Results 31 to 40 of about 7,369 (220)

A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis [PDF]

, 2017
Background: Within the endoplasmic reticulum, thiol isomerase enzymes modulate the formation and rearrangement of disulphide bonds in newly folded proteins entering the secretory pathway to ensure correct protein folding.
Bicknell, A. B., Flora, G. D., Gibbins, J. M., Holbrook, L., Sahli, K., Sandhar, G. K., Sasikumar, P., Schenk, M. P., Stainer, A. R.   +8 more
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Redox proteomics and structural analyses provide insightful implications for additional non-catalytic thiol-disulfide motifs in PDIs

Redox Biology, 2023
Protein disulfide isomerases (PDIs) catalyze redox reactions that reduce, oxidize, or isomerize disulfide bonds and act as chaperones of proteins as they fold. The characteristic features of PDIs are the presence of one or more catalytic thioredoxin (TRX)
Natalia Zamorano Cuervo, Nathalie Grandvaux   +1 more
doaj   +1 more source

Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding.

PLoS ONE, 2013
Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as
Roohi Vinaik, Guennadi Kozlov, Kalle Gehring   +2 more
doaj   +1 more source

Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis [PDF]

, 2008
Wolbachia pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by manipulating the host reproduction machinery to enhance their own transmission. This unusual phenotype is
Alun Jones, Bardwell, Begoña Heras, Collet, Debarbieux, Edeling, Ellermeier, Ellman, Floate, Gautier Robin, Gordon J. King, Goulding, Gruber, Heras, Hillson, Holmgren, Iñaki Iturbe-Ormaetxe, Jennifer L. Martin, Jeyaprakash, Kadokura, Kelley, Mareike Kurz, Martin, Martin, McCarthy, Messens, Nakamoto, Nathan Cowieson, O’Neill, O’Neill, Patrick Frei, Raina, Riegler, Rietsch, Rudi Glockshuber, Russell Jarrott, Sambrook, Scott L. O’Neill, Studier, Taylor, Taylor, Werren, Wu, Yu   +43 more
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Inhibition of thiol isomerase activity diminishes endothelial activation of plasminogen, but not of protein C [PDF]

, 2015
Highlights •A range of thiol isomerase enzymes were expressed by HMEC-1 endothelial cells. •Inhibition of thiol isomerases reduced plasminogen activation on HMEC-1 cells.
Gordge, M.P., Gordge, M.P., Kamaludin, N., Kamaludin, N., Shah, C.M., Shah, C.M., Smith, C.L., Smith, C.L.   +7 more
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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

The cuticle [PDF]

, 2007
The nematode cuticle is an extremely flexible and resilient exoskeleton that permits locomotion via attachment to muscle, confers environmental protection and allows growth by molting.
Johnstone, I. J., Page, A. P.
core   +1 more source

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

Folding of small disulfide-rich proteins : clarifying the puzzle [PDF]

, 2006
Premi a l'excel·lència investigadora. Àmbit de les Ciències Experimentals. 2008The process by which small proteins fold to their native conformations has been intensively studied over the last few decades.
Apuy, Arolas, Arolas, Arolas, Arolas, Baneyx, Bardwell, Cemazar, Cemazar, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chatrenet, Creighton, Creighton, Creighton, Creighton, Creighton, Daggett, Daly, Darby, Dobson, Ellgaard, Francesc X. Aviles, Fuller, Gehrmann, Goldberg, Goldenberg, Heitz, Hogg, Houry, Joan L. Arolas, Jui-Yoa Chang, Klein-Seetharaman, Kortemme, Kuhlman, Laity, Li, Lu, Matagne, Narayan, Narayan, Narayan, Narayan, Onuchic, Permyakov, Ross, Ruoppolo, Ruoppolo, Salamanca, Salvador Ventura, Scheraga, Shimotakahara, Shin, van den Berg, van den Berg, van Mierlo, van Mierlo, Venhudova, Wedemeyer, Weissman, Welker, Welker, Wu, Yang, Zavodszky   +73 more
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