Follistatin N terminus differentially regulates muscle size and fat in vivo.

about

Neonatal Systemic AAV-Mediated Gene Delivery of GDF11 Inhibits Skeletal Muscle Growth.

P2860

Q54262478-056045E9-BFC3-4DA0-A317-89E29A5D4B2F

P2860

Follistatin N terminus differentially regulates muscle size and fat in vivo.

Item

http://www.wikidata.org/entity/Q40040011

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

Follistatin N terminus differentially regulates muscle size and fat in vivo.

@en

type

Item

label

Follistatin N terminus differentially regulates muscle size and fat in vivo.

@en

prefLabel

Follistatin N terminus differentially regulates muscle size and fat in vivo.

@en

P1476

Follistatin N terminus differentially regulates muscle size and fat in vivo.

@en

P2093

Chunping Qiao

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

Chunxia Zhao

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

Hui Zheng

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

Jianbin Li

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

Juan Li

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

Karen Bulaklak

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

Ruhang Tang

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

Xiao Xiao

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

Yi Dai

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

Zhenhua Huang

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

P2860

Structural basis for the inhibition of activin signalling by follistatin.

Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors

Differential biosynthesis and intracellular transport of follistatin isoforms and follistatin-like-3

The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding

TGF beta signals through a heteromeric protein kinase receptor complex

Production of high-titer recombinant adeno-associated virus vectors in the absence of helper adenovirus

Regulation of myostatin activity and muscle growth

Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin

The Structure of FSTL3{middle dot}Activin A Complex: DIFFERENTIAL BINDING OF N-TERMINAL DOMAINS INFLUENCES FOLLISTATIN-TYPE ANTAGONIST SPECIFICITY

The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding

P2888

emm.2017.135

P304

e377

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

P31

scholarly article

P356

10.1038/EMM.2017.135

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

P433

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

P478

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

P577

2017-09-15T00:00:00Z

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

P6179

1091774390

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

P698

28912572

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

P932

5628274

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

Follistatin N terminus differentially regulates muscle size and fat in vivo.

about

P2860

P2860

Follistatin N terminus differentially regulates muscle size and fat in vivo.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P6179

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P6179

P698

P932