Results 1 to 10 of about 41,132 (234)

Collagens - structure, function and biosynthesis. [PDF]

, 2003
The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions.
Aigner, T, Gelse, K, Poschl, E
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Identification and Functional Analysis of a Protein Disulfide Isomerase (AtPDI1) in Arabidopsis thaliana

Frontiers in Plant Science, 2018
Protein disulfide isomerase (PDI) catalyzes the conversion of thiol-disulfide and plays an important role in various physiological events in animals. A PDI (OaPDI) from a tropical plant was detailed studied and it was found to be involved in response of ...
Zhengrong Zhang, Xin Liu, Rong Li, Li Yuan, Yaqing Dai, Xiaoyun Wang   +5 more
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Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols

Antioxidants
Thiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie, Quinn P. Kennedy, Pavel Davizon-Castillo, Moua Yang   +3 more
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Folding of peptides and proteins: role of disulfide bonds, recent developments

Biomolecular Concepts, 2013
Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction.
Hidaka Yuji, Shimamoto Shigeru
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Methods of measuring Protein Disulfide Isomerase activity: a critical overview

Frontiers in Chemistry, 2014
Protein disulfide isomerase is an essential redox chaperone from the endoplasmic reticulum (ER) and is responsible for correct disulfide bond formation in nascent proteins.
Monica Massako Watanabe, Francisco Rafael Martins Laurindo, Denise C Fernandes   +2 more
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nDsbD: a redox interaction hub in the Escherichia coli periplasm [PDF]

, 2018
.: DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain. nDsbD interacts with four different redox proteins involved in the periplasmic disulfide isomerization ...
Capitani, G., Glockshuber, R., Grütter, M., Stirnimann, C.   +3 more
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Cloning, expression, purification and characterization of Leishmania tropica PDI-2 protein

Open Life Sciences, 2016
In Leishmania species, protein disulfide isomerase (PDI) is an essential enzyme that catalyzes thiol-disulfide interchange. The present work describes the isolation, cloning, sequencing and expression of the pdI-2 gene.
Ali Dina, Abbady Abdul-Qader, Kweider Mahmoud, Soukkarieh Chadi   +3 more
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Structural and functional characterization of the oxidoreductase a-DsbA1 from wolbachia pipientis

, 2009
The α-proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host\u27s reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the
Frei, Patrick, Glockshuber, Rudi, Heras, Begoña, Iturbe-Ormaetxe, Iñaki, Jarrott, Russell, Kurz, Mareike, Martin, Jennifer L., O’Neill, Scott L., Shouldice, Stephen R., Wouters, Merridee A.   +9 more
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Protein disulfide isomerase in Philadelphia-negative myeloproliferative neoplasms: a case–control study

The Egyptian Journal of Internal Medicine
Background Classic Philadelphia-negative myeloproliferative neoplasms (MPNs), such as polycythemia vera (PV), essential thrombocythemia (ET), and myelofibrosis (MF), are defined by the unregulated production of bone marrow components resulting from the ...
Marwa Salah Mohammed, Alaa Alnaggar, Nehad Tawfik, Mohamed Abdelkader Morad, Eman Ahmed Abdelaziz, Nagham Yasser, Lamyaa H. Soliman, Mai Galal Elshenoufy   +7 more
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Antiretroviral effect of 4-thio-uridylate against human immunodeficiency virus type 1 [PDF]

, 2012
Albert J., Barbouche R., Beck Z., Berger E. A., Clapham P., Cox S., Doms R. W., Einfeld D., Fenouillet E., Horváth A., Horváth A., Joseph Ongrádi, Juhász E., Kanizsai S., Kanizsai Sz., Kemény B., Kilby J. M., Károly Nagy, Leonard C., Markovic I., Matthias L. J., Nagy K., Nagy K., Nagy K., Nisole S., Ou W., Ryser H. J., Szatmari I., Szilvia Kanizsai, Tarkanyi I., Tõkés S., Wittinghoff E., Ágoston Ghidán   +32 more
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