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

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

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Unexpected role of the L-domai ...... of human erythrocyte calpain.

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Unexpected role of the L-domai ...... of human erythrocyte calpain.

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label

Unexpected role of the L-domai ...... of human erythrocyte calpain.

@en

Unexpected role of the L-domai ...... of human erythrocyte calpain.

@nl

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Unexpected role of the L-domai ...... of human erythrocyte calpain.

@en

Unexpected role of the L-domai ...... of human erythrocyte calpain.

@nl

P1476

Unexpected role of the L-domai ...... of human erythrocyte calpain.

@en

P2093

Alice Franchi

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Antonino Martines

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Bianca Sparatore

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Edon Melloni

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Marco Pedrazzi

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Monica Averna

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Roberta De Tullio

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P2860

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

The Ca(2+)-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel

A Ca(2+) switch aligns the active site of calpain

Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains

Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin

Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization

Molecular diversity in amino-terminal domains of human calpastatin by exon skipping

The calpain system

Degradation of PEP-19, a calmodulin-binding protein, by calpain is implicated in neuronal cell death induced by intracellular Ca2+ overload

Calpain-mediated proteolysis of paxillin negatively regulates focal adhesion dynamics and cell migration.

P31

scholarly article

P356

10.1042/BSR20180147

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P433

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P478

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P577

2018-04-20T00:00:00Z

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P698

29572388

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P932

5968184

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