Results 11 to 20 of about 1,312,330 (378)
Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway
Cells, 2020 Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER).
Philip J. Robinson, Neil J. Bulleid
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PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly
Molecules, 2020 Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the ...
Jiahui Fu +3 more
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PLoS ONE, 2015 Maternal nicotine exposure has been associated with many adverse fetal and placental outcomes. Although underlying mechanisms remain elusive, recent studies have identified that augmented endoplasmic reticulum (ER) stress is linked to placental ...
Michael K Wong +3 more
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PLoS ONE, 2014 Single domain antibodies are the small recombinant variable domains derived from camelid heavy-chain-only antibodies. They are renowned for their stability, in large part due to their ability to refold following thermal or chemical denaturation.
Dan Zabetakis +4 more
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Microbial Cell Factories, 2022 Background Escherichia coli (E. coli) is a promising host for production of recombinant proteins (including antibodies and antibody fragments) that don’t require complex post-translational modifications such as glycosylation.
Tomasz K. Baginski +8 more
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Disulfide Bonds and Protein Folding [PDF]
Biochemistry, 2000 The applications of disulfide-bond chemistry to studies of protein folding, structure, and stability are reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). After surveying the general properties and advantages of disulfide-bond studies, we illustrate the mechanism of reductive unfolding with RNase A, and discuss its application ...
Harold A. Scheraga +3 more
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Prediction of disulfide bond engineering sites using a machine learning method
Scientific Reports, 2020 Disulfide bonds are covalently bonded sulfur atoms from cysteine pairs in protein structures. Due to the importance of disulfide bonds in protein folding and structural stability, artificial disulfide bonds are often engineered by cysteine mutation to ...
Xiang Gao +4 more
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An ultralong CDRH2 in HCV neutralizing antibody demonstrates structural plasticity of antibodies against E2 glycoprotein [PDF]
, 2020 A vaccine protective against diverse HCV variants is needed to control the HCV epidemic. Structures of E2 complexes with front layer-specific broadly neutralizing antibodies (bNAbs) isolated from HCV-infected individuals, revealed a disulfide bond ...
Adams +32 more
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CD44 Binding to Hyaluronic Acid Is Redox Regulated by a Labile Disulfide Bond in the Hyaluronic Acid Binding Site. [PDF]
PLoS ONE, 2015 CD44 is the primary leukocyte cell surface receptor for hyaluronic acid (HA), a component of the extracellular matrix. Enzymatic post translational cleavage of labile disulfide bonds is a mechanism by which proteins are structurally regulated by ...
Helena Kellett-Clarke +3 more
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Redox Potentials of Disulfide Bonds in LOXL2 Studied by Nonequilibrium Alchemical Simulation
Frontiers in Chemistry, 2021 Lysyl oxidase-like 2 (LOXL2) is a metalloenzyme that catalyzes the oxidative deamination ε-amino group of lysine. It is found that LOXL2 is a promotor for the metastasis and invasion of cancer cells. Disulfide bonds are important components in LOXL2, and
Lirui Lin +10 more
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