Results 181 to 190 of about 3,392,726 (209)
Some of the next articles are maybe not open access.
Association and dissociation of protein disulfide isomerase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994Purified protein disulfide isomerase, homogeneous by SDS-PAGE, can be separated into two components by PAGE and by gel filtration. These two components, with the same amino-acid composition as well as N- and C-terminal sequences, are the tetramer and dimer of molecular weight 240 kDa and 120 kDa, respectively.
X C, Yu, C C, Wang, C L, Tsou
openaire +2 more sources
Protein disulfide isomerase is both an enzyme and a chaperone
The FASEB Journal, 1993Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides. So that thiols situated at distant parts of the polypeptide chain can be joined together to form the native disulfides, the polypeptide chain has to be folded, at least to some
C C, Wang, C L, Tsou
openaire +2 more sources
Purification and Characterization of Yeast Protein Disulfide Isomerase
The Journal of Biochemistry, 1990Protein disulfide-isomerase (PDI), which reactivates inactive scrambled RNase, was purified from Saccharomyces cerevisiae. The enzyme was purified 1,850-fold to apparent homogeneity by five purification steps: 30-70% ammonium sulfate fractionation, DEAE Toyopearl-650S and Butyl Toyopearl-650S chromatographies, and differential Phenyl-5PW HPLC with or ...
T, Mizunaga +3 more
openaire +2 more sources
Protein disulfide isomerase: the structure of oxidative folding
Trends in Biochemical Sciences, 2006Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, a step in the oxidative folding pathway that takes place in specialized cellular compartments.
Gruber, Christian W +4 more
openaire +5 more sources
Promotion of insulin aggregation by protein disulfide isomerase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007We examined the aggregation of insulin as a result of reduction of disulfide bonds catalyzed by protein disulfide isomerase (PDI) using various techniques. We demonstrated the kinetic correlation between PDI-catalyzed insulin reduction and the aggregate formation, the relationship between aggregation and amyloid formation, and the structural ...
Ryosuke, Maeda +3 more
openaire +2 more sources
Mammalian protein disulfide isomerases
1997Abstract PDI is readily purified from mammalian liver, or from other highly secretory tissues such as pancreas or placenta. [Here, in subsequent paragraphs where no specific citation is given see Freedman, Tuite (1994), Freedman etal., (1994, 1995), Freedman (1995) for pre-1994 references].
openaire +1 more source
Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum
Archives of Biochemistry and Biophysics, 2017Ana I Soares Moretti +1 more
exaly