Results 271 to 280 of about 97,846 (317)
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Biochimica Et Biophysica Acta - Proteins and Proteomics, 2004
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure.
Hiram F Gilbert
exaly +7 more sources
During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure.
Hiram F Gilbert
exaly +7 more sources
Protein disulfide isomerase is both an enzyme and a chaperone
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
Chih-Chen Wang, Chen-Lu Tsou
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British Journal of Pharmacology, 2021 Protein disulfide isomerase (PDI) is the prototypic member of the thiol isomerase family that catalyses disulfide bond rearrangement. Initially identified in the endoplasmic reticulum as folding catalysts, PDI and other members in its family have also ...
Xulin Xu, Joyce Chiu, Chao Fang
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EMBO Journal, 2020 Accumulated unfolded proteins in the endoplasmic reticulum (ER) trigger the unfolded protein response (UPR) to increase ER protein folding capacity. ER proteostasis and UPR signaling need to be regulated in a precise and timely manner.
Yu Liu, Jianchao Zhang, Guizhi Shi
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Cell Reports, 2022
Coordination of inter-tissue stress signaling is essential for organismal fitness. Neuronal mitochondrial perturbations activate the mitochondrial unfolded-protein response (UPRmt) in the intestine via the mitokine Wnt signaling in Caenorhabditis elegans.
Xinyu Li +9 more
semanticscholar +1 more source
Coordination of inter-tissue stress signaling is essential for organismal fitness. Neuronal mitochondrial perturbations activate the mitochondrial unfolded-protein response (UPRmt) in the intestine via the mitokine Wnt signaling in Caenorhabditis elegans.
Xinyu Li +9 more
semanticscholar +1 more source
The Protein Disulfide Isomerase Family: from proteostasis to pathogenesis.
Biochimica et Biophysica Acta - General Subjects, 2020In mammalian cells, nearly one-third of proteins are inserted into the endoplasmic reticulum (ER), where they undergo oxidative folding and chaperoning assisted by approximately 20 members of the protein disulfide isomerase family (PDIs). PDIs consist of
Motonori Matsusaki +5 more
semanticscholar +1 more source
European Journal of Pharmacology, 2020
Cellular stress and inflammation, establishing as disease pathology, have reached great heights in the last few decades. Stress conditions such as hyperglycemia, hyperlipidemia and lipoproteins are known to disturb proteostasis resulting in the ...
Paul Victor, D. Sarada, K. Ramkumar
semanticscholar +1 more source
Cellular stress and inflammation, establishing as disease pathology, have reached great heights in the last few decades. Stress conditions such as hyperglycemia, hyperlipidemia and lipoproteins are known to disturb proteostasis resulting in the ...
Paul Victor, D. Sarada, K. Ramkumar
semanticscholar +1 more source
Protein Disulfide Isomerase in Thrombosis
Seminars in Thrombosis and Hemostasis, 2015Protein disulfide isomerase (PDI) is a 57-kDa oxidoreductase that facilitates cysteine thiol reactions inside and outside the cell. It mediates reduction or oxidation of protein disulfide bonds, thiol/disulfide exchange reactions, and transfer of NO from one protein thiol to another. It also has chaperone properties.
Joyce, Chiu +3 more
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Current Opinion in Structural Biology, 2020
Time-resolved single-molecule observations by high-speed atomic force microscopy (HS-AFM), have greatly advanced our understanding of how proteins operate to fulfill their unique functions.
M. Okumura, K. Noi, K. Inaba
semanticscholar +1 more source
Time-resolved single-molecule observations by high-speed atomic force microscopy (HS-AFM), have greatly advanced our understanding of how proteins operate to fulfill their unique functions.
M. Okumura, K. Noi, K. Inaba
semanticscholar +1 more source
Wheat protein disulfide isomerase improves bread properties via different mechanisms.
Food Chemistry, 2020Gluten network formation by the oxidation of glutenin sulfhydryl group majorly impacts the subsequent dough and bread properties, and an evolutionary list of chemical oxidants has been used as improvers in bread making.
Chunfei Zhao +7 more
semanticscholar +1 more source