Results 51 to 60 of about 287,054 (305)
Enzymes as chaperones and chaperones as enzymes
FEBS Letters, 1998 Chaperones and foldases are two groups of accessory proteins which assist maturation of nascent peptides into functional proteins in cells. Protein disulfide isomerase, a foldase, and ATP‐dependent proteases, responsible for degradation of misfolded proteins in cells, both have intrinsic chaperone activities.
Wang, Chih-Chen, Tsou, Chen-Lu
openaire +2 more sources
Structural biology of ferritin nanocages
FEBS Letters, EarlyView.Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley +1 more source
Super Spy variants implicate flexibility in chaperone action
eLife, 2014 Experimental study of the role of disorder in protein function is challenging. It has been proposed that proteins utilize disordered regions in the adaptive recognition of their various binding partners.
Shu Quan +8 more
doaj +1 more source
Differential Interactions of Molecular Chaperones and Yeast Prions
Journal of Fungi, 2022 Baker’s yeast Saccharomyces cerevisiae is an important model organism that is applied to study various aspects of eukaryotic cell biology. Prions in yeast are self-perpetuating heritable protein aggregates that can be leveraged to study the interaction ...
Yury A. Barbitoff +2 more
doaj +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
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor. [PDF]
, 2019 Molecular chaperones such as Hsp40 and Hsp70 hold the androgen receptor (AR) in an inactive conformation. They are released in the presence of androgens, enabling transactivation and causing the receptor to become aggregation-prone.
Banduseela, Varuna C +19 more
core +2 more sources
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
Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
eLife, 2014 70-kDa Heat shock proteins are ATP-driven molecular chaperones that perform a myriad of essential cellular tasks. Although structural and biochemical studies have shed some light on their functional mechanism, the fundamental issue of the role of energy ...
Paolo De Los Rios, Alessandro Barducci
doaj +1 more source
A Chaperone-Like Role for EBI3 in Collaboration With Calnexin Under Inflammatory Conditions
Frontiers in Immunology, 2021 The interleukin-6 (IL-6)/IL-12 family of cytokines plays critical roles in the induction and regulation of innate and adaptive immune responses. Among the various cytokines, only this family has the unique characteristic of being composed of two distinct
Aruma Watanabe +12 more
doaj +1 more source
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