(Q27686951)

8

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

author name string

Liping Zhang

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Hong Zhang

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Yining Zhao

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Zhe Li

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Shangke Chen

5

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Jing Zhai

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Yunyun Chen

7

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Zhong Wang

9

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Qing Li

10

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Xuehua Zheng

11

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

Xiaopeng Hu

12

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

language of work or name

English

0 references

publication date

15 November 2013

0 references

published in

FEBS Letters

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

volume

587

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

issue

22

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

1 June 2020

page(s)

3681-3686

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24100137%20AND%20SRC:MED&resulttype=core&format=json

Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms

1 June 2020

cites work

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

All in the family: aldose reductase and closely related aldo-keto reductases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Aldo-Keto Reductases 1B in Endocrinology and Metabolism

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Identification and characterization of a novel human aldose reductase-like gene

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

AKR1B10 and its emerging role in tumor carcinogenesis and as a cancer biomarker.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Selective inhibition of the tumor marker AKR1B10 by antiinflammatory N-phenylanthranilic acids and glycyrrhetic acid

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Potent and selective inhibition of the tumor marker AKR1B10 by bisdemethoxycurcumin: probing the active site of the enzyme with molecular modeling and site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP(+) and the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

The molecular basis for inhibition of sulindac and its metabolites towards human aldose reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

The CCP4 suite: programs for protein crystallography

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

PHENIX: a comprehensive Python-based system for macromolecular structure solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Coot: model-building tools for molecular graphics

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Aldose reductase from Schistosoma japonicum: crystallization and structure-based inhibitor screening for discovering antischistosomal lead compounds

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

1.7 .ANG. Structure of FR-1, a Fibroblast Growth Factor-Induced Member of the Aldo-Keto Reductase Family, Complexed with Coenzyme and Inhibitor

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Refined 1.8 A structure of human aldose reductase complexed with the potent inhibitor zopolrestat

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Ultrahigh resolution drug design. II. Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat: implications for the binding of cyclic imide inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031

Kinetic studies of AKR1B10, human aldose reductase-like protein: endogenous substrates and inhibition by steroids.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2013.09.031