Elucidation of the disulfide folding pathway of hirudin by a topology-based approach [PDF]
, 2003 A theoretical model for the folding of proteins containing disulfide bonds is introduced. The model exploits the knowledge of the native state to favour the progressive establishment of native interactions.
De Filippis, V. +3 more
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The structure of a tetrameric α-carbonic anhydrase fromThermovibrio ammonificansreveals a core formed around intermolecular disulfides that contribute to its thermostability [PDF]
, 2014 Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilic Thermovibrio ammonificans α-carbonic anhydrase (TaCA) has been expressed in Escherichia coli and structurally and biochemically characterized ...
Berg, Svein +7 more
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Novel strategies for the synthesis of unsymmetrical glycosyl disulfides [PDF]
, 2016 yesNovel strategies for the efficient synthesis of unsymmetrical glycosyl disulfides are reported. Glycosyl disulfides are increasingly important as glycomimetics and molecular probes in glycobiology. Sialosyl disulfides are synthesised directly from the
Adinolfi +40 more
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Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]
, 2010 The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian +6 more
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Molecular Networks in Dynamic Multilevel Systems [PDF]
, 2018 Dynamic multilevel systems can be assembled from molecular building blocks through two or more reversible reactions that form covalent bonds. Molecular networks of dynamic multilevel systems can exhibit different connectivities between nodes.
Cabezudo, Ignacio +4 more
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FEBS Letters, 2013 Improving the stability of proteins is an important goal in many biomedical and industrial applications. A logical approach is to emulate stabilizing molecular interactions found in nature. Disulfide bonds are covalent interactions that provide substantial stability to many proteins and conform to well‐defined geometric conformations, thus making them ...
Douglas B. Craig +2 more
openaire +3 more sources
Quantification of thiols and disulfides [PDF]
Biochimica et Biophysica Acta (BBA) - General Subjects, 2014 Disulfide bond formation is a key posttranslational modification, with implications for structure, function and stability of numerous proteins. While disulfide bond formation is a necessary and essential process for many proteins, it is deleterious and disruptive for others.
Winther, Jakob R., Thorpe, Colin
openaire +4 more sources
Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation [PDF]
, 2008 The activation of initiator protein tissue factor (TF) is likely to be a crucial step in the blood coagulation process, which leads to fibrin formation. The stimuli responsible for inducing TF activation are largely undefined.
Altmann, Berid +13 more
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Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway [PDF]
, 2014 In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).
A Jansens +54 more
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Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]
, 2017 The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J. +3 more
core +1 more source