Intersubunit interactions in Plasmodium falciparum thioredoxin reductase (Q39148742)

9 September 2017

title

Intersubunit interactions in Plasmodium falciparum thioredoxin reductase (English)

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9 September 2017

main subject

Plasmodium falciparum

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author name string

Krnajski Z

1

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9 September 2017

Gilberger TW

2

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9 September 2017

Walter RD

3

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9 September 2017

Muller S

4

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9 September 2017

language of work or name

English

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publication date

1 December 2000

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Journal of Biological Chemistry

9 September 2017

published in

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9 September 2017

volume

275

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9 September 2017

issue

52

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9 September 2017

page(s)

40874-40878

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https://api.crossref.org/works/10.1074%2FJBC.M008443200

9 September 2017

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Redox regulation of cellular signalling

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Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity.

21 January 2018

1 reference

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Cloning and sequencing of a human thioredoxin reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

The Caenorhabditis elegans homologue of thioredoxin reductase contains a selenocysteine insertion sequence (SECIS) element that differs from mammalian SECIS elements but directs selenocysteine incorporation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Mutagenesis of the N- and C-terminal cysteine pairs of Tn501 mercuric ion reductase: consequences for bacterial detoxification of mercurials

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

C-terminal cysteines of Tn501 mercuric ion reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Three-dimensional structure of glutathione reductase at 2 Å resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Identification and characterization of the functional amino acids at the active site of the large thioredoxin reductase from Plasmodium falciparum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

The role of the C-terminus for catalysis of the large thioredoxin reductase from Plasmodium falciparum

21 January 2018

1 reference

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

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Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene

21 January 2018

1 reference

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Folding of the four domains and dimerization are impaired by the Gly446-->Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs

21 January 2018

1 reference

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Engineering surface charge. 2. A method for purifying heterodimers of Escherichia coli glutathione reductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Coenzyme A-disulfide reductase from Staphylococcus aureus: evidence for asymmetric behavior on interaction with pyridine nucleotides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Engineering surface charge. 1. A method for detecting subunit exchange in Escherichia coli glutathione reductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Active site complementation in engineered heterodimers of Escherichia coli glutathione reductase created in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M008443200

Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M008443200

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9 September 2017

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