Results 31 to 40 of about 7,315 (215)

Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases [PDF]

, 2016
OBJECTIVE: Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet ...
Ali, Marfoua S., Crescente, Marilena, Falet, H., Gibbins, Jon M., Holbrook, Lisa M., Jones, Ian M., Kahr, W. H. A., Li, L., Lo, R. W., Loureiro, Silvia, Pluthero, F. G., Poole, A. W., Schenk, Michael P., Vaiyapuri, Sakthi, Walsh, T. G.   +14 more
core   +2 more sources

Protein disulfide isomerase mediates integrin‐dependent adhesion [PDF]

FEBS Letters, 2000
Cell adhesion is mediated by the integrin adhesion receptors. Receptor–ligand interaction involves conformational changes in the receptor, but the underlying mechanism remains unclear. Our earlier work implied a role for sulfhydryls in integrin response to ligand binding in the intact blood platelet.
Lahav, J., Gofer-Dadosh, N., Luboshitz, J., Hess, O., Shaklai, M.   +4 more
openaire   +2 more sources

Roles of Protein Disulfide Isomerase in Breast Cancer [PDF]

Cancers, 2022
Protein disulfide isomerase (PDI) is the endoplasmic reticulum (ER)’s most abundant and essential enzyme and serves as the primary catalyst for protein folding. Due to its apparent role in supporting the rapid proliferation of cancer cells, the selective blockade of PDI results in apoptosis through sustained activation of UPR pathways. The functions of
Suhui Yang, Chanel Jackson, Eduard Karapetyan, Pranabananda Dutta, Dulcie Kermah, Yong Wu, Yanyuan Wu, John Schloss, Jaydutt V. Vadgama   +8 more
openaire   +2 more sources

A Protein Disulfide Isomerase Controls Neuronal Migration through Regulation of Wnt Secretion

Cell Reports, 2019
Summary: Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation remain uncharacterized ...
Nanna Torpe, Sandeep Gopal, Oguzhan Baltaci, Lorenzo Rella, Ava Handley, Hendrik C. Korswagen, Roger Pocock   +6 more
doaj   +1 more source

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

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

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

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

Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy [PDF]

, 2015
published_or_final_versio
Chong, CM, Chu, IK, Cui, G, Guo, L, Hoi, MPM, Lee, SMY, Li, G, Quan, Q, Shan, L, Sun, Y, Wang, Y, Yu, P, Zhang, Z, Zhao, Y   +13 more
core   +1 more source