Results 41 to 50 of about 227,395 (295)

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, April L. Darling, Vladimir N. Uversky, Laura J. Blair   +3 more
doaj   +1 more source

Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone [PDF]

, 2012
Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln).
Aksam, Antonenkov, Arnold, Bartoszewska, Bender, Bota, Buchner, Dobson, Ellis, Fraaije, Franke, Goldberg, Guinier, Hanson, Hartl, Hillenga, Islinger, Iyer, Jaenicke, Jahn, Kiel, Kiel, Kikuchi, Kozin, Lee, Lingard, Liu, Meijer, Nettleship, Nijland, Okumoto, Omi, Opaliński, Paraszkiewicz, Petoukhov, Petoukhov, Petoukhov, Powers, Quiocho, Reeder, Rep, Roessle, Roudiak, Sambrook, Sauer, Stahlberg, Steinberg, Svergun, Tyedmers, van Dijken, van Roermund, Venkatesh, Volkov, von Janowsky, Wagner, Walton, Wanders, Waterham, West   +58 more
core   +4 more sources

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

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

Aggregation Prevention Assay for Chaperone Activity of Proteins Using Spectroflurometry

Bio-Protocol, 2017
The ability to stabilize other proteins against thermal aggregation is one of the major characteristics of chaperone proteins. Molecular chaperones bind to nonnative conformations of proteins.
Manish Bhuwan, Madhuri Suragani, Nasreen Ehtesham, Seyed Hasnain   +3 more
doaj   +1 more source

An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated RidA

Redox Biology, 2022
Under physiological conditions, Escherichia coli RidA is an enamine/imine deaminase, which promotes the release of ammonia from reactive enamine/imine intermediates.
Marharyta Varatnitskaya, Julia Fasel, Alexandra Müller, Natalie Lupilov, Yunlong Shi, Kristin Fuchs, Marco Krewing, Christoph Jung, Timo Jacob, Barbara Sitek, Julia E. Bandow, Kate S. Carroll, Eckhard Hofmann, Lars I. Leichert   +13 more
doaj   +1 more source

Amyloid prions in fungi [PDF]

, 2016
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi, Aguzzi, Aigle, Alberti, Aron, Balguerie, Ball, Bardill, Baudin-Baillieu, Baxa, Baxa, Borchsenius, Brachmann, Bradley, Brown, Byers, Cai, Chakrabortee, Chen, Chernoff, Collinge, Coustou, Coustou-Linares, Cox, Daskalov, Daskalov, Daskalov, Daskalov, Derkatch, Derkatch, Derkatch, Diaz-Avalos, DiSalvo, Douglas, Eichner, Espinosa Angarica, Fan, Garcia, Glover, Glover, Gorkovskiy, Griswold, Habenstein, Halfmann, Halfmann, Harrison, Higurashi, Holmes, Huang, Jarosz, Jarosz, Jung, Kabir, Kajava, Kajava, Kelly, King, King, Koch, Kochneva-Pervukhova, Krishnan, Kryndushkin, Kumar, Kunz, Lancaster, Li, Lum, Malato, Masel, Masison, Masison, Mathur, McGlinchey, Mizuno, Nakayashiki, Nelson, Newnam, Ohhashi, Patel, Patino, Paushkin, Prusiner, Rajon, Ritter, Rizet, Roberts, Ross, Ross, Schlieker, Schlumpberger, Sen, Seuring, Shewmaker, Shorter, Sondheimer, Sondheimer, Speldewinde, Stein, Taneja, Tapia, Tessier, Tipton, Tompa, Toyama, True, True, Tsai, Tycko, Tyedmers, Uptain, Van Melckebeke, Verges, Wan, Wasmer, Watts, Westergard, Wickner, Wickner, Wickner, Wickner, Wickner, Wickner, Zhou   +122 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, Trina Dykstra‐MacPherson, Mathias A. Bell, Peter L. Davies, Ruby May A. Sullan   +4 more
wiley   +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

Universal Stress Protein exhibits a redox-dependent chaperone function in Arabidopsis and enhances plant tolerance to heat shock and oxidative stress

Frontiers in Plant Science, 2015
Although a wide range of physiological information on Universal Stress Proteins (USPs) is available from many organisms, their biochemical and molecular functions remain unidentified.
Jung eYoung Jun, Sarah Mae Boyles Melencion, Lee eEun Seon, Park eJoung Hun, Cresilda Vergara Alinapon, Hun Taek eOh, Dae-Jin eYun, Yong Hun eChi, Sang Yeol eLee   +8 more
doaj   +1 more source