Digestion of mu- and m-calpain by trypsin and chymotrypsin. (Q53929603)

22 May 2018

title

Digestion of mu- and m-calpain by trypsin and chymotrypsin. (English)

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22 May 2018

author name string

Valery F Thompson

1

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22 May 2018

Kathryn R Lawson

2

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22 May 2018

James Barlow

3

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22 May 2018

Darrel E Goll

4

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22 May 2018

publication date

1 May 2003

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22 May 2018

Biochimica et Biophysica Acta

published in

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22 May 2018

volume

1648

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22 May 2018

issue

1-2

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22 May 2018

page(s)

140-153

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22 May 2018

Proteolytic enzymes as probes of the secondary structure of fibrous proteins

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Effect of trypsin on rabbit skeletal muscle alpha-actinin

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

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

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Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin?

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Ca(2+)-induced structural changes in rat m-calpain revealed by partial proteolysis

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Comparison of the autolyzed and unautolyzed forms of mu- and m-calpain from bovine skeletal muscle

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Separation of peptides on the basis of the difference in positive charge: simultaneous isolation of C-terminal and blocked N-terminal peptides from tryptic digests

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

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Measurement of protein using bicinchoninic acid

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Two-stage autolysis of the catalytic subunit initiates activation of calpain I

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7 January 2021

Structural modifications associated with the change in Ca2+ sensitivity on activation of m-calpain

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Structural Basis for Possible Calcium-Induced Activation Mechanisms of Calpains

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

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

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A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases

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Casein zymography: a method to study mu-calpain, m-calpain, and their inhibitory agents

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Human micro-calpain: simple isolation from erythrocytes and characterization of autolysis fragments

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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

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7 January 2021

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

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7 January 2021

10.1016/S1570-9639(03)00115-8

Identifiers

DOI

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22 May 2018

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22 May 2018