Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

about

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

Item

http://www.wikidata.org/entity/Q55154096

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@en

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@nl

type

Item

label

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@en

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@nl

prefLabel

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@en

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@nl

P1476

Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.

@en

P2093

Katelyn Stine

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

Martin St Maurice

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

P2860

A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A

Molecular structure of a 9-MDa icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopy

Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA

The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together

Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme

Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction

The crystal structure of a mammalian fatty acid synthase

Interaction between the Biotin Carboxyl Carrier Domain and the Biotin Carboxylase Domain in Pyruvate Carboxylase from Rhizobium etli

Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains

A Substrate-induced Biotin Binding Pocket in the Carboxyltransferase Domain of Pyruvate Carboxylase

P2888

s41467-018-03814-8

P304

1384

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

P31

scholarly article

P356

10.1038/S41467-018-03814-8

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

Melissa M Budelier

Yumeng Liu

P577

2018-04-11T00:00:00Z

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

P6179

1103213309

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

P698

29643369

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

P932

5895798

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