Add to ORKGTese de doutoramento em Bioquímica (Regulação Bioquímica), apresentada à Universidade de Lisboa através da Faculdade de Ciências, 200
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
In eukaryotic cells, protein disulfide bond formation occurs in the lumen of the ER as part of the f...
Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (P...
Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 1999.Includes bibliographic...
Human Ero1alpha is an endoplasmic reticulum (ER)-resident protein responsible for protein disulfide ...
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide is...
Protein disulfide isomerases (PDIs) catalyze the oxidation and isomerization of disulfide bonds in p...
Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of ...
Aims: Efficient oxidative protein folding (OPF) in the endoplasmic reticulum (ER) is a key requireme...
AbstractProtein disulfide bonds are an important co- and post-translational modification for protein...
AbstractThe Erv flavoenzymes contain a compact module that catalyzes the pairing of cysteine thiols ...
Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and ...
Human Ero1alpha is an endoplasmic reticulum (ER)-resident protein responsible for protein disulfide ...
Les protéines destinées à la sécrétion ou adressées à la membrane transitent par le réticulum endop...
The formation of native intramolecular disulfide bonds is critical for the folding and stability of ...
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
In eukaryotic cells, protein disulfide bond formation occurs in the lumen of the ER as part of the f...
Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (P...
Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Biology, 1999.Includes bibliographic...
Human Ero1alpha is an endoplasmic reticulum (ER)-resident protein responsible for protein disulfide ...
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide is...
Protein disulfide isomerases (PDIs) catalyze the oxidation and isomerization of disulfide bonds in p...
Oxidizing conditions must be maintained in the endoplasmic reticulum (ER) to allow the formation of ...
Aims: Efficient oxidative protein folding (OPF) in the endoplasmic reticulum (ER) is a key requireme...
AbstractProtein disulfide bonds are an important co- and post-translational modification for protein...
AbstractThe Erv flavoenzymes contain a compact module that catalyzes the pairing of cysteine thiols ...
Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and ...
Human Ero1alpha is an endoplasmic reticulum (ER)-resident protein responsible for protein disulfide ...
Les protéines destinées à la sécrétion ou adressées à la membrane transitent par le réticulum endop...
The formation of native intramolecular disulfide bonds is critical for the folding and stability of ...
Protein disulfide bonds are an important co- and post-translational modification for proteins enteri...
In eukaryotic cells, protein disulfide bond formation occurs in the lumen of the ER as part of the f...
Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (P...