Results 11 to 20 of about 96,012 (310)
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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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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Basis for using thioredoxin as an electron donor by Schizosaccharomyces pombe Gpx1 and Tpx1
AMB Express, 2022 Key points spGpx1 contains two conserved Cys residues (Cys36 and Cys82), which may form a disulfide bond upon oxidation and the reduction of this disulfide bond is most likely to be mediated by Trx in vivo.
Fawad Ahmad +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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