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Protein structure / Proteins / Disulfide bond / Posttranslational modification / Sulfur / Protein disulfide-isomerase / ER oxidoreductin / Oxidative folding / Unfolded protein response / Chemistry / Biology / Thiols


Biosci. Rep[removed]art:e00103 / doi[removed]BSR20130124 Biochemical evidence that regulation of Ero1β
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City

Williams / Memphis / Bulleid / L. A. / Eppendorf / Copenhagen / Rutkevich / Milan / Basel / Hørsholm / /

Company

Juncker A. S. / Life Technologies / Qiagen / Creative Commons / Covance / Suzuki / Novo Nordisk / /

Country

Switzerland / United States / Denmark / /

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Facility

University of Basel / University of Copenhagen / Technical University of Denmark / /

IndustryTerm

active site / outer active site / reaction products / conserved hydrogen bond network / side chain / web-based environment / modification protocol / protein structure prediction software / inner active site / non-solvent exposed site / /

Movie

A. I. / /

Organization

Faculty of Science / Technical University of Denmark / University of Basel / Department of Biology / PDI / Lundbeck Foundation / Danish Ministry of Science / Department of Pharmaceutical Sciences / Swiss National Science Foundation / University of Copenhagen / Department of International Health / Immunology and Microbiology / /

Person

Cecilie Søltoft / Christian Appenzeller-Herzog / Julia Birk / Jonas Schmidt / Lars Ellgaard / Henning Hansen / using αHis / /

Position

RT / Author / representative / /

Product

Vitamin K / dimethyl sulfoxide / /

ProvinceOrState

New Jersey / ERp57 / Ero1β / PDI / /

Technology

Bioinformatics / Antibodies / modification protocol / http / /

URL

http /

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