Results 151 to 160 of about 21,311 (187)

Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase

Journal of Bioscience and Bioengineering, 2001
Disulfide bond formation in the refolding of thermophilic fungal protein disulfide isomerase (PDI) was investigated. It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the
T, Harada, E, Kurimoto, K, Tokuhiro, O, Asami, T, Sakai, D, Nohara, K, Kato   +6 more
openaire   +2 more sources

Catalysis of Disulfide Isomerization in Thrombospondin 1 by Protein Disulfide Isomerase

Biochemistry, 1996
Thrombospondin 1 is a multidomain glycoprotein from platelets and most cells that participates in diverse biological processes. The structure and some functional properties of thrombospondin 1 are regulated by disulfide interchange in the Ca(2+)-binding repeats and C-globular domain. The recent identification of the enzyme, protein disulfide isomerase,
K A, Hotchkiss, C N, Chesterman, P J, Hogg   +2 more
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Mammalian protein disulfide isomerases

1997
Abstract 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 isomerase: the structure of oxidative folding

Trends in Biochemical Sciences, 2006
Cellular 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, Cemazar, Maga, Heras, Begona, Martin, Jennifer L, Craik, David J   +4 more
openaire   +3 more sources

Promotion of insulin aggregation by protein disulfide isomerase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007
We 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, Kazuyoshi, Ado, Naohiro, Takeda, Yoshihiro, Taniguchi   +3 more
openaire   +2 more sources

ER calcistorin/protein disulfide isomerase

1996
Abstract ER calcistorin!Protein disulfide isomerase (ECaSt!POJ), identified in the endoplasmic reticulum (ER) of the sea urchin egg, is a high capacity, low affinity Ca2+-binding protein which also has POI activity. The molecule apparently has a dual function of Ca2+storage and POI activity in the ER of the sea urchin egg.
openaire   +1 more source

Protein Disulfide Isomerase

2016
Andrea Shergalis, Nouri Neamati
openaire   +1 more source

Mechanisms, regulation and functions of the unfolded protein response

Nature Reviews Molecular Cell Biology, 2020
Claudio Hetz, Kezhong Zhang, Randal J Kaufman   +2 more
exaly  

Protein disulfide-isomerase.

Methods in enzymology, 1995
R B, Freedman, H C, Hawkins, S H, McLaughlin   +2 more
openaire   +1 more source

Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing

Nature Reviews Molecular Cell Biology, 2021
Simon Alberti, Anthony A Hyman
exaly