Results 31 to 40 of about 96,012 (310)
The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract. [PDF]
PLoS ONE, 2013 Although disulfide bond formation in proteins is one of the most common types of post-translational modifications, the production of recombinant disulfide-rich proteins remains a challenge.
Wael Gad +9 more
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Microbial Cell Factories, 2010 Background The formation of native disulfide bonds is a complex and essential post-translational modification for many proteins. The large scale production of these proteins can be difficult and depends on targeting the protein to a compartment in which ...
Hatahet Feras +3 more
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Molecules, 2020 The polypeptide backbone of proteins is held together by two main types of covalent bonds: the peptide bonds that link the amino acid residues and the disulfide bonds that link pairs of cysteine amino acids. Disulfide bonds form as a protein folds in the
Philip J. Hogg
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Disulfide bond isomerization in prokaryotes
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2008 Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase.
Gleiter, Stefan, Bardwell, James C.A.
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Native disulfide bond formation in proteins [PDF]
Current Opinion in Chemical Biology, 2000 Native disulfide bond formation is critical for the proper folding of many proteins. Recent studies using newly identified protein oxidants, folding catalysts, and mutant cells provide insight into the mechanism of oxidative protein folding in vivo. This insight promises new strategies for more efficient protein production.
K J, Woycechowsky, R T, Raines
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Bioengineering, 2021 Glucose oxidase (GOx) holds considerable advantages for various applications. Nevertheless, the thermal instability of the enzyme remains a grand challenge, impeding the success in applications outside the well-controlled laboratories, particularly in ...
Sirawit Ittisoponpisan +1 more
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Preventing disulfide bond formation weakens non-covalent forces among lysozyme aggregates. [PDF]
PLoS ONE, 2014 Nonnative disulfide bonds have been observed among protein aggregates in several diseases like amyotrophic lateral sclerosis, cataract and so on. The molecular mechanism by which formation of such bonds promotes protein aggregation is poorly understood ...
Vijay Kumar Ravi +4 more
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Disulfide Bonds Enable Accelerated Protein Evolution [PDF]
Molecular Biology and Evolution, 2017 The different proteins of any proteome evolve at enormously different rates. What factors contribute to this variability, and to what extent, is still a largely open question. We hypothesized that disulfide bonds, by increasing protein stability, should make proteins' structures relatively independent of their amino acid sequences, thus acting as ...
Felix, Feyertag, David, Alvarez-Ponce
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Function‐driven design of a surrogate interleukin‐2 receptor ligand
FEBS Letters, EarlyView.Interleukin (IL)‐2 signaling can be achieved and precisely fine‐tuned through the affinity, distance, and orientation of the heterodimeric receptors with their ligands. We designed a biased IL‐2 surrogate ligand that selectively promotes effector T and natural killer cell activation and differentiation. Interleukin (IL) receptors play a pivotal role in
Ziwei Tang +9 more
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Forcing the reversibility of a mechanochemical reaction
Nature Communications, 2018 Mechanical force can facilitate thermodynamically unfavourable reactions. Here, the authors found that a stretching force can promote the SN2 cleavage of a protein disulfide bond by weak nucleophilic thiols, and that removing this force reverses the ...
Amy E. M. Beedle +5 more
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