Results 21 to 30 of about 153,321 (216)

Effects of Signal Peptide and Chaperone Co-Expression on Heterologous Protein Production in Escherichia coli

Molecules, 2023
Various host systems have been employed to increase the yield of recombinant proteins. However, some recombinant proteins were successfully produced at high yields but with no functional activities. To achieve both high protein yield and high activities,
Juntratip Jomrit, Suhardi Suhardi, Pijug Summpunn   +2 more
doaj   +1 more source

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

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

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

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