(Q54436865)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17675287%20AND%20SRC:MED&resulttype=core&format=json

3 January 2020

title

The CXXC motif is more than a redox rheostat (English)

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3 January 2020

1

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3 January 2020

author name string

Irmhild Schneider

2

1 reference

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3 January 2020

Jonathan Pan

3

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3 January 2020

Annekathrin Von Hacht

4

1 reference

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3 January 2020

James C A Bardwell

5

1 reference

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3 January 2020

language of work or name

English

0 references

publication date

3 August 2007

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17675287%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

3 January 2020

published in

1 reference

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3 January 2020

volume

282

1 reference

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3 January 2020

issue

39

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3 January 2020

page(s)

28823-28833

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Protein disulfide bond formation in prokaryotes

3 January 2020

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Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases

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The CXXC motif: a rheostat in the active site.

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The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

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A pathway for disulfide bond formation in vivo

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Why is DsbA such an oxidizing disulfide catalyst?

21 January 2018

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Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli

21 January 2018

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Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm

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Crystal structure of the DsbA protein required for disulphide bond formation in vivo

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The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.

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Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.

21 January 2018

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21 January 2018

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Steady-state and transient kinetic analyses of taurine/alpha-ketoglutarate dioxygenase: effects of oxygen concentration, alternative sulfonates, and active-site variants on the FeIV-oxo intermediate

21 January 2018

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Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.

21 January 2018

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Reconstitution of a disulfide isomerization system

21 January 2018

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Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria

21 January 2018

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Biochemical effects of mercury, cadmium, and lead

21 January 2018

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Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis.

21 January 2018

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Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cells

21 January 2018

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Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coli

21 January 2018

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Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+.

21 January 2018

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Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli

21 January 2018

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DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.

21 January 2018

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Kinetic characterization of the disulfide bond-forming enzyme DsbB.

21 January 2018

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Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.

21 January 2018

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Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine

21 January 2018

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Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate

21 January 2018

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21 January 2018

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Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.

21 January 2018

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Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp

21 January 2018

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Different types of interactions involving cysteine sulfhydryl group in proteins.

21 January 2018

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The local electrostatic environment determines cysteine reactivity of tubulin

21 January 2018

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Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization

21 January 2018

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Dipoles localized at helix termini of proteins stabilize charges

21 January 2018

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21 January 2018

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Dimerization by domain hybridization bestows chaperone and isomerase activities

21 January 2018

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Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae

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