Extracellular chaperone networks and the export of J-domain proteins

JEA Braun - Journal of Biological Chemistry, 2023 - ASBMB
An extracellular network of molecular chaperones protects a diverse array of proteins that
reside in or pass through extracellular spaces. Proteins in the extracellular milieu face …

BAG family members as mitophagy regulators in mammals

S Pattingre, A Turtoi - Cells, 2022 - mdpi.com
The BCL-2-associated athanogene (BAG) family is a multifunctional group of co-chaperones
that are evolutionarily conserved from yeast to mammals. In addition to their common BAG …

Incorporating the molecular mimicry of environmental antigens into the causality of autoimmune hepatitis

AJ Czaja - Digestive Diseases and Sciences, 2023 - Springer
Molecular mimicry between foreign and self-antigens has been implicated as a cause of
autoimmune hepatitis in experimental models and cross-reacting antibodies in patients. This …

The role of heat shock protein 70 subfamily in the hyperplastic prostate: from molecular mechanisms to therapeutic opportunities

X Fu, H Liu, J Liu, ME DiSanto, X Zhang - Cells, 2022 - mdpi.com
Benign prostatic hyperplasia (BPH) is one of the most common causes of lower urinary tract
symptoms (LUTS) in men, which is characterized by a noncancerous enlargement of the …

Tau Protein and Tauopathies: Exploring Tau Protein–Protein and Microtubule Interactions, Cross‐Interactions and Therapeutic Strategies

D Di Lorenzo - ChemMedChem, 2024 - Wiley Online Library
Tau, a microtubule‐associated protein (MAP), is essential to maintaining neuronal stability
and function in the healthy brain. However, aberrant modifications and pathological …

[HTML][HTML] Targeting chaperone modifications: Innovative approaches to cancer treatment

M Stewart, JC Schisler - Journal of Biological Chemistry, 2024 - Elsevier
Cancer and other chronic diseases are marked by alterations in the protein quality control
system, affecting the post-translational destiny of various proteins that regulate, structure …

Molecular chaperones HSP40, HSP70, STIP1, and HSP90 are involved in stabilization of Cx43

L An, H Gao, Y Zhong, Y Liu, Y Cao, J Yi, X Huang… - Cytotechnology, 2023 - Springer
To investigate the involvement of stress induced phosphoprotein 1 (STIP1), heat shock
protein (HSP) 70, and HSP90 in ubiquitination of connexin 43 (Cx43) in rat H9c2 …

Hemin competitively inhibits HSPA8 ATPase activity mitigating its foldase function

AK Pandey, V Trivedi - Archives of Biochemistry and Biophysics, 2024 - Elsevier
Hemolysis in red blood cells followed by hemoglobin degradation results in high hemin
levels in the systemic circulation. Such a level of hemin is disastrous for cells and tissues …

[HTML][HTML] Elevation of major constitutive heat shock proteins is heat shock factor independent and essential for establishment and growth of Lgl loss and Yorkie gain …

G Singh, S Chakraborty, SC Lakhotia - Cell Stress and Chaperones, 2022 - Elsevier
Cancer cells generally overexpress heat shock proteins (Hsps), the major components of
cellular stress response, to overcome and survive the diverse stresses. However, the …

New Insights into Hsp90 Structural Plasticity Revealed by cryoEM

K Minari, VH Balasco Serrão, JC Borges - BioChem, 2024 - mdpi.com
Heat Shock Protein 90 (Hsp90) acts as a crucial molecular chaperone, playing an essential
role in activating numerous signaling proteins. The intricate mechanism of Hsp90 involving …