Results 101 to 110 of about 146,944 (294)

ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage [PDF]

open access: yes, 2010
Chaperone and protease systems play essential roles in cellular homeostasis and have vital functions in controlling the abundance of specific cellular proteins involved in processes such as transcription, replication, metabolism and virulence.
Butler, R.E.   +7 more
core   +3 more sources

3D Bioprinted Fat‐Myocardium Model Unravels the Role of Adipocyte Hypertrophy in Atrial Dysfunction

open access: yesAdvanced Science, EarlyView.
A human‐derived 3D bioprinted fat–myocardium model is developed to investigate how adipocyte hypertrophy drives atrial dysfunction in obesity. Palmitate‐induced adipocyte hypertrophy promotes adipose dysfunction that impairs atrial cardiomyocyte metabolism and electrophysiology through both paracrine and direct interactions. This platform recapitulates
Lara Ece Celebi, Pinar Zorlutuna
wiley   +1 more source

Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis

open access: yesCell Reports, 2019
Summary: The extracellular molecular chaperone heat shock protein 90 (eHSP90) stabilizes protease client the matrix metalloproteinase 2 (MMP2), leading to tumor cell invasion.
Alexander J. Baker-Williams   +15 more
doaj   +1 more source

Prompting Fab Yeast Surface Display Efficiency by ER Retention and Molecular Chaperon Co-expression. [PDF]

open access: yes, 2019
For antibody discovery and engineering, yeast surface display (YSD) of antigen-binding fragments (Fabs) and coupled fluorescence activated cell sorting (FACS) provide intact paratopic conformations and quantitative analysis at the monoclonal level, and ...
Ge, Xin   +7 more
core  

The structure of the PapD-PapGII pilin complex reveals an open and flexible P5 pocket [PDF]

open access: yes, 2012
P pili are hairlike polymeric structures that mediate binding of uropathogenic Escherichia coli to the surface of the kidney via the PapG adhesin at their tips.
Baga M   +48 more
core   +2 more sources

Single‐Cell Atlas of Subchondral Bone Marrow Lesions Reveals Proteostasis Dysfunction as a Druggable Mechanism for Early Osteoarthritis

open access: yesAdvanced Science, EarlyView.
This study reveals that abnormal mechanical stress downregulates the expression of HSP70 and impairs proteasome function in osteoarthritic bone cells, leading to misfolded collagen I accumulation and ER stress. When intracellular proteostasis capacity is exceeded, USP19 mediates the secretion of misfolded proteins into the extracellular space ...
Hailun Xu   +20 more
wiley   +1 more source

Mitochondrial stress in advanced fibrosis and cirrhosis associated with chronic hepatitis B, chronic hepatitis C, or nonalcoholic steatohepatitis

open access: yesHepatology, EarlyView., 2022
Adaptive mitochondrial mechanisms allow mitochondrial resilience and prevent the worsening of fibrosis, while deregulation of these mechanisms promotes the progression from no/minimal‐mild (F0‐F2) fibrosis to advanced fibrosis and cirrhosis (F3‐F4). Abstract Background and Aims Hepatitis B virus (HBV) infection causes oxidative stress (OS) and alters ...
Dimitri Loureiro   +17 more
wiley   +1 more source

Aneuploidy and proteotoxic stress in cancer [PDF]

open access: yes, 2015
Although nearly ubiquitous in cancer, aneuploidy exerts detrimental effects on human cells. We recently demonstrated that aneuploid human cells exhibit impaired heat shock factor protein 1 (HSF1) and HSP90 function, suggesting a functional link between ...
Donnelly, N., Storchova, Z.
core   +2 more sources

Gymnastics of Molecular Chaperones [PDF]

open access: yesMolecular Cell, 2010
Molecular chaperones assist folding processes and conformational changes in many proteins. In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families.
openaire   +2 more sources

Alphaviral Capsid Proteins Inhibit Stress Granule Assembly via Competitive RNA Binding With G3BP1

open access: yesAdvanced Science, EarlyView.
Stress granules exert antiviral functions. This study illustrates a conserved function of alphaviral capsid proteins in modulating stress granules. Oligomerization mediated by a helical motif coupled with a positively charged intrinsically disordered region (IDR) directly competes with G3BP1 for RNA binding, thereby disrupting G3BP1‐RNA liquid–liquid ...
Yun Zhang   +10 more
wiley   +1 more source

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