Results 41 to 50 of about 3,296,549 (170)
F1000Research, 2015 Proteins must adopt a defined three-dimensional structure in order to gain functional activity, or must they? An ever-increasing number of intrinsically disordered proteins and amyloid-forming polypeptides challenge this dogma. While molecular chaperones
Wilson Jeng +4 more
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Life, 2020 The property of molecular chaperones to dissolve protein aggregates of Parkinson-related α-synuclein has been known for some time. Recent findings point to an even more active role of molecular chaperones preventing the transformation of α-synuclein into
Emelie E. Aspholm +2 more
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Hsp70 in mitochondrial biogenesis [PDF]
, 1994 The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
Stuart, Rosemary A. +2 more
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Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria [PDF]
, 1994 ATP dependent proteolytic degradation of misfolded proteins in the mitochondrial matrix is mediated by the PIM1 protease and depends on the molecular chaperone proteins mt-hsp70 and Mdj1p. Chaperone function is essential to maintain misfolded proteins in
Dyck, Luc van +4 more
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Malaria Journal, 2010 Background Molecular chaperones have been shown to be important in the growth of the malaria parasite Plasmodium falciparum and inhibition of chaperone function by pharmacological agents has been shown to abrogate parasite growth.
Pallavi Rani +4 more
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RNA can function as molecular chaperone for RNA folding
Giant, 2020 RNAs can mimic the information storage, replication and catalysis functions of DNAs and proteins, providing physical evidence for the widely accepted RNA world hypothesis that RNA alone constitutes earlier life forms.
Zhi-Chao Lei +8 more
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Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease
Frontiers in Pharmacology, 2019 Misfolding, aggregation, and aberrant accumulation of proteins are central components in the progression of neurodegenerative disease. Cellular molecular chaperone systems modulate proteostasis, and, therefore, are primed to influence aberrant protein ...
Jack M. Webster +3 more
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Type III secretion chaperones : a molecular toolkit for all occasions
, 2010 Common to many bacteria is the ability to establish a symbiotic relationship or to evade innate immune responses of an animal, plant, fish or insect host. Most often this capacity is mediated by a type III secretion system (T3SS).
Francis, Matthew S
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Emerging roles of J proteins in neurodegenerative disorders
Neurobiology of Disease, 2008 Several families of proteins called molecular chaperones comprise the cellular machinery that has evolved to maintain protein structure and eliminate misfolded proteins in the cell. In experimental animal models, chaperones have been shown to be powerful
Sarah J. Gibbs, Janice E.A. Braun
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Discovery of molecular chaperones
Cell Stress & Chaperones, 1996 When I wish to provoke my colleagues at the University of Warwick I invite them to challenge my contention that there have been no really major conceptual advances in biochemistry since 1963, when chemiosmosis and allostery illuminated the cellular scene.
openaire +3 more sources