Results 41 to 50 of about 285,190 (188)

Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone

mBio, 2020
The bacterial pathogen Mycobacterium tuberculosis is the leading cause of death by an infectious disease among humans. Here, we describe a previously uncharacterized M.
Samuel H. Becker, Kathrin Ulrich, Avantika Dhabaria, Beatrix Ueberheide, William Beavers, Eric P. Skaar, Lakshminarayan M. Iyer, L. Aravind, Ursula Jakob, K. Heran Darwin   +9 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, Barabasi, Blais, Borodina, C. Sőti, Chan, Cherian, Cowen, Csermely, Csermely, Csermely, Csermely, Donaldson, Dorogovtsev, Dukan, Fares, Ferrarini, Gavin, Goldberger, Hayflick, He, Herndon, Heydari, Himmelstein, Imai, Irish, Macario, Morimoto, Mukai, Nardai, Nardai, Nollen, P. Csermely, Paulsson, Promislow, Pál, Queitsch, Rual, Rutherford, Schwarzer, Song, Stadtman, Stelzl, Sőti, Sőti, Sőti, Sőti, von Mering, Werner-Washburne, Westerheide, White, Yam, Young, Young, Zhao, Zhu, Zou   +56 more
core   +1 more source

A Twist in Yeast: New Perspectives for Studying TDP-43 Proteinopathies in S. cerevisiae

Journal of Fungi
TAR DNA-binding protein 43 kDa (TDP-43) proteinopathies are a group of neurodegenerative diseases (NDs) characterized by the abnormal accumulation of the TDP-43 protein in neurons and glial cells.
Roberto Stella, Alessandro Bertoli, Raffaele Lopreiato, Caterina Peggion   +3 more
doaj   +1 more source

Amino-Terminal Processing of Helicobacter pylori Serine Protease HtrA: Role in Oligomerization and Activity Regulation

Frontiers in Microbiology, 2018
The HtrA family of serine proteases is found in most bacteria, and plays an essential role in the virulence of the gastric pathogen Helicobacter pylori. Secreted H.
Nicole Albrecht, Nicole Tegtmeyer, Heinrich Sticht, Joanna Skórko-Glonek, Steffen Backert   +4 more
doaj   +1 more source

Distinct transcriptional responses elicited by unfolded nuclear or cytoplasmic protein in mammalian cells

eLife, 2015
Eukaryotic cells possess a variety of signaling pathways that prevent accumulation of unfolded and misfolded proteins. Chief among these is the heat shock response (HSR), which is assumed to respond to unfolded proteins in the cytosol and nucleus alike ...
Yusuke Miyazaki, Ling-chun Chen, Bernard W Chu, Tomek Swigut, Thomas J Wandless   +4 more
doaj   +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, Nguyen, Basile, Rios, Paolo De Los, Seifert, Udo   +3 more
core   +2 more sources

Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules

eLife, 2015
RNA-protein (RNP) granules have been proposed to assemble by forming solid RNA/protein aggregates or through phase separation into a liquid RNA/protein phase. Which model describes RNP granules in living cells is still unclear.
Sonja Kroschwald, Shovamayee Maharana, Daniel Mateju, Liliana Malinovska, Elisabeth Nüske, Ina Poser, Doris Richter, Simon Alberti   +7 more
doaj   +1 more source

Protein Aggregation in the ER: Calm behind the Storm

Cells, 2021
As one of the largest organelles in eukaryotic cells, the endoplasmic reticulum (ER) plays a vital role in the synthesis, folding, and assembly of secretory and membrane proteins.
Haisen Li, Shengyi Sun
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

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