A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.

about

Reconstituted IMPDH polymers accommodate both catalytically active and inactive conformations.IMP/GTP balance modulates cytoophidium assembly and IMPDH activity.

P2860

Q47113122-DFA5DF8F-DD5F-4969-AF19-D6736C04403C Q55382907-C1F1F8C4-3BCC-40D2-AEDE-D15E3DF36FD4

P2860

A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.

Item

http://www.wikidata.org/entity/Q41966229

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

A nucleotide-controlled confor ...... eukaryotic IMP dehydrogenases.

@en

type

Item

label

A nucleotide-controlled confor ...... eukaryotic IMP dehydrogenases.

@en

prefLabel

A nucleotide-controlled confor ...... eukaryotic IMP dehydrogenases.

@en

P1476

A nucleotide-controlled confor ...... eukaryotic IMP dehydrogenases

@en

P2093

David Fernández-Justel

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

Graeme Winter

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

José Luis Revuelta

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

Rubén M Buey

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

P2860

Autosomal dominant retinitis pigmentosa mutations in inosine 5'-monophosphate dehydrogenase type I disrupt nucleic acid binding

CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations

IMP dehydrogenase: structure, mechanism, and inhibition.

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms

Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design

Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase

The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase

Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes

MgATP regulates allostery and fiber formation in IMPDHs

P2888

s41598-017-02805-x

P304

2648

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

P31

scholarly article

P356

10.1038/S41598-017-02805-X

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

P407

English

P433

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

P478

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

P50

José M de Pereda

Paulino Gómez-Puertas

Iñigo Marcos-Alcalde

P577

2017-06-01T00:00:00Z

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

P698

28572600

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

P932

5454003

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

A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.

about

P2860

P2860

A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932