Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

about

cCMP and cUMP Across the Tree of Life: From cCMP and cUMP Generators to cCMP- and cUMP-Regulated Cell Functions.

P2860

Q50456694-07D3FD34-A46E-473A-A1A8-2AD03263EE63

P2860

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

Item

http://www.wikidata.org/entity/Q46452983

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@en

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@nl

type

Item

label

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@en

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@nl

prefLabel

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@en

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@nl

P1476

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

@en

P2093

Stefan Dove

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

P2860

Cytosolic adenylyl cyclase defines a unique signaling molecule in mammals

Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate

Crystal structures of the catalytic domain of human soluble guanylate cyclase

Crystal structures of human soluble adenylyl cyclase reveal mechanisms of catalysis and of its activation through bicarbonate

Two-metal-Ion catalysis in adenylyl cyclase

Molecular basis for P-site inhibition of adenylyl cyclase

PAS-mediated Dimerization of Soluble Guanylyl Cyclase Revealed by Signal Transduction Histidine Kinase Domain Crystal Structure

Structural Basis for Inhibition of Mammalian Adenylyl Cyclase by Calcium †

Crystal Structure of Human Soluble Adenylate Cyclase Reveals a Distinct, Highly Flexible Allosteric Bicarbonate Binding Pocket

Interfacial residues promote an optimal alignment of the catalytic center in human soluble guanylate cyclase: heterodimerization is required but not sufficient for activity.

P304

49-66

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

P31

scholarly article

P356

10.1007/164_2015_34

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

P478

238

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

P577

2016-11-30T00:00:00Z

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

P698

27900607

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

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

about

P2860

P2860

Mammalian Nucleotidyl Cyclases and Their Nucleotide Binding Sites.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698