Results 31 to 40 of about 3,371,845 (256)

Conformational Transitions of Heat Shock Proteins: The Case of Hsp90 [PDF]

open access: yesBiophysical Journal, 2012
The most abundant cellular protein, Hsp90, partakes in many biological pathways, not only in times of induced stress, but also under normal physiological conditions. Its role in controlling proteostasis, by assisting in protein folding and reducing aggregation, together with its direct involvement in cancer cell survival and neurological disorders ...
Simunovic, Mijo, Voth, Gregory A.
openaire   +1 more source

Heat Shock Proteins in Cancer: Mechanisms and Therapeutic Targeting. [PDF]

open access: yesMedComm (2020)
This review illustrates heat shock proteins (HSPs) as central regulators of cancer metabolic reprogramming. By stabilizing key metabolic enzymes and coordinating glycolysis, oxidative phosphorylation, redox homeostasis, and stress adaptation, HSPs support tumor growth, metastasis, and therapeutic resistance. Targeting HSP networks may therefore provide
Ma S   +5 more
europepmc   +2 more sources

Arabidopsis HEAT SHOCK TRANSCRIPTION FACTORA1b overexpression enhances water productivity, resistance to drought, and infection [PDF]

open access: yes, 2013
Heat-stressed crops suffer dehydration, depressed growth, and a consequent decline in water productivity, which is the yield of harvestable product as a function of lifetime water consumption and is a trait associated with plant growth and development ...
Schöffl, F.   +46 more
core   +1 more source

Nuclear HSP90 and HSP70 in COPD patients treated with formoterol or formoterol and corticosteroids

open access: yesEuropean Journal of Medical Research, 2009
Objective Heat shock proteins assist cellular protein folding and are required for the normal activity of steroid receptors. In this study we assessed nuclear HSP90 and HSP70 proteins and mRNA levels in cells isolated from induced sputum of chronic ...
Holownia A   +4 more
doaj   +1 more source

The Human TPR Protein TTC4 Is a Putative Hsp90 Co-Chaperone Which Interacts with CDC6 and Shows Alterations in Transformed Cells. [PDF]

open access: yes, 2008
BACKGROUND: The human TTC4 protein is a TPR (tetratricopeptide repeat) motif-containing protein. The gene was originally identified as being localized in a genomic region linked to breast cancer and subsequent studies on melanoma cell lines revealed ...
Bennett, D   +8 more
core   +2 more sources

Non-enzymatic cleavage of Hsp90 by oxidative stress leads to actin aggregate formation: A novel gain-of-function mechanism

open access: yesRedox Biology, 2019
Aging is accompanied by the accumulation of oxidized proteins. To remove them, cells employ the proteasomal and autophagy-lysosomal systems; however, if the clearance rate is inferior to its formation, protein aggregates form as a hallmark of ...
José Pedro Castro   +5 more
doaj   +1 more source

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

open access: yes, 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.
Herrmann, Johannes M.   +3 more
core   +2 more sources

Targeting GRP75 improves HSP90 inhibitor efficacy by enhancing p53-mediated apoptosis in hepatocellular carcinoma. [PDF]

open access: yesPLoS ONE, 2014
Heat shock protein 90 (HSP90) inhibitors are potential drugs for cancer therapy. The inhibition of HSP90 on cancer cell growth largely through degrading client proteins, like Akt and p53, therefore, triggering cancer cell apoptosis.
Weiwei Guo   +8 more
doaj   +1 more source

Cell Stress Induced Stressome Release Including Damaged Membrane Vesicles and Extracellular HSP90 by Prostate Cancer Cells

open access: yesCells, 2020
Tumor cells exhibit therapeutic stress resistance-associated secretory phenotype involving extracellular vesicles (EVs) such as oncosomes and heat shock proteins (HSPs). Such a secretory phenotype occurs in response to cell stress and cancer therapeutics.
Takanori Eguchi   +8 more
doaj   +1 more source

Hsp90: From Cellular to Organismal Proteostasis

open access: yesCells, 2022
Assuring a healthy proteome is indispensable for survival and organismal health. Proteome disbalance and the loss of the proteostasis buffer are hallmarks of various diseases.
Milán Somogyvári   +2 more
doaj   +1 more source

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