Oxidative protein folding occurs both in vivo and in vitro and involves the formation and
rearrangement of protein disulfide bonds (SS bonds). In vivo these reactions are catalyzed …

Thiolated chitosans constitute an integral part of designated “thiomers”, which are thiolated
polymers widely investigated for non-invasive drug delivery. In brief, thiomers display thiol …

A new series of 1, 3, 4-thiadiazole-2-thione derivatives have been prepared and assayed for
the inhibition of three physiologically relevant carbonic anhydrase (CA, EC 4.2. 1.1) …

A series of heterocyclic mercaptans incorporating 1, 3, 4-thiadiazole-and 1, 2, 4-triazole
rings have been prepared and assayed for the inhibition of three physiologically relevant …

Thiomers are thiolated polymers with excellent mucoadhesive properties. The aim of this
study was to synthesize a novel thiolated chitosan with higher reactivity in order to further …

Organocatalysts derived from diethylenetriamine effect the rapid isomerization of non-native
protein disulfide bonds to native ones. These catalysts contain a pendant hydrophobic …

Almost all therapeutic proteins and most extracellular proteins contain disulfide bonds. The
production of these proteins in bacteria or in vitro is challenging due to the need to form the …

The production of proteins using recombinant DNA technology often requires the use of in
vitro protein folding. In order to facilitate in vitro protein folding, a redox buffer is added to the …

Thiol based redox buffers are used to enhance the folding rates of disulfide-containing
proteins in vitro. Traditionally, small molecule aliphatic thiols such as glutathione are …

Part I Page 1 ISSN 2321-807X 2812 | Page October 02, 2014 Recent Developments In
Chemistry Of 1,3,4-Thiadiazoles Mahmoud Refaee Mahmoud, Mahmoud Fawzy Ismail* *E-mail …