Substrate independent ATPase activity may complicate high throughput screening.

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Substrate independent ATPase activity may complicate high throughput screening.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

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2016年论文

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2016年论文

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Substrate independent ATPase activity may complicate high throughput screening.

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Substrate independent ATPase activity may complicate high throughput screening.

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Substrate independent ATPase activity may complicate high throughput screening.

@en

P1476

Substrate independent ATPase activity may complicate high throughput screening.

@en

P2093

L W-M Fung

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Micheal L Tuntland

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P2860

Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis

Structures of SAICAR synthetase (PurC) from Streptococcus pneumoniae with ADP, Mg2+, AIR and Asp

The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis

A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays

Rank ordering plate data facilitates data visualization and normalization in high-throughput screening

Three mechanistically distinct kinase assays compared: Measurement of intrinsic ATPase activity identified the most comprehensive set of ITK inhibitors.

High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK.

Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase.

Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase.

Genetic and proteomic analyses of a Xanthomonas campestris pv. campestris purC mutant deficient in purine biosynthesis and virulence.

P304

18-20

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P31

scholarly article

P356

10.1016/J.AB.2016.07.016

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P407

English

P478

510

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P577

2016-07-15T00:00:00Z

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P698

27430931

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P932

4980188

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