نتایج جستجو برای: protein disulfide isomerase

تعداد نتایج: 1249610  

Journal: :EMBO reports 2005
Lars Ellgaard Lloyd W Ruddock

The process of disulphide bond formation in the endoplasmic reticulum of eukaryotic cells was one of the first mechanisms of catalysed protein folding to be discovered. Protein disulphide isomerase (PDI) is now known to catalyse all of the reactions that are involved in native disulphide bond formation, but despite more than 40 years of study, its mechanism of action is still not fully understo...

Journal: :Organic & biomolecular chemistry 2014
John C Lukesh Kristen A Andersen Kelly K Wallin Ronald T Raines

Organocatalysts derived from diethylenetriamine effect the rapid isomerization of non-native protein disulfide bonds to native ones. These catalysts contain a pendant hydrophobic moiety to encourage interaction with the non-native state, and two thiol groups with low pKa values that form a disulfide bond with a high E°' value.

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