Specificity of neuropeptide degradation by two calcium-activated neutral proteases from human skeletal muscle-Reference-Cited by-同舟云学术

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Specificity of neuropeptide degradation by two calcium-activated neutral proteases from human skeletal muscle

Published:1985-08 Issue:8 Volume:37 Page:725-730
ISSN:0024-3205
Container-title:Life Sciences
language:en
Short-container-title:Life Sciences

Author:

McDermott JR,Mantle D,Biggins JA,Kidd AM,Davison K,Lauffart B,Pennington RJT

Publisher

Elsevier BV

Subject

General Pharmacology, Toxicology and Pharmaceutics,General Biochemistry, Genetics and Molecular Biology,General Medicine

Reference15 articles.

1. Characterization of a brain calcium-activated protease that degrades neurofilament proteins

2. Purification and characterization of two forms of Ca2+-activated neutral protease from calf brain.

3. A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme

4. Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.

5. Progesterone-binding components of chick oviduct: partial purification and characterization of a calcium-activated protease which hydrolyzes the progesterone receptor

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1. An easy-to-use FRET protein substrate to detect calpain cleavage in vitro and in vivo;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;2018-02

2. Calpain-3-mediated regulation of the Na+-Ca2+ exchanger isoform 3;Pflügers Archiv - European Journal of Physiology;2015-10-27

3. Determination of Peptide Substrate Specificity for μ-Calpain by a Peptide Library-based Approach;Journal of Biological Chemistry;2005-12

4. Mechanism of Production of Troponin T Fragments during Postmortem Aging of Porcine Muscle;Journal of Agricultural and Food Chemistry;2005-04-16

5. Adverse and Beneficial Functions of Proteolytic Enzymes in Skeletal Muscle;Adverse Drug Reactions and Toxicological Reviews;2002-03

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