Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

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Adenoviral neutral endopeptidase gene delivery in combination with paclitaxel for the treatment of prostate cancer.

P2860

Q39297022-3FE58286-4F2A-4338-9ED9-F4E104209284

P2860

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

Item

http://www.wikidata.org/entity/Q42606516

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

@en

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

@nl

type

Item

label

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

@en

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

@nl

prefLabel

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

@en

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

@nl

P1476

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins

@en

P2093

Akio Horiguchi

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

David M Nanus

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

Katsuyuki Iida

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

Rong Zheng

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

Ruoqian Shen

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

P2860

Homology modeling using parametric alignment ensemble generation with consensus and energy-based model selection

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.

Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex

Structural basis of PSGL-1 binding to ERM proteins

Structural Basis for CD44 Recognition by ERM Proteins

VMD: visual molecular dynamics

Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation

Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation

The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44

P304

1042-1050

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

P31

scholarly article

P356

10.1002/PRO.114

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

P433

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

P478

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

P50

Masha Niv

P577

2009-05-01T00:00:00Z

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

P5875

24351372

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

P698

19388049

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

P932

2771306

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

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

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P2860

P2860

Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P5875

P698

P932