Jack of all trades: versatile catechol crosslinking mechanisms

J Yang, MAC Stuart, M Kamperman - Chemical Society Reviews, 2014 - pubs.rsc.org
Catechols play an important role in many natural systems. They are known to readily interact
with both organic (eg, amino acids) and inorganic (eg, metal ions, metal oxides) compounds …

The thiol pool in human plasma: the central contribution of albumin to redox processes

L Turell, R Radi, B Alvarez - Free Radical Biology and Medicine, 2013 - Elsevier
The plasma compartment has particular features regarding the nature and concentration of
low and high molecular weight thiols and oxidized derivatives. Plasma is relatively poor in …

Redox-responsive polymers for drug delivery: from molecular design to applications

M Huo, J Yuan, L Tao, Y Wei - Polymer Chemistry, 2014 - pubs.rsc.org
Glutathione has been regarded as a significant signal for distinguishing between tumor and
normal tissue. Recently, reactive oxygen species have attracted much attention for their …

Kinetics and mechanisms of thiol–disulfide exchange covering direct substitution and thiol oxidation-mediated pathways

P Nagy - Antioxidants & redox signaling, 2013 - liebertpub.com
Significance: Disulfides are important building blocks in the secondary and tertiary structures
of proteins, serving as inter-and intra-subunit cross links. Disulfides are also the major …

Mussel protein adhesion depends on interprotein thiol-mediated redox modulation

J Yu, W Wei, E Danner, RK Ashley… - Nature chemical …, 2011 - nature.com
Mussel adhesion is mediated by foot proteins (mfps) rich in a catecholic amino acid, 3, 4-
dihydroxyphenylalanine (dopa), capable of forming strong bidentate interactions with a …

Structure, function, and mechanism of thioredoxin proteins

JF Collet, J Messens - Antioxidants & redox signaling, 2010 - liebertpub.com
Thioredoxins are ubiquitous antioxidant enzymes that play important roles in many health-
related cellular processes. As such, the fundamental knowledge of how these enzymes work …

From structure to redox: The diverse functional roles of disulfides and implications in disease

TJ Bechtel, E Weerapana - Proteomics, 2017 - Wiley Online Library
This review provides a comprehensive overview of the functional roles of disulfide bonds
and their relevance to human disease. The critical roles of disulfide bonds in protein …

Understanding the pKa of Redox Cysteines: The Key Role of Hydrogen Bonding

G Roos, N Foloppe, J Messens - Antioxidants & redox signaling, 2013 - liebertpub.com
Many cellular functions involve cysteine chemistry via thiol–disulfide exchange pathways.
The nucleophilic cysteines of the enzymes involved are activated as thiolate. A thiolate is …

An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations

RE Hansen, JR Winther - Analytical biochemistry, 2009 - Elsevier
The majority of the thiols (SH) 2 and disulfides (SS) in cells are found as the amino acid
cysteine and its disulfide, cystine (Fig. 1 A). The thiolate anion is intrinsically one of the …

Disulfide-containing parenteral delivery systems and their redox-biological fate

L Brülisauer, MA Gauthier, JC Leroux - Journal of Controlled Release, 2014 - Elsevier
Exploiting the redox-sensitivity of disulfide bonds is an increasingly popular means to trigger
drug release at a target location in the body. The bio-reducible linker (containing a disulfide) …