Results 41 to 50 of about 287,054 (305)

Inhibitors of the AAA+ Chaperone p97

Molecules, 2015
It is remarkable that a pathway as ubiquitous as protein quality control can be targeted to treat cancer. Bortezomib, an inhibitor of the proteasome, was first approved by the US Food and Drug Administration (FDA) more than 10 years ago to treat ...
Eli Chapman, Nick Maksim, Fabian de la Cruz, James J. La Clair   +3 more
doaj   +1 more source

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

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

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

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

Fluctuations in Polymer Translocation

, 2010
We investigate a model of chaperone-assisted polymer translocation through a nanopore in a membrane. Translocation is driven by irreversible random sequential absorption of chaperone proteins that bind to the polymer on one side of the membrane.
Abramowitz M, Alberts B, Ambjörnsson T, Ambjörnsson T, Antal T, de Duve C, Dembo A, Derrida B, D’Orsogna M R, Feynman R P, Goursat E J B, Howard J, K Mallick, Krapivsky P L, Kurchan J, Landau L D, Montroll E W, Nelson P, P L Krapivsky, Redner S, Van Kampen N G, Watson J D   +21 more
core   +3 more sources

Wrapping the alpha-crystallin domain fold in a chaperone assembly [PDF]

, 2005
Small heat shock proteins (sHsps) are oligomers that perform a protective function by binding denatured proteins. Although ubiquitous, they are of variable sequence except for a C-terminal similar to 90-residue "alpha-crystallin domain".
Basha, Basha, Benitez, Benndorf, Bova, Brunger, Bullard, Cashikar, Chen, Christine Slingsby, De Jong, De La Fortelle, Ding, Doublié, Eddy, Ehrnsperger, Evans, French, Fu, Giese, Guido Kappé, Haslbeck, Haslbeck, Head, Heger, Horwitz, Hsu, Irobi, Kappe, Kappé, Kim, Kim, Laskowski, Lee, Leslie, Lindner, MacRae, Mao, McManus, McRee, Merckelbach, Mogk, Mounier, Nene, Orengo, Perng, Rekas, Robin Stamler, Schneider, Sobott, Stromer, Studer, Theriault, Valdez, Van Montfort, van Montfort, Wilbert Boelens, Zourlidou   +57 more
core   +1 more source