Page last updated: 2024-08-25

leupeptin and calpastatin

leupeptin has been researched along with calpastatin in 15 studies

Research

Studies (15)

TimeframeStudies, this research(%)All Research%
pre-19904 (26.67)18.7374
1990's4 (26.67)18.2507
2000's5 (33.33)29.6817
2010's2 (13.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Schlaepfer, WW; Zimmerman, UJ2
Adachi, Y; Hatanaka, M; Lee, WJ; Maki, M; Murachi, T1
Hayashi, M; Inomata, M; Kawashima, S; Nakamura, M; Saito, Y1
Ando, Y; Imamura, S; Kannagi, R; Kitahara, A; Murachi, T; Saji, H; Yamagata, Y1
Hatanaka, M; Kannagi, R; Murachi, T; Murakami, T; Yoshimura, N1
Balcerzak, D; Brustis, JJ; Cottin, P; Ducastaing, A; Elamrani, N; Poussard, S; Safwate, A; Soriano, M1
Hattori, A; Takahashi, K; Tatsumi, R1
Maupoil, V; Perrin, C; Rochette, L; Vergely, C; Zeller, M1
Imai, M; Ishibashi, K; Mochizuki, T; Ohki, G; Somlo, S; Suzuki, M1
Baum, MA; Hammond, TG; Harris, HW; Puliyanda, DP; Ward, DT1
Beis, I; Gaitanaki, C; Papazafiri, P1
Brustis, JJ; Cottin, P; Dargelos, E; Dedieu, S; Grise, F; Mazères, G; Poussard, S1
Acosta, P; Barton, E; Carver, T; Pendrak, K; Pham, J; Selsby, J; Sweeney, HL; Tian, Z; Zadel, M1
Campbell, RL; Davies, PL; McCartney, CE; Ye, Q1

Other Studies

15 other study(ies) available for leupeptin and calpastatin

ArticleYear
Two-stage autolysis of the catalytic subunit initiates activation of calpain I.
    Biochimica et biophysica acta, 1991, Jun-24, Volume: 1078, Issue:2

    Topics: Amino Acid Sequence; Animals; Calcium; Calcium-Binding Proteins; Calpain; Carbohydrate Sequence; Cattle; Enzyme Activation; Erythrocytes; Leupeptins; Molecular Sequence Data

1991
Factors influencing the binding of calpain I to human erythrocyte inside-out vesicles.
    Biochemistry international, 1990, Volume: 22, Issue:1

    Topics: Arginase; Calcium; Calcium-Binding Proteins; Calpain; Caseins; Erythrocyte Membrane; Humans; Immunoelectrophoresis; Immunoglobulins; Leupeptins; Models, Biological; Muramidase; Ovalbumin; Protease Inhibitors

1990
Properties of erythrocyte membrane binding and autolytic activation of calcium-activated neutral protease.
    The Journal of biological chemistry, 1989, Nov-05, Volume: 264, Issue:31

    Topics: Animals; Blood Proteins; Calcium; Calcium-Binding Proteins; Calpain; Caseins; Chickens; Egtazic Acid; Enzyme Activation; Erythrocyte Membrane; Immunoblotting; Kinetics; Leupeptins; Macromolecular Substances; Membrane Proteins; Mice; Molecular Weight; Rabbits; Vimentin

1989
Calcium-activated neutral proteases (calpains) are carbohydrate binding proteins.
    The Journal of biological chemistry, 1988, Aug-25, Volume: 263, Issue:24

    Topics: Calcium; Calcium-Binding Proteins; Calpain; Carbohydrate Metabolism; Chromatography; Disaccharides; Enzyme Activation; Ethylene Glycol; Ethylene Glycols; Leupeptins; Octoxynol; Polyethylene Glycols; Sepharose; Thiocyanates; Urea

1988
Platelet factor XIII is activated by calpain.
    Biochemical and biophysical research communications, 1987, Apr-14, Volume: 144, Issue:1

    Topics: Blood Platelets; Calcium; Calcium-Binding Proteins; Calpain; Enzyme Activation; Factor XIII; Humans; In Vitro Techniques; Leupeptins; Thrombin; Transglutaminases

1987
Evidence for membrane-associated calpain I in human erythrocytes. Detection by an immunoelectrophoretic blotting method using monospecific antibody.
    Biochemistry, 1984, Jul-03, Volume: 23, Issue:14

    Topics: Antibodies, Monoclonal; Calcium; Calcium-Binding Proteins; Calpain; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Erythrocyte Membrane; Humans; Immunoelectrophoresis; Immunoglobulin G; Leupeptins; Protease Inhibitors

1984
Rat myoblast fusion requires exteriorized m-calpain activity.
    European journal of cell biology, 1994, Volume: 64, Issue:2

    Topics: Animals; Biological Assay; Calcium-Binding Proteins; Calpain; Cell Fusion; Cells, Cultured; Culture Media; Immunoglobulin G; Immunohistochemistry; Kinetics; Leupeptins; Muscle Fibers, Skeletal; Rats; Rats, Wistar

1994
Deterioration of connectin/titin and nebulin filaments by an excess of protease inhibitors.
    Bioscience, biotechnology, and biochemistry, 1998, Volume: 62, Issue:5

    Topics: Animals; Calcium-Binding Proteins; Connectin; Cysteine Proteinase Inhibitors; Leupeptins; Muscle Proteins; Myofibrils; Protein Kinases; Rabbits

1998
[Demonstration of secondary free radicals and the role of calpain in functional changes associated with the myocardial ischemia-reperfusion sequence].
    Archives des maladies du coeur et des vaisseaux, 2000, Volume: 93, Issue:8

    Topics: Animals; Antioxidants; Calcium-Binding Proteins; Calpain; Catalase; Cathepsins; Cyclic N-Oxides; Cysteine Proteinase Inhibitors; Electron Spin Resonance Spectroscopy; Free Radical Scavengers; Free Radicals; Hydroxyl Radical; Leupeptins; Magnetic Resonance Spectroscopy; Male; Myocardial Contraction; Myocardial Ischemia; Myocardial Reperfusion Injury; Nitrogen Oxides; Oxidative Stress; Phycocyanin; Rats; Rats, Wistar; Spin Labels; Superoxides; Time Factors

2000
Opening of ligand-gated cation channel families by calpain inhibitors.
    FEBS letters, 2002, Apr-24, Volume: 517, Issue:1-3

    Topics: Amino Acid Sequence; Animals; Calcium; Calcium Channels; Calcium-Binding Proteins; Calpain; Cell Membrane Permeability; CHO Cells; Cloning, Molecular; Cricetinae; Cysteine Proteinase Inhibitors; Electrophysiology; Ion Channel Gating; Leupeptins; Ligands; Membrane Proteins; Molecular Sequence Data; Patch-Clamp Techniques; Receptors, Drug; Transfection; TRPP Cation Channels

2002
Calpain-mediated AQP2 proteolysis in inner medullary collecting duct.
    Biochemical and biophysical research communications, 2003, Mar-28, Volume: 303, Issue:1

    Topics: Animals; Aquaporin 2; Aquaporin 6; Aquaporins; Calcium; Calcium-Binding Proteins; Calpain; Caseins; Cysteine Proteinase Inhibitors; Dextrans; Dihydrotachysterol; Dose-Response Relationship, Drug; Down-Regulation; Endosomes; Flow Cytometry; Immunoblotting; Immunohistochemistry; Kidney Tubules, Collecting; Leupeptins; Male; Protein Binding; Rats; Rats, Sprague-Dawley; Trypsin

2003
The calpain-calpastatin system and the calcium paradox in the isolated perfused pigeon heart.
    Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 2003, Volume: 13, Issue:3

    Topics: Animals; Antipain; Barium; Calcium; Calcium-Binding Proteins; Calpain; Cobalt; Columbidae; Dose-Response Relationship, Drug; Enzyme Inhibitors; Ethylmaleimide; Heart; In Vitro Techniques; Kinetics; Leucine; Leupeptins; Magnesium; Manganese; Molecular Weight; Myocardium; Nickel; Phenylmethylsulfonyl Fluoride; Strontium; Time Factors

2003
Myoblast migration is regulated by calpain through its involvement in cell attachment and cytoskeletal organization.
    Experimental cell research, 2004, Jan-01, Volume: 292, Issue:1

    Topics: Animals; Calcium-Binding Proteins; Calpain; Cell Adhesion; Cell Fusion; Cell Line; Cell Movement; Clone Cells; Cysteine Proteinase Inhibitors; Cytoskeleton; Dipeptides; Dose-Response Relationship, Drug; Glucosidases; Intracellular Signaling Peptides and Proteins; Leupeptins; Membrane Proteins; Mice; Muscle Fibers, Skeletal; Myoblasts; Myristoylated Alanine-Rich C Kinase Substrate; Oligopeptides; Phosphoproteins; Stress Fibers

2004
Leupeptin-based inhibitors do not improve the mdx phenotype.
    American journal of physiology. Regulatory, integrative and comparative physiology, 2010, Volume: 299, Issue:5

    Topics: Animals; Biomarkers; Calcium-Binding Proteins; Calpain; Creatine Kinase; Cysteine Proteinase Inhibitors; Diaphragm; Disease Models, Animal; Dose-Response Relationship, Drug; Genotype; Leupeptins; Mice; Mice, Inbred mdx; Muscle Contraction; Muscle Strength; Muscular Dystrophy, Duchenne; Necrosis; Phenotype; Proteasome Endopeptidase Complex; Time Factors

2010
Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide.
    The Journal of biological chemistry, 2018, 11-16, Volume: 293, Issue:46

    Topics: Calcium; Calcium-Binding Proteins; Calpain; Cysteine Proteinase Inhibitors; DNA Transposable Elements; Isoenzymes; Leucine; Leupeptins; Muscle Proteins; Protein Conformation; Proteolysis; Recombinant Proteins

2018