has recently been shown to be a new subunit of the oligosaccharyltransferase; however, its physiological role is still unclear.
Chien-Ming Chen, Chao-Neng Tseng, Jonathan J. Cho, Ya-Zhe Lee, Chiu-Li Kao, Yuan-Bin Cheng, Yi-Ren Hong, Chung-Lung Cho   +7 more
doaj   +1 more source

Heat-Shock Proteins in Neuroinflammation [PDF]

Frontiers in Pharmacology, 2019
The heat-shock response, one of the main pro-survival mechanisms of a living organism, has evolved as the biochemical response of cells to cope with heat stress. The most well-characterized aspect of the heat-shock response is the accumulation of a conserved set of proteins termed heat-shock proteins (HSPs).
Brigitta Dukay, Brigitta Dukay, Bálint Csoboz, Melinda E. Tóth   +3 more
openaire   +4 more sources

Identification of proteins sensitive to thermal stress in human neuroblastoma and glioma cell lines. [PDF]

PLoS ONE, 2012
Heat-shock is an acute insult to the mammalian proteome. The sudden elevation in temperature has far-reaching effects on protein metabolism, leads to a rapid inhibition of most protein synthesis, and the induction of protein chaperones.
Guilian Xu, Stanley M Stevens, Firas Kobeissy, Hilda Brown, Scott McClung, Mark S Gold, David R Borchelt   +6 more
doaj   +1 more source

Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA [PDF]

, 1994
Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix.
W Neupert, Herrmann, Johannes M., Stuart, Rosemary A., Neupert, Walter, J M Herrmann, Craig, Elisabeth A., E A Craig, R A Stuart   +7 more
core   +1 more source

Heat shock induces rapid resorption of primary cilia [PDF]

, 2012
Primary cilia are involved in important developmental and disease pathways, such as the regulation of neurogenesis and tumorigenesis. They function as sensory antennae and are essential in the regulation of key extracellular signalling systems.
Ashworth, R, Prodromou, NV, Osborn, DP, Chapple, JP, Beales, PL, Knight, MM, Thompson, CL, Cogger, KF   +7 more
core   +1 more source

Neural functions of small heat shock proteins

Neural Regeneration Research, 2022
Stress response is a cellular widespread mechanism encoded by a common protein program composed by multiple cellular factors that converge in a defense reaction to protect the cell against damage. Among many mechanisms described, heat shock proteins were
Teresa de los Reyes, Sergio Casas-Tintó
doaj   +1 more source

Immunotherapeutic targeting of membrane Hsp70-expressing tumors using recombinant human granzyme B [PDF]

, 2012
Background: We have previously reported that human recombinant granzyme B (grB) mediates apoptosis in membrane heat shock protein 70 (Hsp70)-positive tumor cells in a perforin-independent ...
Axel Walch, Alan G Pockley, Foulds, GA, Pockley, A. G., Foulds, G. A., Doss, B. T., Pockley, AG, Stangl Stefan, Kirschner, A., Foulds, G.A., Gehrmann, M., Multhoff, G., Walch Axel, Doß Brigitte T., Walch, A.K., Kirschner, A, Gehrmann Mathias, Gemma A Foulds, Stangl, S., Walch, A., Doß, B.T., Pockley, A.G., Multhoff, G, Sievert Wolfgang, Stefan Stangl, Stangl, S, Pockley Alan G., Mathias Gehrmann, Multhoff Gabriele, Sievert, W, Sievert, W., Foulds Gemma A., Andreas Kirschner, Kirschner Andreas, Wolfgang Sievert, Gehrmann, M, Gabriele Multhoff, Doß, BT, Brigitte T Doss, Walch, A   +39 more
core   +1 more source

LPS-induced delayed preconditioning is mediated by Hsp90 and involves the heat shock response in mouse kidney. [PDF]

PLoS ONE, 2014
We and others demonstrated previously that preconditioning with endotoxin (LPS) protected from a subsequent lethal LPS challenge or from renal ischemia-reperfusion injury (IRI).
Tamás Kaucsár, Csaba Bodor, Mária Godó, Csaba Szalay, Csaba Révész, Zalán Németh, Miklós Mózes, Gábor Szénási, László Rosivall, Csaba Sőti, Péter Hamar   +10 more
doaj   +1 more source