(Q54610418)

English

Purification of mu-calpain by a novel affinity chromatography approach. New insights into the mechanism of the interaction of the protease with targets.

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

Purification of mu-calpain by a novel affinity chromatography approach. New insights into the mechanism of the interaction of the protease with targets. (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

Maurizio Molinari

1

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

author name string

Maki M

2

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

Carafoli E

3

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

language of work or name

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publication date

1 June 1995

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

270

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

24

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

14576-14581

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

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1 reference

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Presence of calpain II immunoreactivity in senile plaques in Alzheimer's disease.

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Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis

1 reference

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PEST sequences do not influence substrate susceptibility to calpain proteolysis.

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The design of peptidyldiazomethane inhibitors to distinguish between the cysteine proteinases calpain II, cathepsin L and cathepsin B

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Interaction of calmodulin with the calmodulin binding domain of the plasma membrane Ca2+ pump

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The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction domain of the enzyme

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Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains

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Affinity labelling of the Ca(2+)-activated neutral proteinase (calpain) in intact human platelets

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An improved assay for nanomole amounts of inorganic phosphate

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Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?

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A Calcium-Dependent Protein Kinase with a Regulatory Domain Similar to Calmodulin

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Protein kinases with calmodulin-like domains: novel targets of calcium signals in plants

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Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus

1 reference

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Stimulation of NMDA receptors activates calpain in cultured hippocampal slices

1 reference

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Further characterization of calpain-mediated proteolysis of the human erythrocyte plasma membrane Ca2+-ATPase

1 reference

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21 January 2018

Identifiers

10.1074/JBC.270.24.14576

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7782321

ResearchGate publication ID

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