Results 51 to 60 of about 4,011,919 (357)
Modulation of Amyloid States by Molecular Chaperones.
Cold Spring Harbor Perspectives in Biology, 2019 Aberrant protein aggregation is a defining feature of most neurodegenerative diseases. During pathological aggregation, key proteins transition from their native state to alternative conformations, which are prone to oligomerize into highly ordered ...
A. Wentink +2 more
semanticscholar +1 more source
Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates [PDF]
, 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
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
doaj +1 more source
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
doaj +1 more source
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
doaj +1 more source
Ydj1 governs fungal morphogenesis and stress response, and facilitates mitochondrial protein import via Mas1 and Mas2 [PDF]
, 2017 We thank Zhen-Yuan Lin for help in the preparation of the AP-MS samples, and Cathy Collins for technical assistance. MDL is supported by a Sir Henry Wellcome Postdoctoral Fellowship (Wellcome Trust 096072), LEC is supported by a Canada Research Chair in ...
Bohovych, Iryna +7 more
core +4 more sources
Hsp70 chaperones: Cellular functions and molecular mechanism
Cellular and Molecular Life Sciences, 2005 .Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short ...
M. Mayer, B. Bukau
semanticscholar +1 more source
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
doaj +1 more source
Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.
Biochemical Journal, 2019 The Hsp70 family of chaperones works with its co-chaperones, the nucleotide exchange factors and J-domain proteins, to facilitate a multitude of cellular functions.
Eugenia M. Clerico +5 more
semanticscholar +1 more source
Aging cellular networks: chaperones as major participants
, 2006 We increasingly rely on the network approach to understand the complexity of cellular functions. Chaperones (heat shock proteins) are key "networkers", which have among their functions to sequester and repair damaged protein. In order to link the network
Agoston +56 more
core +1 more source