Results 51 to 60 of about 227,395 (295)

Hsp70 in mitochondrial biogenesis [PDF]

, 1994
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
A. Tzagoloff, A. Tzagoloff, A.J. Caplan, A.J. Caplan, B.D. Gambill, B.S. Glick, C.K. Suzuki, D. Ang, D. M. Cyr, D.M. Cyr, D.M. Cyr, D.M. Cyr, D.M. Cyr, D.P. Atencio, E. Ikeda, E. Kutejová, E.A. Craig, E.A. Craig, F.-U. Hartl, G.S.P. Groot, H.R.B. Pelham, J. Ostermann, J. Rassow, J.F. Dice, J.P. Hendrick, K. Liberek, L. Dyck van, M. Eilers, M. Kiebler, M. Schleyer, M.-J. Gething, M.Y. Cheng, N. Rowley, N. Wang, P. Borst, P. Terpstra, P.-J. Kang, R. A. Stuart, R.A. Stuart, R.A. Stuart, R.B. Deshaies, R.G. Hadikusumo, R.J. Nelson, R.P. Beckman, S. Lindquist, S. Rospert, S.T. Hwang, T. Langer, U.C. Manning-Krieg, W. Neupert, W. Neupert, W. Voos, W.J. Chirico, Z. Xia   +53 more
core   +1 more source

The ubiquitin ligase RNF115 is required for the clearance of damaged lysosomes

FEBS Letters, EarlyView.
Upon lysosomal rupture, an E3 ubiquitin ligase RNF115 translocates from the cytosol to the damaged lysosomal membrane. Moreover, RNF115 depletion impairs the clearance of damaged lysosomes, identifying it as a key regulator of lysosomal quality control.
Sae Nakanaga, Toshiki Takahashi, Akiko Kuma, Hiroyuki Kawahara   +3 more
wiley   +1 more source

Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery

Acta Pharmaceutica Sinica B, 2020
Modulation of protein fate decision and protein homeostasis plays a significant role in altering the protein level, which acts as an orientation to develop drugs with new mechanisms.
Lei Wang, Xiaoli Xu, Zhengyu Jiang, Qidong You   +3 more
doaj   +1 more source

Redox-regulated molecular chaperones [PDF]

Cellular and Molecular Life Sciences, 2002
The conserved heat shock protein Hsp33 functions as a potent molecular chaperone with a highly sophisticated regulation. On transcriptional level, the Hsp33 gene is under heat shock control; on posttranslational level, the Hsp33 protein is under oxidative stress control.
Jakob, Ursula, Graf, Paul C. F.
openaire   +3 more sources

AAA+ protein unfoldases—the Moirai of the proteome

FEBS Letters, EarlyView.
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley   +1 more source

Regulation of Protein Transport Pathways by the Cytosolic Hsp90s

Biomolecules, 2022
The highly conserved molecular chaperone heat shock protein 90 (Hsp90) is well-known for maintaining metastable proteins and mediating various aspects of intracellular protein dynamics. Intriguingly, high-throughput interactome studies suggest that Hsp90
Anna G. Mankovich, Brian C. Freeman
doaj   +1 more source

Differential regulation of ZFAS1 splice variants by endoplasmic reticulum stress in hepatocyte cell lines

FEBS Open Bio, EarlyView.
ZFAS1 is a lncRNA promoting cell proliferation and migration, exhibiting high expression in various cancers. It is conserved, widely expressed, and produces multiple splice variants with unclear roles. We identified several splice variants in hepatocyte models, and found that inhibiting or suppressing regulators of the unfolded protein response (PERK ...
Sébastien Soubeyrand, Paulina Lau, Ruth McPherson   +2 more
wiley   +1 more source

Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection. [PDF]

, 2019
The interplay between a highly polymorphic set of MHC-I alleles and molecular chaperones shapes the repertoire of peptide antigens displayed on the cell surface for T cell surveillance.
Choi, Hannah, Devlin, Christine A, Flores-Solis, David, McShan, Andrew C, Moschidi, Danai, Overall, Sarah A, Park, Jihye, Procko, Erik, Sgourakis, Nikolaos G, Toor, Jugmohit S, Tripathi, Sarvind   +10 more
core  

Characterization of HSP90 isoforms in transformed bovine leukocytes infected with Theileria annulata [PDF]

, 2016
HSP90 chaperones are essential regulators of cellular function, as they ensure the appropriate conformation of multiple key client proteins. Four HSP90 isoforms were identified in the protozoan parasite Theileria annulata.
Calder, Ewen D.D., Devaney, Eileen, Gillan, Victoria, Hostettler, Isabel, Kinnaird, Jane H., Shiels, Brian R., Singh, Meetali, Tatu, Utpal, Weir, William   +8 more
core   +2 more sources

Promiscuous stimulation of HSP70 ATPase activity by parasite‐derived J‐domains

FEBS Open Bio, EarlyView.
The malaria parasite Plasmodium falciparum exports three highly homologous yet functionally divergent J‐domain proteins into human erythrocytes. Here, we show that J‐domains isolated from all three proteins effectively stimulate the ATPase activity of both endogenous host and exported parasite HSP70 chaperones.
Julian Barth, Moritz Koch, Le‐Han Rössner, Johanna Eichhorn, Denys Pogoryelov, Matthias P. Mayer, Jude M. Przyborski   +6 more
wiley   +1 more source