Mitochondrial HSP70 chaperone system—the influence of post-translational modifications and involvement in human diseases

H Havalová, G Ondrovičová, B Keresztesová… - International journal of …, 2021 - mdpi.com
Since their discovery, heat shock proteins (HSPs) have been identified in all domains of life,
which demonstrates their importance and conserved functional role in maintaining protein …

Molecular Chaperones of Leishmania: Central Players in Many Stress‐Related and ‐Unrelated Physiological Processes

JM Requena, AM Montalvo… - BioMed research …, 2015 - Wiley Online Library
Molecular chaperones are key components in the maintenance of cellular homeostasis and
survival, not only during stress but also under optimal growth conditions. Folding of nascent …

Biodegradation Mechanisms of Patulin in Candida guilliermondii: An iTRAQ-Based Proteomic Analysis

Y Chen, HM Peng, X Wang, BQ Li, MY Long, SP Tian - Toxins, 2017 - mdpi.com
Patulin, a potent mycotoxin, contaminates fruits and derived products worldwide, and is a
serious health concern. Several yeast strains have shown the ability to effectively degrade …

[HTML][HTML] Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings …

PR Dores-Silva, DM Cauvi, ALS Coto… - Cell Stress and …, 2021 - Elsevier
Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis
by participating in an array of biological processes. In addition, HSP play an important role in …

Human mitochondrial Hsp70 (mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization

PR Dores-Silva, LRS Barbosa, CHI Ramos, JC Borges - PloS one, 2015 - journals.plos.org
The human mitochondrial Hsp70, also called mortalin, is of considerable importance for
mitochondria biogenesis and the correct functioning of the cell machinery. In the …

Molecular cochaperones: tumor growth and cancer treatment

SK Calderwood - Scientifica, 2013 - Wiley Online Library
Molecular chaperones play important roles in all cellular organisms by maintaining the
proteome in an optimally folded state. They appear to be at a premium in cancer cells whose …

[HTML][HTML] Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain

PR Dores-Silva, DM Cauvi, ALS Coto… - Cell Stress and …, 2020 - Elsevier
Heat shock proteins (HSPs) are ubiquitous polypeptides expressed in all living organisms
that participate in several basic cellular processes, including protein folding, from which their …

Modified enzyme-linked immunosorbent assay strategy using graphene oxide sheets and gold nanoparticles functionalized with different antibody types

H Lin, Y Liu, J Huo, A Zhang, Y Pan, H Bai… - Analytical …, 2013 - ACS Publications
Gold nanoparticles (GNPs) and graphene oxide (GO) sheets are excellent nano carriers in
many analytical methods. In this study, a modified enzyme-linked immunosorbent assay …

Structural characterization of the human DjC20/HscB cochaperone in solution

AL de Souza Coto, AA Pereira, SD Oliveira… - … et Biophysica Acta (BBA …, 2024 - Elsevier
J-domain proteins (JDPs) form a very large molecular chaperone family involved in
proteostasis processes, such as protein folding, trafficking through membranes and …

Mortalin restricts porcine epidemic diarrhea virus entry by downregulating clathrin-mediated endocytosis

B Fan, L Zhu, X Chang, J Zhou, R Guo, Y Zhao… - Veterinary …, 2019 - Elsevier
Clathrin-mediated endocytosis is a mechanism used for the invasion of cells by a variety of
viruses. Mortalin protein is involved in a variety of cellular functions and plays a role in viral …