(Q58850244)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24189737%20AND%20SRC:MED&resulttype=core&format=json

29 February 2020

title

Rational design of peptide-based inhibitors of trypanothione reductase as potential antitrypanosomal drugs (English)

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29 February 2020

5

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29 February 2020

author name string

J Garforth

1

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29 February 2020

J H McKie

2

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29 February 2020

R Jaouhari

3

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29 February 2020

T J Benson

4

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29 February 2020

K T Douglas

6

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29 February 2020

publication date

1 October 1994

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29 February 2020

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29 February 2020

volume

6

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29 February 2020

issue

3

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29 February 2020

page(s)

295-299

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https://scigraph.springernature.com/pub.10.1007/bf00813749

29 February 2020

exact match

0 references

cites work

Refined structure of glutathione reductase at 1.54 A resolution

1 reference

12 December 2020

Expression of Trypanosoma congolense trypanothione reductase in Escherichia coli: overproduction, purification, and characterization

1 reference

12 December 2020

Rationally designed selective inhibitors of trypanothione reductase. Phenothiazines and related tricyclics as lead structures

1 reference

12 December 2020

X-ray structure of trypanothione reductase from Crithidia fasciculata at 2.4-A resolution

1 reference

12 December 2020

Human glutathione reductase: purification of the crystalline enzyme from erythrocytes.

1 reference

12 December 2020

Synthesis of N-benzyloxycarbonyl-l-cysteinylglycine 3-dimethylaminopropylamide disulfide: A cheap and convenient new assay for trypanothione reductase

1 reference

12 December 2020

Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide

1 reference

12 December 2020

Active site of trypanothione reductase. A target for rational drug design.

1 reference

12 December 2020

Molecular studies on trypanothione reductase, a target for antiparasitic drugs

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF00813749

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29 February 2020

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