Identification of the physiological substrates of PDIp, a pancreas-specific protein-disulfide isomerase family member-Reference-Cited by-同舟云学术

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Identification of the physiological substrates of PDIp, a pancreas-specific protein-disulfide isomerase family member

Published:2018-11 Issue:48 Volume:293 Page:18421-18433
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Fujimoto Takushi,Nakamura Orie,Saito Michiko,Tsuru Akio,Matsumoto Masaki,Kohno Kenji^ORCID,Inaba Kenji,Kadokura Hiroshi^ORCID

Funder

MEXT | Japan Society for the Promotion of Science (JSPS)

MEXT | JST | Core Research for Evolutional Science and Technology (CREST)

Noda Institute for Scientific Research (NISR)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference46 articles.

1. Mechanisms of oxidative protein folding in the bacterial cell envelope;Kadokura;Antioxid. Redox Signal,2010

2. Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum;Okumura;Free Radic. Biol. Med,2015

3. Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals;Sato;FEBS J,2012

4. ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. Mol;Oka;Cell,2013

5. Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER;Poet;EMBO J,2017

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4. O-fucosylation stabilizes the TSR3 motif in thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond;Journal of Biological Chemistry;2022-06

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