Detecting the active conformation of calpain with calpastatin-based reagents.

about

Unexpected role of the L-domain of calpastatin during the autoproteolytic activation of human erythrocyte calpain.

P2860

Q52639440-AB5A48C3-6359-478B-9F25-CCBB96273F0B

P2860

Detecting the active conformation of calpain with calpastatin-based reagents.

Item

http://www.wikidata.org/entity/Q42094050

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Detecting the active conformation of calpain with calpastatin-based reagents.

@en

Detecting the active conformation of calpain with calpastatin-based reagents.

@nl

type

Item

label

Detecting the active conformation of calpain with calpastatin-based reagents.

@en

Detecting the active conformation of calpain with calpastatin-based reagents.

@nl

prefLabel

Detecting the active conformation of calpain with calpastatin-based reagents.

@en

Detecting the active conformation of calpain with calpastatin-based reagents.

@nl

P1476

Detecting the active conformation of calpain with calpastatin-based reagents.

@en

P2093

Dorothy E Croall

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

Lisa M Vanhooser

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

Robert E Cashon

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

P2860

The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium

Calcium-induced tripartite binding of intrinsically disordered calpastatin to its cognate enzyme, calpain

Labeling of fusion proteins with synthetic fluorophores in live cells

m-Calpain is required for preimplantation embryonic development in mice.

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation.

A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor

Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement

Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

P304

1676-1686

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

P31

scholarly article

P356

10.1016/J.BBAPAP.2008.08.013

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

P433

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

P478

1784

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

P577

2008-08-28T00:00:00Z

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

P698

18793761

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

P932

2646846

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

Detecting the active conformation of calpain with calpastatin-based reagents.

about

P2860

P2860

Detecting the active conformation of calpain with calpastatin-based reagents.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932