Literature DB >> 10597631

Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum.

R Noiva1.   

Abstract

Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the oxidation, reduction and isomerization of protein disulfides. In the endoplasmic reticulum PDI catalyzes both the oxidation and isomerization of disulfides on nascent polypeptides. Under the reducing condition of the cytoplasm, endosomes and cell surface. PDI catalyzes the reduction of protein disulfides. At those locations, PDI has been demonstrated to participate in the regulation of reception function, cell-cell interaction, gene expression, and actin filament polymerization. These activities of PDI will be discussed, as well as its activity as a chaperone and subunit of prolyl 4-hydroxylase and microsomal triglyceride transfer protein.

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Year:  1999        PMID: 10597631     DOI: 10.1006/scdb.1999.0319

Source DB:  PubMed          Journal:  Semin Cell Dev Biol        ISSN: 1084-9521            Impact factor:   7.727


  69 in total

1.  Molecular characterization of a Bombyx mori protein disulfide isomerase (bPDI).

Authors:  Tae Won Goo; Eun Young Yun; Jae-Sam Hwang; Seok-Woo Kang; Soojung Park; Kwan-Hee You; O-Yu Kwon
Journal:  Cell Stress Chaperones       Date:  2002-01       Impact factor: 3.667

2.  Design of an in vivo cleavable disulfide linker in recombinant fusion proteins.

Authors:  Xiaoying Chen; Yun Bai; Jennica L Zaro; Wei-Chiang Shen
Journal:  Biotechniques       Date:  2010-07       Impact factor: 1.993

3.  Protein disulfide isomerase is required for platelet-derived growth factor-induced vascular smooth muscle cell migration, Nox1 NADPH oxidase expression, and RhoGTPase activation.

Authors:  Luciana A Pescatore; Diego Bonatto; Fábio L Forti; Amine Sadok; Hervé Kovacic; Francisco R M Laurindo
Journal:  J Biol Chem       Date:  2012-07-06       Impact factor: 5.157

4.  Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfide-based antibody-drug conjugates.

Authors:  Cary D Austin; Xiaohui Wen; Lewis Gazzard; Christopher Nelson; Richard H Scheller; Suzie J Scales
Journal:  Proc Natl Acad Sci U S A       Date:  2005-12-01       Impact factor: 11.205

Review 5.  Redox regulatory mechanisms in cellular stress responses.

Authors:  Nina Fedoroff
Journal:  Ann Bot       Date:  2006-06-21       Impact factor: 4.357

6.  Exosome-driven antigen transfer for MHC class II presentation facilitated by the receptor binding activity of influenza hemagglutinin.

Authors:  James S Testa; Geraud S Apcher; Joseph D Comber; Laurence C Eisenlohr
Journal:  J Immunol       Date:  2010-11-03       Impact factor: 5.422

7.  Stress-induced transcription of the endoplasmic reticulum oxidoreductin gene ERO1 in the yeast Saccharomyces cerevisiae.

Authors:  Yukiko Takemori; Ayako Sakaguchi; Sayuri Matsuda; Yu Mizukami; Hiroshi Sakurai
Journal:  Mol Genet Genomics       Date:  2005-11-15       Impact factor: 3.291

Review 8.  Bioreducible polycations as shuttles for therapeutic nucleic acid and protein transfection.

Authors:  Philipp M Klein; Ernst Wagner
Journal:  Antioxid Redox Signal       Date:  2014-01-08       Impact factor: 8.401

9.  Identification of genes in thyrocytes regulated by unfolded protein response by using disulfide bond reducing agent of dithiothreitol.

Authors:  S Park; I Hwang; M Shong; O Y Kwon
Journal:  J Endocrinol Invest       Date:  2003-02       Impact factor: 4.256

10.  Overexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion protein.

Authors:  Surbhi Jain; Lori W McGinnes; Trudy G Morrison
Journal:  J Virol       Date:  2008-10-01       Impact factor: 5.103

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