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Calpain research for drug discovery: challenges and potential

Nature reviews. Drug discovery, 2016-12, Vol.15 (12), p.854-876

2016

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Calpain chronicle—an enzyme family under multidisciplinary characterization

Proceedings of the Japan Academy, Series B, 2011/06/10, Vol.87(6), pp.287-327

2011

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Impact of genetic insights into calpain biology

Journal of biochemistry (Tokyo), 2011-07, Vol.150 (1), p.23-37

2011

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Collaboration between a cis-interacting natural killer cell receptor and membrane sphingolipid is critical for the phagocyte function

Frontiers in immunology, 2024-04, Vol.15, p.1401294-1401294

2024

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The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3

Nature communications, 2022-12, Vol.13 (1), p.7857-7857, Article 7857

2022

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Structure, Activation, and Biology of Calpain

Diabetes (New York, N.Y.), 2004-02, Vol.53 (suppl 1), p.S12-S18

2004

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Understanding the substrate specificity of conventional calpains

Biological chemistry, 2012-09, Vol.393 (9), p.853-871

2012

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Calpain cleavage prediction using multiple kernel learning

PloS one, 2011-05, Vol.6 (5), p.e19035

2011

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Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

The Journal of clinical investigation, 2010-08, Vol.120 (8), p.2672-2683

2010

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Calpains — An elaborate proteolytic system

Biochimica et biophysica acta, 2012-01, Vol.1824 (1), p.224-236

2012

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A Gastrointestinal Calpain Complex, G-calpain, Is a Heterodimer of CAPN8 and CAPN9 Calpain Isoforms, Which Play Catalytic and Regulatory Roles, Respectively

The Journal of biological chemistry, 2016-12, Vol.291 (53), p.27313-27322

2016

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Calpain-6 confers atherogenicity to macrophages by dysregulating pre-mRNA splicing

The Journal of clinical investigation, 2016-09, Vol.126 (9), p.3417-3432

2016

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Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense

PLoS genetics, 2010-07, Vol.6 (7), p.e1001040

2010

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Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles

Journal of molecular biology, 2011-04, Vol.407 (3), p.439-449

2011

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Predictions of Cleavability of Calpain Proteolysis by Quantitative Structure-Activity Relationship Analysis Using Newly Determined Cleavage Sites and Catalytic Efficiencies of an Oligopeptide Array

Molecular & cellular proteomics, 2016-04, Vol.15 (4), p.1262-1280

2016

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The Structure of Calpain

Journal of biochemistry (Tokyo), 2001-05, Vol.129 (5), p.653-664

2001

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Calpain-6 deficiency promotes skeletal muscle development and regeneration

PLoS genetics, 2013-08, Vol.9 (8), p.e1003668

2013

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The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation

Proceedings of the National Academy of Sciences - PNAS, 2014-12, Vol.111 (51), p.18110-18110

2014

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Structure and physiological function of calpains

Biochemical journal, 1997-12, Vol.328 ( Pt 3) (3), p.721-732

1997

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Involvement of calpain‐7 in epidermal growth factor receptor degradation via the endosomal sorting pathway

The FEBS journal, 2014-08, Vol.281 (16), p.3642-3655

2014

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Constitutive Activation of the pH-Responsive Rim101 Pathway in Yeast Mutants Defective in Late Steps of the MVB/ESCRT Pathway

Molecular and Cellular Biology, 2005-11, Vol.25 (21), p.9478-9490

2005

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Multiple Molecular Interactions Implicate the Connectin/Titin N2A Region as a Modulating Scaffold for p94/Calpain 3 Activity in Skeletal Muscle

The Journal of biological chemistry, 2008-05, Vol.283 (21), p.14801-14814

2008

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Removal of immunoglobulin-like domains from titin's spring segment alters titin splicing in mouse skeletal muscle and causes myopathy

The Journal of general physiology, 2014-02, Vol.143 (2), p.215-230

2014

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Nutrient-dependent Multimerization of the Mammalian Target of Rapamycin through the N-terminal HEAT Repeat Region

The Journal of biological chemistry, 2006-09, Vol.281 (39), p.28605-28614

2006

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Muscle‐specific calpain‐3 is phosphorylated in its unique insertion region for enrichment in a myofibril fraction

Genes to cells : devoted to molecular & cellular mechanisms, 2014-11, Vol.19 (11), p.830-841

2014

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Calpain research for drug discovery: challenges and potential

Calpain chronicle—an enzyme family under multidisciplinary characterization

Impact of genetic insights into calpain biology

Collaboration between a cis-interacting natural killer cell receptor and membrane sphingolipid is critical for the phagocyte function

The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3

Structure, Activation, and Biology of Calpain

Understanding the substrate specificity of conventional calpains

Calpain cleavage prediction using multiple kernel learning

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

Calpains — An elaborate proteolytic system

A Gastrointestinal Calpain Complex, G-calpain, Is a Heterodimer of CAPN8 and CAPN9 Calpain Isoforms, Which Play Catalytic and Regulatory Roles, Respectively

Calpain-6 confers atherogenicity to macrophages by dysregulating pre-mRNA splicing

Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense

Non-Proteolytic Functions of Calpain-3 in Sarcoplasmic Reticulum in Skeletal Muscles

Predictions of Cleavability of Calpain Proteolysis by Quantitative Structure-Activity Relationship Analysis Using Newly Determined Cleavage Sites and Catalytic Efficiencies of an Oligopeptide Array

The Structure of Calpain

Calpain-6 deficiency promotes skeletal muscle development and regeneration

The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation

Structure and physiological function of calpains

Involvement of calpain‐7 in epidermal growth factor receptor degradation via the endosomal sorting pathway

Constitutive Activation of the pH-Responsive Rim101 Pathway in Yeast Mutants Defective in Late Steps of the MVB/ESCRT Pathway

Multiple Molecular Interactions Implicate the Connectin/Titin N2A Region as a Modulating Scaffold for p94/Calpain 3 Activity in Skeletal Muscle

Removal of immunoglobulin-like domains from titin's spring segment alters titin splicing in mouse skeletal muscle and causes myopathy

Nutrient-dependent Multimerization of the Mammalian Target of Rapamycin through the N-terminal HEAT Repeat Region

Muscle‐specific calpain‐3 is phosphorylated in its unique insertion region for enrichment in a myofibril fraction

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