Results 31 to 40 of about 158,532 (263)

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

open access: yesMolecules, 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   +2 more
doaj   +1 more source

Extracellular Chaperones

open access: yes, 2010
The maintenance of the levels and correct folding state of proteins (proteostasis) is a fundamental prerequisite for life. Life has evolved complex mechanisms to maintain proteostasis and many of these that operate inside cells are now well understood.
Dabbs, Rebecca A   +4 more
openaire   +5 more sources

Co-chaperones are limiting in a depleted chaperone network [PDF]

open access: yesCellular and Molecular Life Sciences, 2010
To probe the limiting nodes in the chaperoning network which maintains cellular proteostasis, we expressed a dominant negative mutant of heat shock factor 1 (dnHSF1), the regulator of the cytoplasmic proteotoxic stress response. Microarray analysis of non-stressed dnHSF1 cells showed a two- or more fold decrease in the transcript level of 10 genes ...
Heldens, L.   +6 more
openaire   +4 more sources

Inhibitors of the AAA+ Chaperone p97

open access: yesMolecules, 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   +3 more
doaj   +1 more source

Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone

open access: yesmBio, 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   +9 more
doaj   +1 more source

Molecular Chaperones and Co-Chaperones in Parkinson Disease [PDF]

open access: yesThe Neuroscientist, 2012
Parkinson disease, a progressive neurodegenerative disorder, is caused by the pathological accumulation of proteins, including the ubiquitous presynaptic protein α-synuclein. Alterations in the metabolism of α-synuclein have clearly been linked to neurodegeneration, and early steps in the pathological sequence of this protein include the formation of ...
Hemi, Dimant   +2 more
openaire   +2 more sources

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

open access: yesJournal 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   +3 more
doaj   +1 more source

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

open access: yesFrontiers 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   +4 more
doaj   +1 more source

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

open access: yeseLife, 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   +4 more
doaj   +1 more source

Chaperone-assisted translocation [PDF]

open access: yesPhysical Biology, 2004
24 pages, 3 figures, LaTeX (IOP class file)
Ambjørnsson, T, Metzler, R
openaire   +3 more sources

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