Results 41 to 50 of about 94,343 (283)
Molecular Chaperones in Neurodegeneration [PDF]
, 2022 Neurodegenerative diseases are characterized by the degeneration of our brain cells. One of the most common neurodegenerative diseases is Alzheimer’s Disease.
Koopman, Margreet Berna
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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
doaj +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source
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
Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones [PDF]
, 2011 Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases.
Sikor, Martin
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FEBS Letters, EarlyView.Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura +2 more
wiley +1 more source
How do Chaperones Bind (Partly) Unfolded Client Proteins?
Frontiers in Molecular Biosciences, 2021 Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to ...
Iva Sučec +3 more
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The ubiquitin ligase RNF115 is required for the clearance of damaged lysosomes
FEBS Letters, EarlyView.Upon lysosomal rupture, an E3 ubiquitin ligase RNF115 translocates from the cytosol to the damaged lysosomal membrane. Moreover, RNF115 depletion impairs the clearance of damaged lysosomes, identifying it as a key regulator of lysosomal quality control.
Sae Nakanaga +3 more
wiley +1 more source
Artificial chaperones: from conventional designs to smart systems
NPG Asia MaterialsChaperones are essential for the functions of many biomacromolecules as they facilitate folding, stabilize conformation, and prevent aggregation.
Wancheng Zhang, Atsushi Maruyama
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Type III secretion chaperones : a molecular toolkit for all occasions [PDF]
, 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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