Results 41 to 50 of about 7,369 (220)

Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue [PDF]

, 2009
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease.
Guoping Ren, Daniel Stephan, Zhaohui Xu, Ying Zheng, Danming Tang, Rosemary S. Harrison, Mareike Kurz, Russell Jarrott, Stephen R. Shouldice, Annie Hiniker, Jennifer L. Martin, Begonña Heras, James C.A. Bardwell, Heras, Martin, Pan, Holmgren, Gruber, Krause, Lin, Zapun, Appenzeller-Herzog, Jonda, Quan, Mössner, Huber-Wunderlich, Woycechowsky, DeLano, Georgescu, Charbonnier, Kadokura, Su, Maeda, Inaba, Dai, Hiniker, Bessette, Collet, Nelson, Holmgren, Lundström, Hillson, Tapley, Hiniker, Brünger, Jones, Murshudov, Adams, Grimshaw, Grauschopf, McCarthy, Heras, Hibbert, Johannes, Ritz, Vallee, Rietsch, Chivers, Shaked, Heras, Salsbury, Malojcić, Street, Kallberg, Hahn, Guddat, Katti   +66 more
core   +3 more sources

Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]

, 2016
The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D.
Bindoli, Alberto, Cali', Tito, Citta, Anna, Folda, Alessandra, Rigobello, MARIA PIA, Scalcon, Valeria, Scutari, Guido, Zonta, Francesco   +7 more
core   +1 more source

Molecular Chaperones in Cancer Stem Cells: Determinants of Stemness and Potential Targets for Antitumor Therapy

Cells, 2020
Cancer stem cells (CSCs) are a great challenge in the fight against cancer because these self-renewing tumorigenic cell fractions are thought to be responsible for metastasis dissemination and cases of tumor recurrence. In comparison with non-stem cancer
Alexander Kabakov, Anna Yakimova, Olga Matchuk   +2 more
doaj   +1 more source

Biophysical characterization of Cyclophilin B reveals membrane localization as its primary functional determinant as a prolyl isomerase. [PDF]

Protein Sci
Abstract The endoplasmic reticulum (ER) provides a specialized environment for the folding of secreted and membrane proteins, a process supported by many different chaperones. Among these chaperones, peptidyl‐prolyl cis/trans isomerases (PPIases) catalyze a rate‐limiting conformational step in protein folding, yet the principles governing isoform ...
DeVoe SC, Yost TC, Newton AJ, Grever GA, Ayala MF, Griffith WP, Latvala RD, Schmidpeter PAM.   +7 more
europepmc   +2 more sources

Inhibition of Protein Disulfide Isomerase in Thrombosis [PDF]

Basic & Clinical Pharmacology & Toxicology, 2016
AbstractThis MiniReview addresses our current understanding of the mechanisms by which protein disulfide isomerase (PDI) mediates thrombus formation and discusses the potential of blocking thrombosis by targeting PDI. Thiol isomerases are ubiquitous oxidoreductases primarily localized to the endoplasmic reticulum (ER) where they serve a critical role ...
Roelof H, Bekendam, Robert, Flaumenhaft
openaire   +2 more sources

Protein Disulfide Isomerase and Host-Pathogen Interaction [PDF]

The Scientific World JOURNAL, 2011
Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways in the host-pathogen interaction.
Beatriz S. Stolf, Ioannis Smyrnias, Lucia R. Lopes, Alcione Vendramin, Hiro Goto, Francisco R. M. Laurindo, Ajay M. Shah, Celio X. C. Santos   +7 more
openaire   +3 more sources

Introduction to protein folding for physicists [PDF]

, 2007
The prediction of the three-dimensional native structure of proteins from the knowledge of their amino acid sequence, known as the protein folding problem, is one of the most important yet unsolved issues of modern science.
Abagyan R. A., Arnold V. I., Calera C. Gómez-Moreno, Chothia C., Creighton T. E., Dawkins R., Dawkins R., Drenth J., Dubrovin B. A., Fersht A., Gibson G., Goldstein H., Greiner W., Halgren T. A., Haltia T., Head-Gordon T., Lesk A. M., Levinthal C., Pablo Echenique, Plotkin S. S., Smith C., van Kampen N. G.   +21 more
core   +3 more sources

Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway [PDF]

, 2014
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).
A Jansens, A Land, A Pirneskoski, A. Katrine Wallis, Alistair G. Irvine, AR Karala, AR Karala, AY Denisov, B van den Berg, B van den Berg, B van den Berg, CB Anfinsen, Claudia A. Blindauer, CPM van Mierlo, CPM van Mierlo, CW Gruber, DP Goldenberg, E van Anken, F Hatahet, G Kozlov, G Wagner, HC Shin, HC Shin, J Riemer, JH Laity, JL Arolas, JS Weissman, JS Weissman, L Wang, LJ Byrne, Lloyd W. Ruddock, M Narayan, Mark J. Howard, Michelle L. Rowe, Narinder Sanghera, NJ Bulleid, NJ Darby, P Klappa, P Venetianer, RA Williamson, RB Freedman, RF Goldberger, Richard A. Williamson, RJ Ellis, Robert B. Freedman, S Masui, S Talluri, Salvador Ventura, TE Creighton, TE Creighton, TE Creighton, TE Creighton, VD Nguyen, VD Nguyen, WF Vranken   +54 more
core   +3 more sources

Interaction of Calreticulin with Protein Disulfide Isomerase [PDF]

Journal of Biological Chemistry, 1995
We report here that calreticulin interacts with protein disulfide isomerase (PDI). The PDI-calreticulin complex can be dissociated by Zn(2+)-iminodiacetate-substituted Sepharose-agarose chromatography, suggesting that these interactions may be Zn2+-dependent.
S, Baksh, K, Burns, C, Andrin, M, Michalak   +3 more
openaire   +2 more sources

Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]

, 2017
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J., Pringle, Marie Anne, Robinson, Philip J., Woolhead, Cheryl A.   +3 more
core   +1 more source