نتایج جستجو برای: protein disulfide isomerase

تعداد نتایج: 1249610  

2012
Adam M. Benham Marcel van Lith Roberto Sitia Ineke Braakman

The formation of disulfide bonds between cysteine residues occurs during the folding of many proteins that enter the secretory pathway. As the polypeptide chain collapses, cysteines brought into proximity can form covalent linkages during a process catalyzed by members of the protein disulfide isomerase family. There are multiple pathways in mammalian cells to ensure disulfides are introduced i...

2004
Benjamin P. Tu Jonathan S. Weissman

The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protein folding. Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FADdependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as ...

2013
Yoshimi Sato Rieko Kojima Masaki Okumura Masatoshi Hagiwara Shoji Masui Ken-ichi Maegawa Masatoshi Saiki Tomohisa Horibe Mamoru Suzuki Kenji Inaba

The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1α and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding. Here, we clarified the Prx4 preferential recognition of two PDI family proteins, P5 and ERp46, and the mode of intera...

Journal: :Cell 2004
Einav Gross David B Kastner Chris A Kaiser Deborah Fass

The flavoenzyme Ero1p produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum. Disulfides generated de novo within Ero1p are transferred to protein disulfide isomerase and then to substrate proteins by dithiol-disulfide exchange reactions. Despite this key role of Ero1p, little is known about the mechanism by which this enzyme catalyzes thiol oxidation. Here, we pres...

Journal: :Proteomics 2007
Toru Ezure Takashi Suzuki Masamitsu Shikata Masaaki Ito Eiji Ando Osamu Nishimura Susumu Tsunasawa

Escherichia coli alkaline phosphatase (AP) and human lysozyme (h-LYZ), which contain two and four disulfide bonds, respectively, were expressed in a cell-free protein synthesis system constructed from Spodoptera frugiperda 21 (Sf21) cells. AP was expressed in a soluble and active form using the insect cell-free system under non-reducing conditions, and h-LYZ was expressed in a soluble and activ...

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