(Q44626786)

English

Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter

scientific article published on 21 October 2003

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scholarly article

1 reference

Europe PubMed Central

4 December 2017

Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter (English)

1 reference

Europe PubMed Central

4 December 2017

1 reference

based on heuristic

inferred from title

author name string

Kai-Hui Wu

1

1 reference

Europe PubMed Central

4 December 2017

Phang C Tai

2

1 reference

Europe PubMed Central

4 December 2017

language of work or name

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publication date

21 October 2003

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Europe PubMed Central

4 December 2017

Journal of Biological Chemistry

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Europe PubMed Central

4 December 2017

279

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Europe PubMed Central

4 December 2017

2

1 reference

Europe PubMed Central

4 December 2017

901-909

1 reference

Europe PubMed Central

4 December 2017

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1 reference

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1 reference

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1 reference

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Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis

1 reference

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Heterologous protein secretion and the versatile Escherichia coli haemolysin translocator

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A family of bacteriocin ABC transporters carry out proteolytic processing of their substrates concomitant with export

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Processing of colicin V-1, a secretable marker protein of a bacterial ATP binding cassette export system, requires membrane integrity, energy, and cytosolic factors.

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1 reference

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1 reference

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Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly and cell spreading

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21 January 2018

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

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21 January 2018

Luminescence spectroscopy

1 reference

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Dissociation and aggregation of calpain in the presence of calcium

1 reference

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Biochemical characteristics of caspases-3, -6, -7, and -8

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Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis

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

1 reference

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M308296200

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

1 reference

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Evidence for histidine in the active site of papain

1 reference

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Identification of active-site amino acid residues in the Chiba virus 3C-like protease

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Studies on transformation of Escherichia coli with plasmids

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Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

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Identifiers

10.1074/JBC.M308296200

1 reference

Europe PubMed Central

4 December 2017

1 reference

Europe PubMed Central

4 December 2017

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