Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523

Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523

Item
http://www.wikidata.org/entity/Q27747915
Yersinia enterocolitica type III secretion: evidence for the ability to transport proteins that are folded prior to secretionStructural analysis of a holoenzyme complex of mouse dihydrofolate reductase with NADPH and a ternary complex with the potent and selective inhibitor 2,4-diamino-6-(2′-hydroxydibenz[b,f]azepin-5-yl)methylpteridineCrystal Structure of Bacillus anthracis Dihydrofolate Reductase with the Dihydrophthalazine-Based Trimethoprim Derivative RAB1 Provides a Structural Explanation of Potency and SelectivityMultiple Conformers in Active Site of Human Dihydrofolate Reductase F31R/Q35E Double Mutant Suggest Structural Basis for Methotrexate ResistanceTheZisomer of 2,4-diaminofuro[2,3-d]pyrimidine antifolate promotes unusual crystal packing in a human dihydrofolate reductase ternary complexProteochemometric modelling coupled to in silico target prediction: an integrated approach for the simultaneous prediction of polypharmacology and binding affinity/potency of small moleculesTobacco budworm dihydrofolate reductase is a promising target for insecticide discovery.The identification of novel Mycobacterium tuberculosis DHFR inhibitors and the investigation of their binding preferences by using molecular modelling.Advances in quantitative structure-activity relationship models of antimalarials.2,4-Diamino-5-(2'-arylpropargyl)pyrimidine derivatives as new nonclassical antifolates for human dihydrofolate reductase inhibition.In pursuit of virtual lead optimization: the role of the receptor structure and ensembles in accurate docking.In pursuit of virtual lead optimization: pruning ensembles of receptor structures for increased efficiency and accuracy during docking.Interactions of 5-deazapteridine derivatives with Mycobacterium tuberculosis and with human dihydrofolate reductases.Binding mode analysis of 2,4-diamino-5-methyl-5-deaza-6-substituted pteridines with Mycobacterium tuberculosis and human dihydrofolate reductases.
P2860

Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523

Item
http://www.wikidata.org/entity/Q27747915
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
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1997年学术文章
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1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
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name
Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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type
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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Comparison of two independent ...... tight-binding inhibitor PT523
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P2093
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921