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Modelling the catalytic reaction in human aldose reductase
scientific article published on 01 November 1999
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scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
title
Modelling the catalytic reaction in human aldose reductase
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
author name string
Várnai P
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Richards WG
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
Lyne PD
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
publication date
1 November 1999
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
published in
Proteins
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
volume
37
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
issue
2
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
page(s)
218-227
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
cites work
Substrate specificity of human aldose reductase: identification of 4-hydroxynonenal as an endogenous substrate
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Crossref
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21 January 2018
Aldose reductase: model for a new paradigm of enzymic perfection in detoxification catalysts
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21 January 2018
Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase.
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21 January 2018
The role of aldose reductase in the development of diabetic complications
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Mechanistic basis for nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase
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An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications
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21 January 2018
Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme
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Aldose reductase as a target for drug design: molecular modeling calculations on the binding of acyclic sugar substrates to the enzyme
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A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil
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21 January 2018
Human Aldose Reductase: pK of Tyrosine 48 Reveals the Preferred Ionization State for Catalysis and Inhibition
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Computer simulation and analysis of the reaction pathway of triosephosphate isomerase
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Simulation of the enzyme reaction mechanism of malate dehydrogenase
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An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate
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Comparison of simple potential functions for simulating liquid water
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Calculations of electrostatic interactions in biological systems and in solutions
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Novel NADPH-binding domain revealed by the crystal structure of aldose reductase
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Multiple replacements establish the importance of tyrosine-503 in beta-galactosidase (Escherichia coli).
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Kinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomerase
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Stereochemistry of the concerted enolization catalyzed by delta 5-3-ketosteroid isomerase
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Structure of porcine aldehyde reductase holoenzyme.
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Catalytic mechanism of aldose reductase studied by the combined potentials of quantum mechanics and molecular mechanics
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The application of hydrogen bonding analysis in X-ray crystallography to help orientate asparagine, glutamine and histidine side chains
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All in the family
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Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability
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21 January 2018
Human aldose reductase: rate constants for a mechanism including interconversion of ternary complexes by recombinant wild-type enzyme
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21 January 2018
Mechanism of human aldehyde reductase: characterization of the active site pocket
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retrieved
21 January 2018
Identifiers
DOI
10.1002/(SICI)1097-0134(19991101)37:2<218::AID-PROT7>3.0.CO;2-E
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
PubMed ID
10584067
1 reference
stated in
Europe PubMed Central
PubMed ID
10584067
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10584067%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
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