Results 241 to 250 of about 40,867 (306)

Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins. [PDF]

open access: yesFront Bioinform
Cuevas Ortiz D   +8 more
europepmc   +1 more source

Resin-Supported Site-Specific Antibody Conjugation Method Leads to Antibody-Drug Conjugates with Retained Efficacy and Improved Stability. [PDF]

open access: yesBioconjug Chem
Mullapudi MR   +8 more
europepmc   +1 more source

Revisiting Disulfide–Yne and Disulfide–Diazonium Reactions for Potential Direct Modification of Disulfide Bonds in Proteins

The Journal of Organic Chemistry, 2022
To find their potential use in protein research, direct addition of a disulfide compound to alkyne (namely disulfide-yne reaction) and S-arylation with arenediazonium salt (namely disulfide-diazonium reaction) were investigated in aqueous or protic solutions.
Wei-Cheng Hung   +6 more
openaire   +2 more sources

Dicubyl Disulfide

Journal of the American Chemical Society, 2002
Dicubyl disulfide (1) has been prepared in six steps from commercially available dimethyl-1,4-cubanedicarboxylate in 47% overall yield. In the final step, the previously unknown cubanethiol 2 was oxidized to disulfide 1. X-ray crystallography for 1 reveals the shortest tetragonal C-S bond on record (1.771 A).
Ronny, Priefer   +9 more
openaire   +2 more sources

Thiol–Disulfide Exchange in Signaling: Disulfide Bonds As a Switch

Antioxidants & Redox Signaling, 2013
The major function of disulfide bonds is not only the stabilization of protein structures. Over the last 30 years, a change in perspective took place driven by groundbreaking experiments, which promoted disulfide bonds to central players in essential thiol-disulfide exchange reactions involved in signal transduction, thiol protection, and redox ...
Messens, Joris, Collet, Jean François
openaire   +3 more sources

Disulfide-disulfide interchange catalyzed by a liver supernatant enzyme

Biochimica et Biophysica Acta (BBA) - Enzymology, 1979
An enzyme widely distributed in rabbit tissues which catalyzes an interchange between N,N-di-dinitrophenyl-L-cystine and oxidized glutathione to form the mixed disulfide is described. D-Penicillamine disulfide can be substituted for oxidized glutathione and the mixed disulfide of cysteine and glutathione can serve as the sole substrate giving as one ...
G W, Rafter, G G, Harmison
openaire   +2 more sources

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