The NMR contribution to protein-protein networking in Fe-S protein maturation.

about

NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis

P2860

Q58778523-21181EC1-D9C2-4608-BF9E-3269922FD321

P2860

The NMR contribution to protein-protein networking in Fe-S protein maturation.

Item

http://www.wikidata.org/entity/Q52641197

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

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@en

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@nl

type

Item

label

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@en

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@nl

prefLabel

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@en

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@nl

P1476

The NMR contribution to protein-protein networking in Fe-S protein maturation.

@en

P2093

Francesca Camponeschi

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

Mario Piccioli

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

P275

Creative Commons Attribution 4.0 International

P2860

Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster

Human ind1, an iron-sulfur cluster assembly factor for respiratory complex I

Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis

MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism

MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity

A novel eukaryotic factor for cytosolic Fe-S cluster assembly

Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery

A refined model for the solution structure of oxidized putidaredoxin

A model for the solution structure of oxidized terpredoxin, a Fe2S2 ferredoxin from Pseudomonas

The solution structure of a [3Fe-4S] ferredoxin: oxidised ferredoxin II from Desulfovibrio gigas

P2888

s00775-018-1552-x

P304

665-685

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

P31

scholarly article

review article

P356

10.1007/S00775-018-1552-X

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

P433

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

P478

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

P50

Lucia Banci

Simone Ciofi-Baffoni

P577

2018-03-22T00:00:00Z

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

2018-06-01T00:00:00Z

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

P698

29569085

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

P921

metalloprotein

biomedical investigative technique

P932

6006191

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

The NMR contribution to protein-protein networking in Fe-S protein maturation.

about

P2860

P2860

The NMR contribution to protein-protein networking in Fe-S protein maturation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P275

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P275

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932