نتایج جستجو برای: heat shock protein

تعداد نتایج: 1480588  

2015
Karol Dokladny Orrin B Myers Pope L Moseley

Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as ...

Journal: :Molecules and cells 2007
Hee-Jung Kim Na Rae Hwang Kong-Joo Lee

Extracellular stresses induce heat shock response and render cells resistant to lethal stresses. Heat shock response involves induction of heat shock proteins (Hsps). Recently the roles of Hsps in neurodegenerative diseases and cancer are attracting increasing attention and have accelerated the study of heat shock response mechanism. This review focuses on the stress sensing steps, molecules in...

2015
Neysan Donnelly Zuzana Storchová

Although nearly ubiquitous in cancer, aneuploidy exerts detrimental effects on human cells. We recently demonstrated that aneuploid human cells exhibit impaired heat shock factor protein 1 (HSF1) and HSP90 function, suggesting a functional link between two recurring features of cancer cells: aneuploidy and proteotoxic stress. Further, our findings implicate HSF1 as a key factor in mitigating th...

Journal: :Atlas of Genetics and Cytogenetics in Oncology and Haematology 2014

Journal: :Current Biology 2004
Ming Der Perng Roy A Quinlan

Mutations in HSPB1 and HSPB8, members of the small heat shock protein family, have recently been shown to cause some distal motor neuropathies. Their function in motor neurones is now under scrutiny.

Journal: :Molecular microbiology 2003
Axel Mogk Elke Deuerling Sonja Vorderwülbecke Elizabeth Vierling Bernd Bukau

Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly understood. We demonstrate that sHsps of Escherichia coli, IbpA and IbpB, co-operate with ClpB and the DnaK system in vitro and in vivo, forming a functional triade of chaperones. IbpA/IbpB and ClpB support independ...

Journal: :Applied and environmental microbiology 1994
J Michiels C Verreth J Vanderleyden

High soil temperatures in tropical areas limit nodulation and dinitrogen fixation by strains of Rhizobium. Several heat-tolerant bean-nodulating Rhizobium strains have been isolated previously. However, the basis of their resistance to heat remains unknown. In this study, we compared the effects of heat on symbiotic nitrogen fixation, cell survival, amino acid uptake, and protein synthesis in a...

Journal: :Biochemistry 1998
S Diamant P Goloubinoff

Heat-shock proteins DnaK, DnaJ, and GrpE (KJE) from Escherichia coli constitute a three-component chaperone system that prevents aggregation of denatured proteins and assists the refolding of proteins in an ATP-dependent manner. We found that the rate of KJE-mediated refolding of heat- and chemically denatured proteins is decreased at high temperatures. The efficiency and reversibility of prote...

2015
Michael Howell Howard Brickner Violaine D. Delorme-Walker Justin Choi Jean-Michel Saffin Daniel Miller Andreas Panopoulos Céline DerMardirossian Arun Fotedar Robert L. Margolis Rati Fotedar

We previously identified Waf1 Cip1 stabilizing protein 39 (WISp39) as a binding partner for heat shock protein 90 (Hsp90). We now report that WISp39 has an essential function in the control of directed cell migration, which requires WISp39 interaction with Hsp90. WISp39 knockdown (KD) resulted in the loss of directional motility of mammalian cells and profound changes in cell morphology, includ...

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