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The interaction between NLRP1 and oxidized TRX1 involves a transient disulfide bond. [PDF]
Cell Chem BiolGeeson MB +4 more
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Retraction Note: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo. [PDF]
Nat Chem BiolMizrachi D +5 more
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Biochemistry, 2006
Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan, Schmidt +2 more
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Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan, Schmidt +2 more
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MAKING AND BREAKING DISULFIDE BONDS
Annual Review of Microbiology, 1997▪ Abstract It is now well established that protein folding requires the assistance of folding helpers in vivo. The formation or isomerization of disulfide bonds in proteins is a slow process requiring catalysis. In nascent polypeptide chains the cysteine residues are in the thiol form.
Raina S, Missiakas D
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Disulfide bond formation in prokaryotes
Nature Microbiology, 2018Interest in protein disulfide bond formation has recently increased because of the prominent role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that introduces disulfide bonds into cell envelope proteins consists of Escherichia coli enzymes DsbA and DsbB.
Cristina, Landeta +2 more
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Disulfide Bond Exchange in Rhodopsin
Biochemistry, 1998Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein. However, recent work on a rhodopsin mutant split in the cytoplasmic loop connecting helixes 3 and 4 has shown that the ...
M, Kono, H, Yu, D D, Oprian
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Disulfide Bond Formation in the Cytoplasm
Antioxidants & Redox Signaling, 2013Disulfide bond formation is critical for biogenesis of many proteins. While most studies in this field are aimed at elucidating the mechanisms in the endoplasmic reticulum, intermembrane space of mitochondria, and prokaryotic periplasm, structural disulfide bond formation also occurs in other compartments including the cytoplasm.
Mirva J, Saaranen, Lloyd W, Ruddock
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THE GENETICS OF DISULFIDE BOND METABOLISM
Annual Review of Genetics, 1998▪ Abstract Disulfide bonds are required for the stability and function of a large number of proteins. Genetic analysis in combination with biochemical studies have elucidated the main catalysts involved in facilitating these processes in the cell. All enzymes involved in thiol-disulfide metabolism have a conserved active site that consists of two ...
A, Rietsch, J, Beckwith
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The position of disulfide bonds in cobrotoxin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970Abstract 1. 1. The positions of four disulfide bonds in cobrotoxin were investigated. Cobrotoxin was digested with acid protease A, and the resulting five cystine peptides were separated by high-voltage electrophoresis on paper. The identification of the disulfide bridges was made by determining the amino acid composition of the corresponding ...
C C, Yang, H J, Yang, R H, Chiu
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