The Role of Thiols and Disulfides on Protein Stability

Trivedi, Maulik; Laurence, Jennifer S.; Siahaan, Teruna J.

doi:10.2174/138920309789630534

Cited by 341 publications

(252 citation statements)

References 90 publications

Supporting

Mentioning

244

Contrasting

Unclassified

Order By: Relevance

“…The roles of Cys-oxidation in protein folding and structural stability are manifold (Wedemeyer et al 2000;Trivedi et al 2009), and more recently, there has been an increased appreciation of the potential for Cys oxidation/ reduction as a component of cellular signaling pathways (Balsera et al 2014;García-Santamarina et al 2014;Kim et al 2014a, b). Furthermore, many enzymes have an activesite Cys residue (e.g., Waszczak et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Rao

Thelen

Miernyk

2015

Cell Stress and Chaperones

View full text Add to dashboard Cite

Oxidation of methionine (Met) to Met sulfoxide (MetSO) is a frequently found reversible posttranslational modification. It has been presumed that the major functional role for oxidation-labile Met residues is to protect proteins/ cells from oxidative stress. However, Met oxidation has been established as a key mechanism for direct regulation of a wide range of protein functions and cellular processes. Furthermore, recent reports suggest an interaction between Met oxidation and O-phosphorylation. Such interactions are a potentially direct interface between redox sensing and signaling, and cellular protein kinase/phosphatase-based signaling. Herein, we describe the current state of Met oxidation research, provide some mechanistic insight into crosstalk between these two major posttranslational modifications, and consider the evolutionary significance and regulatory potential of this crosstalk.

show abstract

Section: Introductionmentioning

confidence: 99%

Convergent signaling pathways—interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation

Rao

Thelen

Miernyk

2015

Cell Stress and Chaperones

View full text Add to dashboard Cite

show abstract

“…It is their high potency as well as small size (16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26) and selectivity that renders -conotoxins very interesting (18). The latter characteristic in particular is a valuable quality for the development of potential therapeutics.…”

mentioning

confidence: 99%

Design of Bioactive Peptides from Naturally Occurring μ-Conotoxin Structures

Stevens

Peigneur

Dyubankova

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: -Conotoxins possess interesting blocking effects on voltage-gated sodium channels (Na v s). Results: Based on two known -conotoxins, we designed miniaturized peptides that potently and selectively block Na v s, although they do not contain an ␣-helix. Conclusion: Peptidomimetics constitute a valuable tool to develop novel, synthetic Na v blockers. Significance: Our compounds prove to be an ideal starting platform in the search for therapeutics to treat Na v -related diseases.

show abstract

“…Soybean BBI do not lose activity at pH values as low as 1.5 in the presence of pepsin at 37 °C for 2 h [34]; these proteins are also stable to both the acidic conditions and the action of digestive enzymes under simulated gastric and intestinal digestion [35]. Such stability is associated with the rigid structure provided by the seven intra-molecular disulphide bridges that maintain the structural and functional features of the binding sites by adding covalent attachment to the inhibitor core [10,36]. BBI are fully inactivated by autoclaving or reduction of their disulphide bridges followed by alkylation of the cysteinyl sulfhydryl groups [26].…”

Section: Bioavailability and Metabolism Of Bbimentioning

confidence: 99%