wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs. - Wikidata - awgldk - TriplyDB

wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.

wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.

http://www.wikidata.org/entity/Q37697445

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In vitro activity of wALADin benzimidazoles against different life cycle stages of Plasmodium parasites.Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.

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P2860

wALADin benzimidazoles differentially modulate the function of porphobilinogen synthase orthologs.

http://www.wikidata.org/entity/Q37697445

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 25 February 2014

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

@en

wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

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type

label

wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

@en

wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

@nl

prefLabel

wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

@en

wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

@nl

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Journal of Medicinal Chemistry

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wALADin benzimidazoles differe ...... obilinogen synthase orthologs.

@en

P2093

Achim Hoerauf

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Jeffrey S Hannam

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Michael Famulok

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Sarah H Lawrence

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Silke Strassel

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Victoria S Halls

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P2860

Allostery and the dynamic oligomerization of porphobilinogen synthase

Expanding the concepts in protein structure-function relationships and enzyme kinetics: Teaching using morpheeins

Shape shifting leads to small-molecule allosteric drug discovery

Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer

X-ray structure of 5-aminolevulinic acid dehydratase from Escherichia coli complexed with the inhibitor levulinic acid at 2.0 A resolution

High resolution crystal structure of a Mg2+-dependent porphobilinogen synthase

Control of tetrapyrrole biosynthesis by alternate quaternary forms of porphobilinogen synthase

Structure of the Heme Biosynthetic Pseudomonas aeruginosa Porphobilinogen Synthase in Complex with the Antibiotic Alaremycin

Crystal Structure of Toxoplasma gondii Porphobilinogen Synthase

The heme biosynthetic pathway of the obligate Wolbachia endosymbiont of Brugia malayi as a potential anti-filarial drug target

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2498-2510

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scholarly article

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10.1021/JM401785N

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6

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57

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Christian S Lentz

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2014-02-25T00:00:00Z

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260380220

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24568185

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3983392

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