Results 41 to 50 of about 405,578 (278)
Frontiers in Molecular Biosciences, 2022 Small heat shock proteins (sHsp) are a ubiquitous group of ATP-independent chaperones found in all three domains of life. Although sHsps in bacteria and eukaryotes have been studied extensively, little information was available on their archaeal homologs
Mousam Roy +2 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.
Craig, Elisabeth A. +3 more
core +4 more sources
Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding [PDF]
, 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
Unleashing the full potential of Hsp90 inhibitors as cancer therapeutics through simultaneous inactivation of Hsp90, Grp94, and TRAP1 [PDF]
, 2020 Cancer therapeutics: Extending a drug's reach A new drug that blocks heat shock proteins (HSPs), helper proteins that are co-opted by cancer cells to promote tumor growth, shows promise for cancer treatment.
Chae, Young Chan +10 more
core +1 more source
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis [PDF]
, 1989 Mitochondrial heat-shock protein hsp60 functions in the folding of proteins imported into mitochondria. Folding occurs at the surface of hsp60 in an ATP-mediated reaction, followed by release of the bound polypeptides.
Hartl, Franz-Ulrich +3 more
core +1 more source
The role and implications of mammalian cellular circadian entrainment
FEBS Letters, EarlyView.At their most fundamental level, mammalian circadian rhythms occur inside every individual cell. To tell the correct time, cells must align (or ‘entrain’) their circadian rhythm to the external environment. In this review, we highlight how cells entrain to the major circadian cues of light, feeding and temperature, and the implications this has for our
Priya Crosby
wiley +1 more source
Journal of Hematology & OncologyHeat shock proteins are essential molecular chaperones that play crucial roles in stabilizing protein structures, facilitating the repair or degradation of damaged proteins, and maintaining proteostasis and cellular functions.
Wei-Fang Zuo +7 more
doaj +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
Integrative analysis of the heat shock response in Aspergillus fumigatus [PDF]
, 2010 Background Aspergillus fumigatus is a thermotolerant human-pathogenic mold and the most common cause of invasive aspergillosis (IA) in immunocompromised patients. Its predominance is based on several factors most of which are still unknown.
Daniela Albrecht +3 more
core +2 more sources
FEBS Letters, EarlyView.This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva +5 more
wiley +1 more source