Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions - Wikidata - wikimedia - TriplyDB

Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions

Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions

http://www.wikidata.org/entity/Q35424122

about

Structure-based analysis of Bacilli and plasmid dihydrofolate reductase evolution.Protein engineering in the 21st century.Small Angle Neutron Scattering Studies of R67 Dihydrofolate Reductase, a Tetrameric Protein with Intrinsically Disordered N-Termini.

P2860

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P2860

Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active-site substitutions

http://www.wikidata.org/entity/Q35424122

description

2014 nî lūn-bûn

@nan

2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Asymmetric mutations in the te ...... e to active-site substitutions

@ast

Asymmetric mutations in the te ...... e to active-site substitutions

@en

type

label

Asymmetric mutations in the te ...... e to active-site substitutions

@ast

Asymmetric mutations in the te ...... e to active-site substitutions

@en

prefLabel

Asymmetric mutations in the te ...... e to active-site substitutions

@ast

Asymmetric mutations in the te ...... e to active-site substitutions

@en

P1433

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P1433

Protein Science

P1476

Asymmetric mutations in the te ...... e to active-site substitutions

@en

P2093

Andreea R Schmitzer

http://www.w3.org/2001/XMLSchema#string

Joelle N Pelletier

http://www.w3.org/2001/XMLSchema#string

Jordan P Volpato

http://www.w3.org/2001/XMLSchema#string

Krista L Morley

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal Structure of a Type II Dihydrofolate Reductase Catalytic Ternary Complex †

Novel crystallization conditions for tandem variant R67 DHFR yield a wild-type crystal structure

A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

Crystal structure of a novel trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67.

Combinatorial exploration of the catalytic site of a drug-resistant dihydrofolate reductase: creating alternative functional configurations.

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination.

The emergence and spread of antibiotic resistance in food-borne bacteria.

Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein.

Tricine-SDS-PAGE.

P304

495-507

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/PRO.2602

http://www.w3.org/2001/XMLSchema#string

P433

4

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P478

24

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P50

Maximilian Ebert

P577

2014-12-26T00:00:00Z

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P5875

268984902

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P698

25401264

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P932

4380981

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