Domain II of m-calpain is a Ca(2+)-dependent cysteine protease (Q42655298)

4 November 2017

Domain II of m-calpain is a Ca(2+)-dependent cysteine protease (English)

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4 November 2017

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4 November 2017

Hata S

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4 November 2017

Nakagawa K

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4 November 2017

Maeda T

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4 November 2017

Abe K

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4 November 2017

Suzuki K

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4 November 2017

language of work or name

English

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publication date

1 July 2001

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4 November 2017

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4 November 2017

501

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2-3

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4 November 2017

111-114

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Calpain: a protease in search of a function?

4 November 2017

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Structure and physiological function of calpains

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Calpain and caspase: can you tell the difference?

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

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

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

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

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

C2-domains, structure and function of a universal Ca2+-binding domain

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Site-directed activation of calpain is promoted by a membrane-associated natural activator protein

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Molecular and functional properties of a calpain activator protein specific for mu-isoforms.

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Mechanism of action of a new component of the Ca(2+)-dependent proteolytic system in rat brain: the calpain activator.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Crystal structure of calcium bound domain VI of calpain at 1.9 A resolution and its role in enzyme assembly, regulation, and inhibitor binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Molecular cloning and analysis of small optic lobes, a structural brain gene of Drosophila melanogaster

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

VMD: visual molecular dynamics

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Structure and physiology of calpain, an enigmatic protease

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

A novel aspect of calpain activation

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Domain III of calpain is a ca2+-regulated phospholipid-binding domain

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902611-4

10.1016/S0014-5793(01)02611-4

7 January 2021

Identifiers

DOI

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4 November 2017

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