Quantification of thiols and disulfides

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Quantification of thiols and disulfides. / Winther, Jakob R.; Thorpe, Colin.

I: BBA General Subjects, Bind 1840, Nr. 2, 2014, s. 838-846.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Winther, JR & Thorpe, C 2014, 'Quantification of thiols and disulfides', BBA General Subjects, bind 1840, nr. 2, s. 838-846. https://doi.org/10.1016/j.bbagen.2013.03.031

APA

Winther, J. R., & Thorpe, C. (2014). Quantification of thiols and disulfides. BBA General Subjects, 1840(2), 838-846. https://doi.org/10.1016/j.bbagen.2013.03.031

Vancouver

Winther JR, Thorpe C. Quantification of thiols and disulfides. BBA General Subjects. 2014;1840(2):838-846. https://doi.org/10.1016/j.bbagen.2013.03.031

Author

Winther, Jakob R. ; Thorpe, Colin. / Quantification of thiols and disulfides. I: BBA General Subjects. 2014 ; Bind 1840, Nr. 2. s. 838-846.

Bibtex

@article{24bb79a7e3a84b2cacb8ea1a3d184a5d,
title = "Quantification of thiols and disulfides",
abstract = "Disulfide bond formation is a key posttranslational modification, with implications for structure, function and stability of numerous proteins. While disulfide bond formation is a necessary and essential process for many proteins, it is deleterious and disruptive for others. Cells go to great lengths to regulate thiol-disulfide bond homeostasis, typically with several, apparently redundant, systems working in parallel. Dissecting the extent of oxidation and reduction of disulfides is an ongoing challenge due, in part, to the facility of thiol/disulfide exchange reactions.",
author = "Winther, {Jakob R.} and Colin Thorpe",
note = "Current methods to study reactive oxygen species - pros and cons",
year = "2014",
doi = "10.1016/j.bbagen.2013.03.031",
language = "English",
volume = "1840",
pages = "838--846",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Quantification of thiols and disulfides

AU - Winther, Jakob R.

AU - Thorpe, Colin

N1 - Current methods to study reactive oxygen species - pros and cons

PY - 2014

Y1 - 2014

N2 - Disulfide bond formation is a key posttranslational modification, with implications for structure, function and stability of numerous proteins. While disulfide bond formation is a necessary and essential process for many proteins, it is deleterious and disruptive for others. Cells go to great lengths to regulate thiol-disulfide bond homeostasis, typically with several, apparently redundant, systems working in parallel. Dissecting the extent of oxidation and reduction of disulfides is an ongoing challenge due, in part, to the facility of thiol/disulfide exchange reactions.

AB - Disulfide bond formation is a key posttranslational modification, with implications for structure, function and stability of numerous proteins. While disulfide bond formation is a necessary and essential process for many proteins, it is deleterious and disruptive for others. Cells go to great lengths to regulate thiol-disulfide bond homeostasis, typically with several, apparently redundant, systems working in parallel. Dissecting the extent of oxidation and reduction of disulfides is an ongoing challenge due, in part, to the facility of thiol/disulfide exchange reactions.

U2 - 10.1016/j.bbagen.2013.03.031

DO - 10.1016/j.bbagen.2013.03.031

M3 - Review

C2 - 23567800

VL - 1840

SP - 838

EP - 846

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2

ER -

ID: 93948523