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Calpastatin Exon 1B-Derived Peptide, a Selective Inhibitor of Calpain: Enhancing Cell Permeability by Conjugation with Penetratin

https://doi.org/10.1515/bc.2003.045

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-4652(199903)178:3<311::aid-jcp5>3.0.co;2-topenalex-snapshot

Calpain and calpastatin regulate neutrophil apoptosis

inferredcites →https://doi.org/10.1006/bbrc.1997.6809openalex-snapshot

Cytoplasmic Processing of Human Profilaggrin by Active μ-Calpain

inferredcites →https://doi.org/10.1006/bbrc.2001.6197openalex-snapshot

Regulation of Transformed State by Calpastatin via PKCϵ in NIH3T3 Mouse Fibroblasts

inferredcites →https://doi.org/10.1016/0006-291x(90)91035-qopenalex-snapshot

Characterization of a functional domain of human calpastatin

inferredcites →https://doi.org/10.1016/0014-5793(95)00219-yopenalex-snapshot

Preference of calcium‐dependent interactions between calmodulin‐like domains of calpain and calpastatin subdomains

inferredcites →https://doi.org/10.1016/0014-5793(96)00752-1openalex-snapshot

Cyclodextrins as templates for the presentation of protease inhibitors

inferredcites →https://doi.org/10.1016/0968-0004(82)90157-8openalex-snapshot

The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions

inferredcites →https://doi.org/10.1016/s0005-2736(01)00398-4openalex-snapshot

Cargo delivery kinetics of cell-penetrating peptides

inferredcites →https://doi.org/10.1016/s0021-9258(19)47235-9openalex-snapshot

Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene

inferredcites →https://doi.org/10.1016/s0021-9258(19)81507-7openalex-snapshot

Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli.

inferredcites →https://doi.org/10.1016/s0028-3908(02)00010-2openalex-snapshot

An α-mercaptoacrylic acid derivative (PD150606) inhibits selective motor neuron death via inhibition of kainate-induced Ca2+ influx and not via calpain inhibition

inferredcites →https://doi.org/10.1016/s0092-8674(02)00659-1openalex-snapshot

A Ca2+ Switch Aligns the Active Site of Calpain

inferredcites →https://doi.org/10.1016/s0165-6147(00)01447-4openalex-snapshot

Cell-penetrating peptides

inferredcites →https://doi.org/10.1016/s0166-2236(99)01479-4openalex-snapshot

Calpain and caspase: can you tell the difference?

inferredcites →https://doi.org/10.1016/s0167-4889(02)00193-3openalex-snapshot

Participation of the conventional calpains in apoptosis

inferredcites →https://doi.org/10.1016/s0301-0082(00)00006-xopenalex-snapshot

Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates

inferredcites →https://doi.org/10.1016/s0962-8924(01)02179-1openalex-snapshot

Cutting to the chase: calpain proteases in cell motility

inferredcites →https://doi.org/10.1016/s0962-8924(97)01214-2openalex-snapshot

Trojan peptides: the penetratin system for intracellular delivery

inferredcites →https://doi.org/10.1016/s0962-8924(98)80017-2openalex-snapshot

Trojan peptides: the penetratin system for intracellular delivery

inferredcites →https://doi.org/10.1016/s1054-3589(08)60949-7openalex-snapshot

Development and Therapeutic Potential of Calpain Inhibitors

inferredcites →https://doi.org/10.1016/s1367-5931(02)00345-9openalex-snapshot

Recent advances in the synthesis, design and selection of cysteine protease inhibitors

inferredcites →https://doi.org/10.1016/s1471-4914(01)02049-4openalex-snapshot

The calpain family and human disease

inferredcites →https://doi.org/10.1021/bc0155115openalex-snapshot

Cellular Delivery of Impermeable Effector Molecules in the Form of Conjugates with Peptides Capable of Mediating Membrane Translocation

inferredcites →https://doi.org/10.1021/bc990156sopenalex-snapshot

Translocation Properties of Novel Cell Penetrating Transportan and Penetratin Analogues

inferredcites →https://doi.org/10.1021/bi00249a008openalex-snapshot

Domain structure of calpain: mapping the binding site for calpastatin

inferredcites →https://doi.org/10.1021/bi952262xopenalex-snapshot

Kinetic Characterization of the Chymotryptic Activity of the 20S Proteasome

inferredcites →https://doi.org/10.1021/bi970209yopenalex-snapshot

Specific Increase in Amyloid β-Protein 42 Secretion Ratio by Calpain Inhibition

inferredcites →https://doi.org/10.1038/sj.bjp.0703960openalex-snapshot

Heterogeneous increases of cytoplasmic calcium: distinct effects on down‐regulation of cell surface sodium channels and sodium channel subunit mRNA levels

inferredcites →https://doi.org/10.1046/j.1365-2613.2000.00169.xopenalex-snapshot

The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states

inferredcites →https://doi.org/10.1073/pnas.93.13.6687openalex-snapshot

An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective.

inferredcites →https://doi.org/10.1074/jbc.270.42.25115openalex-snapshot

The Role of the Calpain-Calpastatin System in Thyrotropin-releasing Hormone-induced Selective Down-regulation of a Protein Kinase C Isozyme, nPKCε, in Rat Pituitary GH4C1 Cells

inferredcites →https://doi.org/10.1074/jbc.274.20.14359openalex-snapshot

Evidence for a Calpeptin-sensitive Protein-tyrosine Phosphatase Upstream of the Small GTPase Rho

inferredcites →https://doi.org/10.1074/jbc.274.51.36321openalex-snapshot

Inhibition of Calpain Blocks Platelet Secretion, Aggregation, and Spreading

inferredcites →https://doi.org/10.1074/jbc.m007807200openalex-snapshot

Synergistic Activation of Caspase-3 by m-Calpain after Neonatal Hypoxia-Ischemia

inferredcites →https://doi.org/10.1074/jbc.m112037200openalex-snapshot

DNA Ligase III Is Degraded by Calpain during Cell Death Induced by DNA-damaging Agents

inferredcites →https://doi.org/10.1074/jbc.m202945200openalex-snapshot

Ionomycin-activated Calpain Triggers Apoptosis

inferredcites →https://doi.org/10.1074/jbc.m204951200openalex-snapshot

Calpain and Mitochondria in Ischemia/Reperfusion Injury

inferredcites →https://doi.org/10.1074/jbc.m907757199openalex-snapshot

Calpain-dependent Proteolytic Cleavage of the p35 Cyclin-dependent Kinase 5 Activator to p25

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a002903openalex-snapshot

The Structure of Calpain

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a122844openalex-snapshot

Identification and Characterization of Inhibitory Sequences in Four Repeating Domains of the Endogenous Inhibitor for Calcium-Dependent Protease1

inferredcites →https://doi.org/10.1111/j.1399-3011.1986.tb03236.xopenalex-snapshot

Preparation of Boc‐[S‐(3‐nitro‐2‐pyridinesulfenyl)]‐cysteine and its use for unsymmetrical disulfide bond formation

inferredcites →https://doi.org/10.1111/j.1432-0436.1988.tb00806.xopenalex-snapshot

Characterization of the state of differentiation of six newly established human non-small-cell lung cancer cell lines

inferredcites →https://doi.org/10.1128/mcb.20.12.4474-4481.2000openalex-snapshot

Disruption of the Murine Calpain Small Subunit Gene, Capn4 : Calpain Is Essential for Embryonic Development but Not for Cell Growth and Division

inferredcites →https://doi.org/10.1128/mcb.22.1.257-269.2002openalex-snapshot

v-Src-Induced Modulation of the Calpain-Calpastatin Proteolytic System Regulates Transformation

inferredcites →https://doi.org/10.1182/blood.v89.6.2060openalex-snapshot

Phosphatidylserine Externalization Is a Downstream Event of Interleukin-1β–Converting Enzyme Family Protease Activation During Apoptosis

inferredcites →https://doi.org/10.1515/bc.2001.090openalex-snapshot

Calpain Function in the Modulation of Signal Transduction Molecules

inferredcites →https://doi.org/10.1515/bc.2001.209openalex-snapshot

Human -Calpain: Simple Isolation from Erythrocytes and Characterization of Autolysis Fragments

inferredcites →https://doi.org/10.1515/bc.2002.031openalex-snapshot

Intracellular Concentration Measurements in Adherent Cells: A Comparison of Import Efficiencies of Cell-Permeable Peptides

inferredcites →https://doi.org/10.1515/bc.2002.079openalex-snapshot

Calpain Function in the Differentiation of Mesenchymal Stem Cells

inferredcites →https://doi.org/10.1515/bc.2002.090openalex-snapshot

Epoxysuccinyl Peptide-Derived Cathepsin B Inhibitors: Modulating Membrane Permeability by Conjugation with the C-Terminal Heptapeptide Segment of Penetratin

inferredcites →https://doi.org/10.2174/0929867003374129openalex-snapshot

A Survey of Calpain Inhibitors

inferredcites →https://doi.org/10.3109/14756369009035837openalex-snapshot

Inhibitory Effect of di- and Tripeptidyl Aldehydes on Calpains and Cathepsins

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4757046openalex-extracted

Role of CAPN5 in Tumor Immune Microenvironment Based on Multi-Omics: From BLCA Molecular Subtypes to Therapeutic Prediction

inferred← citeshttps://doi.org/10.1002/psc.678openalex-snapshot

Investigation of penetratin peptides. Part 2.In vitro uptake of penetratin and two of its derivatives

inferred← citeshttps://doi.org/10.1002/psc.790openalex-snapshot

A new cell‐permeable calpain inhibitor

inferred← citeshttps://doi.org/10.1007/s00018-004-4445-9openalex-snapshot

Proteinaceous cysteine protease inhibitors

inferred← citeshttps://doi.org/10.1016/j.apsb.2015.08.001openalex-snapshot

Cysteine proteases as therapeutic targets: does selectivity matter? A systematic review of calpain and cathepsin inhibitors

inferred← citeshttps://doi.org/10.1016/j.bbrc.2009.04.141openalex-snapshot

A novel calpastatin-based inhibitor improves postischemic neurological recovery

inferred← citeshttps://doi.org/10.1016/j.bmcl.2005.12.036openalex-snapshot

Novel dual inhibitors of calpain and lipid peroxidation with enhanced cellular activity

inferred← citeshttps://doi.org/10.1016/j.expneurol.2004.03.018openalex-snapshot

Tat-calpastatin fusion proteins transduce primary rat cortical neurons but do not inhibit cellular calpain activity

inferred← citeshttps://doi.org/10.1016/j.mcn.2004.03.005openalex-snapshot

Delivery of bioactive molecules into the cell: the Trojan horse approach

inferred← citeshttps://doi.org/10.1016/j.peptides.2004.09.006openalex-snapshot

Synthesis and evaluation of eight-membered cyclic pseudo-dipeptides

inferred← citeshttps://doi.org/10.1016/j.pneurobio.2016.06.001openalex-snapshot

Calpains and neuronal damage in the ischemic brain: The swiss knife in synaptic injury

inferred← citeshttps://doi.org/10.1021/bc0601976openalex-snapshot

Synthesis of Cell-Penetrating Conjugates of Calpain Activator Peptides

inferred← citeshttps://doi.org/10.1021/bi047590oopenalex-snapshot

Inhibition of a Cathepsin L-Like Cysteine Protease by a Chimeric Propeptide-Derived Inhibitor

inferred← citeshttps://doi.org/10.1021/ja307599zopenalex-snapshot

Development of α-Helical Calpain Probes by Mimicking a Natural Protein–Protein Interaction

inferred← citeshttps://doi.org/10.1038/cdd.2008.125openalex-snapshot

Role of Smac in cephalostatin-induced cell death

inferred← citeshttps://doi.org/10.1038/s41598-024-65537-9openalex-snapshot

Cathepsins L and B target HIF1α for oxygen-independent proteolytic cleavage

inferred← citeshttps://doi.org/10.1074/jbc.m608803200openalex-snapshot

A Mouse Model for Monitoring Calpain Activity under Physiological and Pathological Conditions

inferred← citeshttps://doi.org/10.1080/14728222.2022.2047178openalex-snapshot

Calpain as a therapeutic target in cancer

inferred← citeshttps://doi.org/10.1080/17460441.2020.1722638openalex-snapshot

Modulators of calpain activity: inhibitors and activators as potential drugs

inferred← citeshttps://doi.org/10.1111/j.1471-4159.2005.03122.xopenalex-snapshot

The critical role of calpain versus caspase activation in excitotoxic injury induced by nitric oxide

inferred← citeshttps://doi.org/10.1111/j.1755-5922.2010.00245.xopenalex-snapshot

Physiologic and Pathophysiologic Role of Calpain: Implications for the Occurrence of Atrial Fibrillation

inferred← citeshttps://doi.org/10.1126/science.1171085openalex-snapshot

Apicomplexan Parasites Co-Opt Host Calpains to Facilitate Their Escape from Infected Cells

inferred← citeshttps://doi.org/10.1152/ajpheart.00772.2004openalex-snapshot

Calpains: a physiological regulator of the endothelial barrier?

inferred← citeshttps://doi.org/10.1515/bc.2003.107openalex-snapshot

The Calpastatin-Derived Calpain Inhibitor CP1B Reduces mRNA Expression of Matrix Metalloproteinase-2 and -9 and Invasion by Leukemic THP-1 Cells

inferred← citeshttps://doi.org/10.1515/bc.2008.004openalex-snapshot

Inhibition of human μ-calpain by conformationally constrained calpastatin peptides

inferred← citeshttps://doi.org/10.1517/13543776.2011.568480openalex-snapshot

Calpain inhibitors: a survey of compounds reported in the patent and scientific literature

inferred← citeshttps://doi.org/10.2174/138161208785777432openalex-snapshot

Cell Penetrating Peptides for In Vivo Molecular Imaging Applications

inferred← citeshttps://doi.org/10.5282/edoc.6586openalex-snapshot

Role of Bid and AIF in Glutamate-induced Neuronal Cell Death

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