Results 31 to 40 of about 86,733 (300)

Developmental and hyperthermia-induced expression of the heat shock proteins HSP60 and HSP70 in tissues of the housefly Musca domestica: an in vitro study

open access: yesGenetics and Molecular Biology, 2007
The expression pattern of two major chaperones, the heat shock proteins (HSPs) HSP60 and HSP70 was studied in vitro in tissues of the housefly Musca domestica during larval and adult stages of development to identify their immunological relatives and ...
Sunita Sharma   +2 more
doaj   +1 more source

Bacterial Infection Elicits Heat Shock Protein 72 Release from Pleural Mesothelial Cells [PDF]

open access: yes, 2013
Heat shock protein 70 (HSP70) has been implicated in infection-related processes and has been found in body fluids during infection. This study aimed to determine whether pleural mesothelial cells release HSP70 in response to bacterial infection in vitro
Bielsa, S   +8 more
core   +1 more source

Membrane-anchored heat-shock protein 70 (Hsp70) in cancer

open access: yesCancer Letters, 2020
Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70 family of molecular chaperones and plays a central role in protein homeostasis. The main function of Hsp70 is to protect cells from physiological, pathological and environmental insults, as it assists an ATP-dependent manner the process of protein folding.
Elmallah, Mohammed I.Y.   +5 more
openaire   +6 more sources

Mitochondrial stress in advanced fibrosis and cirrhosis associated with chronic hepatitis B, chronic hepatitis C, or nonalcoholic steatohepatitis

open access: yesHepatology, EarlyView., 2022
Adaptive mitochondrial mechanisms allow mitochondrial resilience and prevent the worsening of fibrosis, while deregulation of these mechanisms promotes the progression from no/minimal‐mild (F0‐F2) fibrosis to advanced fibrosis and cirrhosis (F3‐F4). Abstract Background and Aims Hepatitis B virus (HBV) infection causes oxidative stress (OS) and alters ...
Dimitri Loureiro   +17 more
wiley   +1 more source

Heat shock protein and gene regulation in goats during heat stress

open access: yesIndian Journal of Animal Sciences, 2021
Heat shock proteins (HSPs), also known as molecular chaperons are prominent stress markers. Heat shock proteins consist of highly conserved protein expressed at the time of stress, and play an important role in adaptation to the environmental stress ...
UMESH BABU CHAUDHARY   +4 more
doaj   +1 more source

Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates [PDF]

open access: yes, 2017
The 70 kDa Heat Shock Proteins Hsp70 have several essential functions in living systems, such as protecting cells against protein aggregation, assisting protein folding, remodeling protein complexes and driving the translocation into organelles.
Hartich, David   +3 more
core   +2 more sources

Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70) [PDF]

open access: yesCurrent Topics in Medicinal Chemistry, 2016
Heat shock protein 70 (Hsp70) is a molecular chaperone that plays critical roles in protein homeostasis. Hsp70's chaperone activity is coordinated by intra-molecular interactions between its two domains, as well as inter-molecular interactions between Hsp70 and its co-chaperones.
Li, Xiaokai   +3 more
openaire   +4 more sources

Expression of Heat Shock Protein 70 Is Insufficient To Extend Drosophila melanogaster Longevity

open access: yesG3: Genes, Genomes, Genetics, 2019
It has been known for over 20 years that Drosophila melanogaster flies with twelve additional copies of the hsp70 gene encoding the 70 kD heat shock protein lives longer after a non-lethal heat treatment.
Chengfeng Xiao   +7 more
doaj   +1 more source

Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding [PDF]

open access: yes, 1994
Mdj1p, a novel member of the DnaJ family, is a heat shock protein that is associated with the inner membrane of mitochondria of Saccharomyces cerevisiae.
Amin   +63 more
core   +1 more source

Binding of Heat-Shock Protein 70 (hsp70) to Tubulin

open access: yesArchives of Biochemistry and Biophysics, 1994
Binding of heat-shock protein (hsp70) to polymerized tubulin has been investigated by in vitro experiments. The tubulin region involved in binding to hsp70 corresponds to the carboxy-terminal residues 431-444, also involved in the association with other microtubule-associated proteins (MAPs).
Sánchez, Carlos   +4 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy