This site needs JavaScript to work properly. Please enable it to take advantage of the complete set of features!

Skip to main page content

Email citation

Add to Collections

Your saved search

Name of saved search:

Search terms:

Test search terms

Would you like email updates of new search results?

Yes
No

Email: (change)

Frequency:

Which day?

Which day?

Report format:

Send at most:

Send even when there aren't any new results

Optional text in email:

Your RSS Feed

. 1993 Nov 1;3(11):790-3.

doi: 10.1016/0960-9822(93)90034-l.

A model catalyst of protein disulphide bond formation

T E Creighton¹, R B Freedman

Affiliations

PMID: 15335850
DOI: 10.1016/0960-9822(93)90034-l

A model catalyst of protein disulphide bond formation

T E Creighton et al. Curr Biol. 1993.

. 1993 Nov 1;3(11):790-3.

doi: 10.1016/0960-9822(93)90034-l.

Authors

T E Creighton¹, R B Freedman

Affiliation

¹ European Molecular Biology Laboratory, 69012 Heidelberg, Germany.

PMID: 15335850
DOI: 10.1016/0960-9822(93)90034-l

No abstract available

PubMed Disclaimer

Similar articles

Oxidative protein folding in bacteria.
Collet JF, Bardwell JC. Collet JF, et al. Mol Microbiol. 2002 Apr;44(1):1-8. doi: 10.1046/j.1365-2958.2002.02851.x. Mol Microbiol. 2002. PMID: 11967064 Review.
Intra-A chain disulphide bond forms first during insulin precursor folding.
Yuan Y, Wang ZH, Tang JG. Yuan Y, et al. Biochem J. 1999 Oct 1;343 Pt 1(Pt 1):139-44. Biochem J. 1999. PMID: 10493922 Free PMC article.
Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.
Edman JC, Ellis L, Blacher RW, Roth RA, Rutter WJ. Edman JC, et al. Nature. 1985 Sep 19-25;317(6034):267-70. doi: 10.1038/317267a0. Nature. 1985. PMID: 3840230
Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase.
Weissman JS, Kim PS. Weissman JS, et al. Nature. 1993 Sep 9;365(6442):185-8. doi: 10.1038/365185a0. Nature. 1993. PMID: 7690463
Structural mechanism of disulphide bond-mediated redox switches.
Ryu SE. Ryu SE. J Biochem. 2012 Jun;151(6):579-88. doi: 10.1093/jb/mvs046. Epub 2012 May 2. J Biochem. 2012. PMID: 22554686 Review.

See all similar articles

Cited by

Genotype-protein phenotype characterization of NOD2 and IL23R missense variants associated with inflammatory bowel disease: A paradigm from molecular modelling, dynamics, and docking simulations.
Nasser KK, Shinawi T. Nasser KK, et al. Front Med (Lausanne). 2023 Jan 10;9:1090120. doi: 10.3389/fmed.2022.1090120. eCollection 2022. Front Med (Lausanne). 2023. PMID: 36703890 Free PMC article.
Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.
Stopa JD, Baker KM, Grover SP, Flaumenhaft R, Furie B. Stopa JD, et al. J Biol Chem. 2017 Jun 2;292(22):9063-9074. doi: 10.1074/jbc.M116.771832. Epub 2017 Mar 31. J Biol Chem. 2017. PMID: 28364042 Free PMC article.
Amino acid substitutions in the FXYD motif enhance phospholemman-induced modulation of cardiac L-type calcium channels.
Guo K, Wang X, Gao G, Huang C, Elmslie KS, Peterson BZ. Guo K, et al. Am J Physiol Cell Physiol. 2010 Nov;299(5):C1203-11. doi: 10.1152/ajpcell.00149.2010. Epub 2010 Aug 18. Am J Physiol Cell Physiol. 2010. PMID: 20720179 Free PMC article.
pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate.
Ruddock LW, Hirst TR, Freedman RB. Ruddock LW, et al. Biochem J. 1996 May 1;315 ( Pt 3)(Pt 3):1001-5. doi: 10.1042/bj3151001. Biochem J. 1996. PMID: 8645136 Free PMC article.
The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.
Missiakas D, Georgopoulos C, Raina S. Missiakas D, et al. EMBO J. 1994 Apr 15;13(8):2013-20. doi: 10.1002/j.1460-2075.1994.tb06471.x. EMBO J. 1994. PMID: 8168498 Free PMC article.

See all "Cited by" articles

LinkOut - more resources

Full Text Sources
- Elsevier Science