Energetics of Glutathione Binding to Human Eukaryotic Elongation Factor 1 Gamma: Isothermal Titration Calorimetry and Molecular Dynamics Studies.

about

Energetics of Glutathione Binding to Human Eukaryotic Elongation Factor 1 Gamma: Isothermal Titration Calorimetry and Molecular Dynamics Studies.

Item

http://www.wikidata.org/entity/Q39187517

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

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

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Energetics of Glutathione Bind ...... nd Molecular Dynamics Studies.

@en

Energetics of Glutathione Bind ...... nd Molecular Dynamics Studies.

@nl

type

Item

label

Energetics of Glutathione Bind ...... nd Molecular Dynamics Studies.

@en

Energetics of Glutathione Bind ...... nd Molecular Dynamics Studies.

@nl

prefLabel

Energetics of Glutathione Bind ...... nd Molecular Dynamics Studies.

@en

Energetics of Glutathione Bind ...... nd Molecular Dynamics Studies.

@nl

P1476

Energetics of Glutathione Bind ...... and Molecular Dynamics Studies

@en

P2093

Allan Prior

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

Mihai-Silviu Tomescu

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

Thabiso N Tshabalala

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

Vijayakumar Balakrishnan

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

Yasien Sayed

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

P2860

I-TASSER server for protein 3D structure prediction

3DLigandSite: predicting ligand-binding sites using similar structures

Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling

ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins

Optimization by Simulated Annealing

PROCHECK: a program to check the stereochemical quality of protein structures

1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site

The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae

Arginine 15 stabilizes an S(N)Ar reaction transition state and the binding of anionic ligands at the active site of human glutathione transferase A1-1

Structural Insights into Omega-Class Glutathione Transferases: A Snapshot of Enzyme Reduction and Identification of a Non-Catalytic Ligandin Site

P2888

s10930-016-9688-4

P304

448-458

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

P31

scholarly article

P356

10.1007/S10930-016-9688-4

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

P433

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

P478

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

P50

Heini W Dirr

Ikechukwu Achilonu

P577

2016-12-01T00:00:00Z

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

P698

27844275

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