Results 11 to 20 of about 174,472 (299)
Polarity of disulfide bonds [PDF]
Protein Science, 1993 1Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 ...
A J, Saunders, G B, Young, G J, Pielak
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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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Asian Journal of Pharmaceutical Sciences, 2021 Disulfide bond-bridging strategy has been extensively utilized to construct tumor specificity-responsive aliphatic prodrug nanoparticles (PNPs) for precise cancer therapy.
Yuequan Wang +10 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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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 ...
W J, Wedemeyer +3 more
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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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Analysis of Disulfide Bond Formation [PDF]
Current Protocols in Protein Science, 2017 AbstractIn this unit, protocols are provided for detection of disulfide bond formation in cultures of intact cells and in an in vitro translation system containing isolated microsomes or semi‐permeabilized cells. First, the newly synthesized protein of interest is biosynthetically labeled with radioactive amino acids in a short pulse.
Braakman, Ineke +3 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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FEBS Open Bio, 2014 Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
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Molecules, 2014 Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTrx ...
Adam A. Campos-Acevedo +1 more
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