Results 41 to 50 of about 147,841 (291)

Heat shock proteins in health and disease: therapeutic targets or therapeutic agents? [PDF]

, 2001
For many years, heat shock or stress proteins have been regarded as intracellular molecules that have a range of housekeeping and cytoprotective functions, only being released into the extracellular environment in pathological situations such as necrotic
Pockley, A.G.
core   +1 more source

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

FEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li, Pedro A. Sánchez‐Murcia, Bernd Nidetzky   +2 more
wiley   +1 more source

The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution [PDF]

, 2013
NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a ...
Andrew Bowman, Andrew Stirling, Andrews, Berndsen, Bonangelino, Bowman, Colin M. Hammond, Das, David A. Robinson, David G. Norman, Del Rosario, Dmitri I. Svergun, Driscoll, D’Arcy, D’Arcy, Fillingham, Fleissner, Hagelueken, Hansen, Hassane El-Mkami, Ishimi, Jeschke, Kolonko, Konarev, Krogan, Kuryan, Laskey, McBryant, McBryant, Milov, Newman, Noda, Ohkuni, Park, Park, Petoukhov, Pramila, Ransom, Richard Ward, Roessle, Schwieters, Selth, Selth, Su, Svergun, Svergun, Tang, Tang, Tom Owen-Hughes, Toth, Tsubota, Ward, Weifeng Shang, Xue   +53 more
core   +8 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

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, Trina Dykstra‐MacPherson, Mathias A. Bell, Peter L. Davies, Ruby May A. Sullan   +4 more
wiley   +1 more source

Artificial chaperones: from conventional designs to smart systems

NPG Asia Materials
Chaperones are essential for the functions of many biomacromolecules as they facilitate folding, stabilize conformation, and prevent aggregation.
Wancheng Zhang, Atsushi Maruyama
doaj   +1 more source

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

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, Shin‐ichi Tate, Kyota Yasuda   +2 more
wiley   +1 more source

Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation

Acta Neuropathologica Communications, 2022
The most common inherited cause of two genetically and clinico-pathologically overlapping neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), is the presence of expanded GGGGCC intronic hexanucleotide ...
Feilin Liu, Dmytro Morderer, Melissa C. Wren, Sara A. Vettleson-Trutza, Yanzhe Wang, Benjamin E. Rabichow, Michelle R. Salemi, Brett S. Phinney, Björn Oskarsson, Dennis W. Dickson, Wilfried Rossoll   +10 more
doaj   +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, Beate Bersch, Paul Schanda, Paul Schanda   +3 more
doaj   +1 more source

The Chlamydia trachomatis Type III Secretion Chaperone Slc1 Engages Multiple Early Effectors, Including TepP, a Tyrosine-phosphorylated Protein Required for the Recruitment of CrkI-II to Nascent Inclusions and Innate Immune Signaling [PDF]

, 2014
Chlamydia trachomatis, the causative agent of trachoma and sexually transmitted infections, employs a type III secretion (T3S) system to deliver effector proteins into host epithelial cells to establish a replicative vacuole.
Bastidas, Robert J., Carpenter, Victoria K., Chen, Yi-Shan, Plano, Gregory V., Richards, Kristian L., Saka, Hector Alex, Valdivia, Raphael H.   +6 more
core   +3 more sources