Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

about

Development of α-helical calpain probes by mimicking a natural protein-protein interaction.Physiologic and pathophysiologic role of calpain: implications for the occurrence of atrial fibrillation.Atrial Calpains: Mediators of Atrialmyopathies in Atrial Fibrillation.

P2860

Q36469004-CC357180-90E0-47A8-A163-FC8D020E987D Q37812402-E2756A32-A2EB-4E68-98C0-3FC0BD2759FD Q39036936-738A010C-048E-487E-BD5F-CD71C40D0A9D

P2860

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

Item

http://www.wikidata.org/entity/Q46839254

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年学术文章

@wuu

2008年学术文章

@zh-cn

2008年学术文章

@zh-hans

2008年学术文章

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh

2008年學術文章

@zh-hant

name

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@en

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@nl

type

Item

label

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@en

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@nl

prefLabel

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@en

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@nl

P1476

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

@en

P2093

Irmgard Assfalg-Machleidt

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

José Pfizer

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

Norbert Schaschke

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

Werner Machleidt

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

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

Characterization of a functional domain of human calpastatin

Calpastatin simultaneously binds four calpains with different kinetic constants

Intrinsically unstructured proteins

Natively unfolded proteins: a point where biology waits for physics

The beta- and gamma-CH2 of B27-WT's Leu11 and Ile18 side chains play a direct role in calpain inhibition.

Bicyclic homodetic peptide libraries: comparison of synthetic strategies for their solid-phase synthesis.

Interaction of calpastatin with calpain: a review.

P304

83-90

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

P31

scholarly article

P356

10.1515/BC.2008.004

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

P433

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

P478

389

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

P577

2008-01-01T00:00:00Z

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

P698

18095873

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

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

about

P2860

P2860

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698