Results 31 to 40 of about 3,285 (194)

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

Molecular characterization and expression profiling of the protein disulfide isomerase gene family in Brachypodium distachyon L. [PDF]

PLoS ONE, 2014
Protein disulfide isomerases (PDI) are involved in catalyzing protein disulfide bonding and isomerization in the endoplasmic reticulum and functions as a chaperone to inhibit the aggregation of misfolded proteins. Brachypodium distachyon is a widely used
Chong Zhu, Nana Luo, Miao He, Guanxing Chen, Jiantang Zhu, Guangjun Yin, Xiaohui Li, Yingkao Hu, Jiarui Li, Yueming Yan   +9 more
doaj   +1 more source

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

Myricetin, the Main Flavonoid in Syzygium cumini Leaf, Is a Novel Inhibitor of Platelet Thiol Isomerases PDI and ERp5

Frontiers in Pharmacology, 2020
BackgroundFlavonoids have been characterized as a prominent class of compounds to treat thrombotic diseases through the inhibition of thiol isomerases. Syzygium cumini is a flavonoid-rich medicinal plant that contains myricetin and gallic acid. Little is
Renato Simões Gaspar, Renato Simões Gaspar, Samira Abdalla da Silva, Jennifer Stapleton, João Lucas de Lima Fontelles, Hiran Reis Sousa, Vinicyus Teles Chagas, Shuruq Alsufyani, Andrés Trostchansky, Jonathan M. Gibbins, Antonio Marcus de Andrade Paes   +10 more
doaj   +1 more source

Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]

, 2016
Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the ...
Altieri, Fabio, Cervoni, Laura, Chichiarelli, Silvia, Eufemi, Margherita, Gaucci, Elisa, Grillo, Caterina, Nittari, Giulio, Raimondo, Domenico   +7 more
core   +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

Substrate recognition by the protein disulfide isomerases [PDF]

The FEBS Journal, 2007
Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
Hatahet Feras, Ruddock Lloyd
openaire   +2 more sources

Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17

Scientific Reports, 2018
A Disintegrin and Metalloprotease 17 (ADAM17) can cause the fast release of growth factors and inflammatory mediators from the cell surface. Its activity has to be turned on which occurs by various stimuli.
Sebastian Krossa, Axel J. Scheidig, Joachim Grötzinger, Inken Lorenzen   +3 more
doaj   +1 more source

Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A. [PDF]

PLoS ONE, 2017
Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms.
Benjamin Selles, Flavien Zannini, Jérémy Couturier, Jean-Pierre Jacquot, Nicolas Rouhier   +4 more
doaj   +1 more source