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Calpain–calpastatin system and cancer progression
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inferredcites →https://doi.org/10.1002/(sici)1097-0215(19990219)84:1<6::aid-ijc2>3.0.co;2-topenalex-snapshot
Expression of calpain I messenger RNA in human renal cell carcinoma: Correlation with lymph node metastasis and histological type
inferredcites →https://doi.org/10.1002/1097-4644(20010101)80:1<53::aid-jcb60>3.0.co;2-eopenalex-snapshot
N-terminal cleavage of Bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes Bcl-2-independent cytochrome C release and apoptotic cell death
inferredcites →https://doi.org/10.1002/cam4.1260openalex-snapshot
Calpain‐2 inhibitor treatment preferentially reduces tumor progression for human colon cancer cells expressing highest levels of this enzyme
inferredcites →https://doi.org/10.1002/cbin.10062openalex-snapshot
Calpains are required for invasive and metastatic potentials of human HCC cells
inferredcites →https://doi.org/10.1002/hep.22638openalex-snapshot
Capn4 overexpression underlies tumor invasion and metastasis after liver transplantation for hepatocellular carcinoma: [RETRACTED] #
inferredcites →https://doi.org/10.1002/hep.23169openalex-snapshot
Calpain activation by hepatitis C virus proteins inhibits the extrinsic apoptotic signaling pathway #
inferredcites →https://doi.org/10.1002/ijc.23378openalex-snapshot
Calpain‐mediated pathway dominates cisplatin‐induced apoptosis in human lung adenocarcinoma cells as determined by real‐time single cell analysis
inferredcites →https://doi.org/10.1002/jcp.21565openalex-snapshot
Calpain‐mediated androgen receptor breakdown in apoptotic prostate cancer cells
inferredcites →https://doi.org/10.1002/jcp.22516openalex-snapshot
Calmodulin protects androgen receptor from calpain-mediated breakdown in prostate cancer cells
inferredcites →https://doi.org/10.1002/mrd.20466openalex-snapshot
Calpain 11 is unique to mouse spermatogenic cells
inferredcites →https://doi.org/10.1002/mus.24682openalex-snapshot
Protein and genetic diagnosis of limb girdle muscular dystrophy type 2A: The yield and the pitfalls
inferredcites →https://doi.org/10.1002/path.4395openalex-snapshot
Capn4 contributes to tumour growth and metastasis of hepatocellular carcinoma by activation of the FAK –Src signalling pathways
inferredcites →https://doi.org/10.1002/psc.1131openalex-snapshot
Folding transitions in calpain activator peptides studied by solution NMR spectroscopy
inferredcites →https://doi.org/10.1006/bbrc.1997.7003openalex-snapshot
Evidence for Participation of a Calpain-like Cysteine Protease in Cell Cycle Progression through Late G1Phase
inferredcites →https://doi.org/10.1006/bbrc.2001.4279openalex-snapshot
Domain III of Calpain Is a Ca2+-Regulated Phospholipid-Binding Domain
inferredcites →https://doi.org/10.1006/excr.1998.4021openalex-snapshot
Myristoyl-CoA:ProteinN-Myristoyltransferase from Bovine Cardiac Muscle: Molecular Cloning, Kinetic Analysis, andin VitroProteolytic Cleavage bym-Calpain
inferredcites →https://doi.org/10.1007/s00223-011-9491-3openalex-snapshot
Calpain Modulates Cyclin-Dependent Kinase Inhibitor 1B (p27Kip1) in Cells of the Osteoblast Lineage
inferredcites →https://doi.org/10.1007/s10495-010-0526-4openalex-snapshot
Calpain and caspase processing of caspase-12 contribute to the ER stress-induced cell death pathway in differentiated PC12 cells
inferredcites →https://doi.org/10.1007/s11033-014-3540-8openalex-snapshot
Common polymorphisms of calpain-10 and the risk of polycystic ovary syndrome in Tunisian population: a case–control study
inferredcites →https://doi.org/10.1007/s12029-010-9130-7openalex-snapshot
Association of Diabetes Susceptibility Gene Calpain-10 with Pancreatic Cancer Among Smokers
inferredcites →https://doi.org/10.1007/s12032-015-0500-7openalex-snapshot
Capn4 promotes non-small cell lung cancer progression via upregulation of matrix metalloproteinase 2
inferredcites →https://doi.org/10.1016/0092-8674(95)90368-2openalex-snapshot
Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
inferredcites →https://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
inferredcites →https://doi.org/10.1016/j.arcmed.2014.01.005openalex-snapshot
Role of Calpain-10 in the Development of Diabetes Mellitus and Its Complications
inferredcites →https://doi.org/10.1016/j.arr.2016.05.008openalex-snapshot
Can ‘calpain-cathepsin hypothesis’ explain Alzheimer neuronal death?
inferredcites →https://doi.org/10.1016/j.bbapap.2011.08.005openalex-snapshot
Calpains — An elaborate proteolytic system
inferredcites →https://doi.org/10.1016/j.bbrc.2006.07.052openalex-snapshot
A region of calpastatin domain L that reprimes cardiac L-type Ca2+ channels
inferredcites →https://doi.org/10.1016/j.bcp.2003.12.021openalex-snapshot
Calpain as a multi-site regulator of cell cycle
inferredcites →https://doi.org/10.1016/j.bcp.2006.11.027openalex-snapshot
Genistein induces apoptosis in human hepatocellular carcinomas via interaction of endoplasmic reticulum stress and mitochondrial insult
inferredcites →https://doi.org/10.1016/j.biocel.2004.12.012openalex-snapshot
Calpains in muscle wasting
inferredcites →https://doi.org/10.1016/j.biopha.2015.08.008openalex-snapshot
Role of the calpain on the development of diabetes mellitus and its chronic complications
inferredcites →https://doi.org/10.1016/j.canlet.2013.01.029openalex-snapshot
The oncoprotein HBXIP up-regulates Skp2 via activating transcription factor E2F1 to promote proliferation of breast cancer cells
inferredcites →https://doi.org/10.1016/j.canlet.2014.09.047openalex-snapshot
The oncoprotein HBXIP enhances migration of breast cancer cells through increasing filopodia formation involving MEKK2/ERK1/2/Capn4 signaling
inferredcites →https://doi.org/10.1016/j.dnarep.2008.01.003openalex-snapshot
OGG1 is degraded by calpain following oxidative stress and cisplatin exposure
inferredcites →https://doi.org/10.1016/j.ejmech.2018.08.049openalex-snapshot
Structure-based design of allosteric calpain-1 inhibitors populating a novel bioactivity space
inferredcites →https://doi.org/10.1016/j.febslet.2006.02.076openalex-snapshot
N‐Myristoyltransferase 2 expression in human colon cancer: Cross‐talk between the calpain and caspase system
inferredcites →https://doi.org/10.1016/j.febslet.2007.05.035openalex-snapshot
Calpastatin simultaneously binds four calpains with different kinetic constants
inferredcites →https://doi.org/10.1016/j.jid.2016.07.043openalex-snapshot
Calpain 12 Function Revealed through the Study of an Atypical Case of Autosomal Recessive Congenital Ichthyosis
inferredcites →https://doi.org/10.1016/j.jmb.2006.11.037openalex-snapshot
The Crystal Structures of Human Calpains 1 and 9 Imply Diverse Mechanisms of Action and Auto-inhibition
inferredcites →https://doi.org/10.1016/j.molmed.2003.12.007openalex-snapshot
Calpains: targets of cataract prevention?
inferredcites →https://doi.org/10.1016/j.pathophys.2014.01.003openalex-snapshot
The calpain system and diabetes
inferredcites →https://doi.org/10.1016/s0014-5793(01)02611-4openalex-snapshot
Domain II of m‐calpain is a Ca2+‐dependent cysteine protease
inferredcites →https://doi.org/10.1016/s0014-5793(03)00361-2openalex-snapshot
Glutamate substitutions at a PKA consensus site are consistent with inactivation of calpain by phosphorylation
inferredcites →https://doi.org/10.1016/s0014-5793(97)00225-1openalex-snapshot
On the involvement of calpains in the degradation of the tumor suppressor protein p53
inferredcites →https://doi.org/10.1016/s0014-5793(98)00856-4openalex-snapshot
A novel aspect of calpain activation
inferredcites →https://doi.org/10.1016/s0021-9258(18)51762-2openalex-snapshot
A Neutral, Calcium-activated Proteinase from the Soluble Fraction of Rat Brain
inferredcites →https://doi.org/10.1016/s0021-9258(19)84966-9openalex-snapshot
Limited Proteolysis of Protein Kinase C Subspecies by Calcium-dependent Neutral Protease (Calpain)
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/s0167-5699(96)30064-9openalex-snapshot
The calpain-calpastatin system in rheumatoid arthritis
inferredcites →https://doi.org/10.1016/s0304-3835(02)00552-9openalex-snapshot
Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax
inferredcites →https://doi.org/10.1016/s0304-4157(98)00003-3openalex-snapshot
Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules
inferredcites →https://doi.org/10.1016/s0925-4773(99)00214-2openalex-snapshot
Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development
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/s0969-2126(02)00932-2openalex-snapshot
Metal-Free and Ca2+-Bound Structures of a Multidomain EF-Hand Protein, CBP40, from the Lower Eukaryote Physarum polycephalum
inferredcites →https://doi.org/10.1021/bi800201aopenalex-snapshot
Local Structural Preferences of Calpastatin, the Intrinsically Unstructured Protein Inhibitor of Calpain
inferredcites →https://doi.org/10.1038/342505a0openalex-snapshot
Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs
inferredcites →https://doi.org/10.1038/cddis.2011.29openalex-snapshot
Calpain-mediated cleavage of Beclin-1 and autophagy deregulation following retinal ischemic injury in vivo
inferredcites →https://doi.org/10.1038/nature07353openalex-snapshot
Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains
inferredcites →https://doi.org/10.1038/nature07451openalex-snapshot
Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin
inferredcites →https://doi.org/10.1038/ncb0402-e97openalex-snapshot
Adhesion assembly, disassembly and turnover in migrating cells – over and over and over again
inferredcites →https://doi.org/10.1038/ncb1868openalex-snapshot
Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration
inferredcites →https://doi.org/10.1038/nm0898-915openalex-snapshot
The involvement of calpain-independent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas
inferredcites →https://doi.org/10.1038/nrd.2016.212openalex-snapshot
Calpain research for drug discovery: challenges and potential
inferredcites →https://doi.org/10.1038/nsb0797-532openalex-snapshot
Structure of a calpain Ca2+-binding domain reveals a novel EF-hand and Ca2+-induced conformational changes
inferredcites →https://doi.org/10.1038/nsb917openalex-snapshot
Calpain silencing by a reversible intrinsic mechanism
inferredcites →https://doi.org/10.1038/onc.2008.425openalex-snapshot
Calpain small-1 modulates Akt/FoxO3A signaling and apoptosis through PP2A
inferredcites →https://doi.org/10.1038/sj.onc.1200841openalex-snapshot
Inhibition of the growth of WI-38 fibroblasts by benzyloxycarbonyl-Leu-Leu-Tyr diazomethyl ketone: evidence that cleavage of p53 by a calpain-like protease is necessary for G1 to S-phase transition
inferredcites →https://doi.org/10.1038/sj.onc.1204257openalex-snapshot
Her-2/neu overexpression induces NF-κB via a PI3-kinase/Akt pathway involving calpain-mediated degradation of IκB-α that can be inhibited by the tumor suppressor PTEN
inferredcites →https://doi.org/10.1042/bj2620693openalex-snapshot
Calmodulin-binding proteins as calpain substrates
inferredcites →https://doi.org/10.1042/bj3180897openalex-snapshot
Autolysis parallels activation of μ-calpain
inferredcites →https://doi.org/10.1042/bj3280721openalex-snapshot
Structure and physiological function of calpains
inferredcites →https://doi.org/10.1073/pnas.0307161101openalex-snapshot
Physical and functional interaction of androgen receptor with calmodulin in prostate cancer cells
inferredcites →https://doi.org/10.1073/pnas.84.11.3590openalex-snapshot
Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites.
inferredcites →https://doi.org/10.1073/pnas.84.8.2251openalex-snapshot
Activation of pp60c-src protein kinase activity in human colon carcinoma.
inferredcites →https://doi.org/10.1073/pnas.93.20.10815openalex-snapshot
p53-dependent cell cycle arrest induced by N-acetyl-L-leucinyl-L-leucinyl-L-norleucinal in platelet-derived growth factor-stimulated human fibroblasts.
inferredcites →https://doi.org/10.1073/pnas.97.2.588openalex-snapshot
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium
inferredcites →https://doi.org/10.1074/jbc.272.17.11268openalex-snapshot
Autolysis, Ca2+ Requirement, and Heterodimer Stability in m-Calpain
inferredcites →https://doi.org/10.1074/jbc.273.26.15879openalex-snapshot
C2-domains, Structure and Function of a Universal Ca2+-binding Domain
inferredcites →https://doi.org/10.1074/jbc.275.1.82openalex-snapshot
Acyl-CoA-binding Protein Is a Potent m-Calpain Activator
inferredcites →https://doi.org/10.1074/jbc.275.7.5131openalex-snapshot
Direct Cleavage by the Calcium-activated Protease Calpain Can Lead to Inactivation of Caspases
inferredcites →https://doi.org/10.1074/jbc.c100700200openalex-snapshot
Calpastatin Subdomains A and C Are Activators of Calpain
inferredcites →https://doi.org/10.1074/jbc.m007352200openalex-snapshot
Calpain Mutants with Increased Ca2+ Sensitivity and Implications for the Role of the C2-like Domain
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.m008847200openalex-snapshot
Membrane Proximal ERK Signaling Is Required for M-calpain Activation Downstream of Epidermal Growth Factor Receptor Signaling
inferredcites →https://doi.org/10.1074/jbc.m008972200openalex-snapshot
Cleavage of Focal Adhesion Kinase by Different Proteases during Src-regulated Transformation and Apoptosis
inferredcites →https://doi.org/10.1074/jbc.m109.038174openalex-snapshot
Calpain-1 Cleaves and Activates Caspase-7
inferredcites →https://doi.org/10.1074/jbc.m111.242248openalex-snapshot
Calpastatin Domain L Is a Partial Agonist of the Calmodulin-binding Site for Channel Activation in Cav1.2 Ca2+ Channels
inferredcites →https://doi.org/10.1074/jbc.m111689200openalex-snapshot
Calpain Inhibition Decreases the Growth Rate of Mammalian Cell Colonies
inferredcites →https://doi.org/10.1074/jbc.m202945200openalex-snapshot
Ionomycin-activated Calpain Triggers Apoptosis
inferredcites →https://doi.org/10.1074/jbc.m203457200openalex-snapshot
Calpain Cleaves RhoA Generating a Dominant-negative Form That Inhibits Integrin-induced Actin Filament Assembly and Cell Spreading
inferredcites →https://doi.org/10.1074/jbc.m204471200openalex-snapshot
Conformational Changes of Calpain from Human Erythrocytes in the Presence of Ca2+
inferredcites →https://doi.org/10.1074/jbc.m208772200openalex-snapshot
The Role of Calpain in the Proteolytic Cleavage of E-cadherin in Prostate and Mammary Epithelial Cells
inferredcites →https://doi.org/10.1074/jbc.m310460200openalex-snapshot
Calpain Activation by Cooperative Ca2+ Binding at Two Non-EF-hand Sites
inferredcites →https://doi.org/10.1074/jbc.m409889200openalex-snapshot
Tobacco-specific Nitrosamine 4-(Methylnitrosamino)-1-(3-pyridyl)-1-butanone Induces Phosphorylation of μ- and m-Calpain in Association with Increased Secretion, Cell Migration, and Invasion
inferredcites →https://doi.org/10.1074/jbc.m510721200openalex-snapshot
Protein Kinase Cι Promotes Nicotine-induced Migration and Invasion of Cancer Cells via Phosphorylation of μ- and m-Calpains
inferredcites →https://doi.org/10.1074/jbc.m601449200openalex-snapshot
Association of Calpastatin with Inactive Calpain
inferredcites →https://doi.org/10.1074/jbc.m601978200openalex-snapshot
Ubiquitous Calpains Promote Both Apoptosis and Survival Signals in Response to Different Cell Death Stimuli
inferredcites →https://doi.org/10.1074/jbc.m703168200openalex-snapshot
Stomach-specific Calpain, nCL-2/Calpain 8, Is Active without Calpain Regulatory Subunit and Oligomerizes through C2-like Domains
inferredcites →https://doi.org/10.1074/jbc.m706472200openalex-snapshot
Calmodulin Binds and Stabilizes the Regulatory Enzyme, CTP:Phosphocholine Cytidylyltransferase
inferredcites →https://doi.org/10.1074/jbc.m900561200openalex-snapshot
Calpain Expression and Activity during Lens Fiber Cell Differentiation
inferredcites →https://doi.org/10.1074/jbc.m910445199openalex-snapshot
Mitotic Clonal Expansion during Preadipocyte Differentiation: Calpain-mediated Turnover of p27
inferredcites →https://doi.org/10.1074/jbc.ra117.001097openalex-snapshot
Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation
inferredcites →https://doi.org/10.1083/jcb.200601024openalex-snapshot
Calpain is required for macroautophagy in mammalian cells
inferredcites →https://doi.org/10.1083/jcb.200708048openalex-snapshot
Calpain 2 and PTP1B function in a novel pathway with Src to regulate invadopodia dynamics and breast cancer cell invasion
inferredcites →https://doi.org/10.1091/mbc.e05-08-0770openalex-snapshot
Calpain Mediates a von Hippel-Lindau Protein–independent Destruction of Hypoxia-inducible Factor-1α
inferredcites →https://doi.org/10.1093/carcin/bgp098openalex-snapshot
Novel variants of muscle calpain 3 identified in human melanoma cells: cisplatin-induced changes in vitro and differential expression in melanocytic lesions
inferredcites →https://doi.org/10.1093/cvr/cvs157openalex-snapshot
Regulation and physiological roles of the calpain system in muscular disorders
inferredcites →https://doi.org/10.1093/emboj/18.18.4988openalex-snapshot
Implication of calpain in caspase activation during B cell clonal deletion
inferredcites →https://doi.org/10.1093/emboj/18.24.6880openalex-snapshot
Crystal structure of calpain reveals the structural basis for Ca2+‐dependent protease activity and a novel mode of enzyme activation
inferredcites →https://doi.org/10.1093/hmg/ddw086openalex-snapshot
Failure to up-regulate transcription of genes necessary for muscle adaptation underlies limb girdle muscular dystrophy 2A (calpainopathy)
inferredcites →https://doi.org/10.1093/humrep/dei443openalex-snapshot
Specific haplotypes of the CALPAIN-5 gene are associated with polycystic ovary syndrome
inferredcites →https://doi.org/10.1093/nar/gky427openalex-snapshot
SWISS-MODEL: homology modelling of protein structures and complexes
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a002903openalex-snapshot
The Structure of Calpain
inferredcites →https://doi.org/10.1110/ps.03138803openalex-snapshot
Binding‐induced folding transitions in calpastatin subdomains A and C
inferredcites →https://doi.org/10.1111/febs.12849openalex-snapshot
Crystal structure of calpain‐3 penta‐ EF ‐hand ( PEF ) domain – a homodimerized PEF family member with calcium bound at the fifth EF ‐hand
inferredcites →https://doi.org/10.1111/j.1349-7006.2000.tb00967.xopenalex-snapshot
Isolation of Two Novel Genes, Down‐regulated in Gastric Cancer
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb19013.xopenalex-snapshot
The calpain cleavage sites in the epidermal growth factor receptor kinase domain
inferredcites →https://doi.org/10.1111/j.1440-1746.2007.04843.xopenalex-snapshot
Identification of a protective haplogenotype withinCAPN10gene influencing colorectal cancer susceptibility
inferredcites →https://doi.org/10.1111/j.1525-1438.2006.00756.xopenalex-snapshot
Increased expression of calpain 6 in uterine sarcomas and carcinosarcomas: an immunohistochemical analysis
inferredcites →https://doi.org/10.1111/j.1742-4658.2006.05351.xopenalex-snapshot
Calpain 3: a key regulator of the sarcomere?
inferredcites →https://doi.org/10.1111/j.1753-4887.1981.tb06752.xopenalex-snapshot
Proceedings of the National Academy of Sciences of the United States of America
inferredcites →https://doi.org/10.1124/mol.107.039040openalex-snapshot
Mitochondria, Calcium, and Calpain are Key Mediators of Resveratrol-Induced Apoptosis in Breast Cancer
inferredcites →https://doi.org/10.1126/science.2834825openalex-snapshot
Calpain II Involvement in Mitosis
inferredcites →https://doi.org/10.1126/stke.114re1openalex-snapshot
Calpain in the CNS: From Synaptic Function to Neurotoxicity
inferredcites →https://doi.org/10.1128/jvi.03385-12openalex-snapshot
Prototype Foamy Virus Bet Impairs the Dimerization and Cytosolic Solubility of Human APOBEC3G
inferredcites →https://doi.org/10.1128/mcb.01406-12openalex-snapshot
CAPNS1 Regulates USP1 Stability and Maintenance of Genome Integrity
inferredcites →https://doi.org/10.1128/mcb.17.1.460openalex-snapshot
Proteolytic Cleavage of Human p53 by Calpain: a Potential Regulator of Protein Stability
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/10.1128/mcb.22.8.2716-2727.2002openalex-snapshot
Activation of m-Calpain (Calpain II) by Epidermal Growth Factor Is Limited by Protein Kinase A Phosphorylation of m-Calpain
inferredcites →https://doi.org/10.1128/mcb.24.6.2499-2512.2004openalex-snapshot
Epidermal Growth Factor Activates m-Calpain (Calpain II), at Least in Part, by Extracellular Signal-Regulated Kinase-Mediated Phosphorylation
inferredcites →https://doi.org/10.1146/annurev.biochem.67.1.425openalex-snapshot
THE UBIQUITIN SYSTEM
inferredcites →https://doi.org/10.11501/3148188openalex-snapshot
The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas
inferredcites →https://doi.org/10.1152/ajpheart.00849.2009openalex-snapshot
Cardioprotective effects of a novel calpain inhibitor SNJ-1945 for reperfusion injury after cardioplegic cardiac arrest
inferredcites →https://doi.org/10.1158/1055-9965.1604.13.10openalex-snapshot
Overexpression of m-Calpain in Human Colorectal Adenocarcinomas
inferredcites →https://doi.org/10.1158/1078-0432.ccr-08-1402openalex-snapshot
Nuclear versus Cytoplasmic Localization of Filamin A in Prostate Cancer: Immunohistochemical Correlation with Metastases
inferredcites →https://doi.org/10.1159/000430464openalex-snapshot
Calpain in Breast Cancer: Role in Disease Progression and Treatment Response
inferredcites →https://doi.org/10.1161/01.res.72.2.413openalex-snapshot
Effects of thiol protease inhibitors on cell cycle and proliferation of vascular smooth muscle cells in culture.
inferredcites →https://doi.org/10.1161/atvbaha.116.307285openalex-snapshot
Leukocyte Calpain Deficiency Reduces Angiotensin II–Induced Inflammation and Atherosclerosis But Not Abdominal Aortic Aneurysms in Mice
inferredcites →https://doi.org/10.1161/circulationaha.113.001340openalex-snapshot
Restriction of Calpain3 Expression to the Skeletal Muscle Prevents Cardiac Toxicity and Corrects Pathology in a Murine Model of Limb-Girdle Muscular Dystrophy
inferredcites →https://doi.org/10.1186/1471-2407-14-995openalex-snapshot
Low calpain-9 is associated with adverse disease-specific survival following endocrine therapy in breast cancer
inferredcites →https://doi.org/10.1186/s12943-019-1085-0openalex-snapshot
The significance of exosomes in the development and treatment of hepatocellular carcinoma
inferredcites →https://doi.org/10.1186/s12943-020-1138-4openalex-snapshot
Autophagy and autophagy-related proteins in cancer
inferredcites →https://doi.org/10.1242/bio.022806openalex-snapshot
Calpain mobilizes Atg9/Bif-1 vesicles from Golgi stacks upon autophagy induction by thapsigargin
inferredcites →https://doi.org/10.1242/jcs.02562openalex-snapshot
Regulating cell migration: calpains make the cut
inferredcites →https://doi.org/10.1371/journal.pgen.1001040openalex-snapshot
Calpain 8/nCL-2 and Calpain 9/nCL-4 Constitute an Active Protease Complex, G-Calpain, Involved in Gastric Mucosal Defense
inferredcites →https://doi.org/10.1371/journal.pone.0031458openalex-snapshot
Hepatitis B Virus X Protein Drives Multiple Cross-Talk Cascade Loops Involving NF-κB, 5-LOX, OPN and Capn4 to Promote Cell Migration
inferredcites →https://doi.org/10.1515/bc.2001.091openalex-snapshot
Structural Basis for Possible Calcium-Induced Activation Mechanisms of Calpains
inferredcites →https://doi.org/10.1515/bc.2004.054openalex-snapshot
Interaction of calpastatin with calpain: a review
inferredcites →https://doi.org/10.1515/bc.2008.004openalex-snapshot
Inhibition of human μ-calpain by conformationally constrained calpastatin peptides
inferredcites →https://doi.org/10.1517/14728222.2011.553611openalex-snapshot
Calpains as potential anti-cancer targets
inferredcites →https://doi.org/10.1523/jneurosci.4119-08.2008openalex-snapshot
Marked Calpastatin (CAST) Depletion in Alzheimer's Disease Accelerates Cytoskeleton Disruption and Neurodegeneration: Neuroprotection by CAST Overexpression
inferredcites →https://doi.org/10.18388/abp.2010_2369openalex-snapshot
Cloning and characterization of the yak gene coding for calpastatin and in silico analysis of its putative product.
inferredcites →https://doi.org/10.18632/oncotarget.8791openalex-snapshot
Calcium influx-mediated translocation ofm-calpain induces Ku80 cleavage and enhances the Ku80-related DNA repair pathway
inferredcites →https://doi.org/10.3858/emm.2009.41.11.102openalex-snapshot
The function of p27 KIP1 during tumor development
inferredcites →https://doi.org/10.3892/br.2016.785openalex-snapshot
Critical role of calpain in inflammation
inferredcites →https://doi.org/10.3892/ijmm.18.3.471openalex-snapshot
The gene expression and activity of calpains and the muscle wasting-associated ubiquitin ligases, atrogin-1 and MuRF1, are not altered in patients with primary hyperparathyroidism
inferredcites →https://doi.org/10.3892/ijo.2013.2196openalex-snapshot
Prolonged androgen deprivation leads to overexpression of calpain 2: Implications for prostate cancer progression
inferredcites →https://doi.org/10.3892/or.19.4.859openalex-snapshot
Increased expression of calpain 6 during the progression of uterine cervical neoplasia: Immunohistochemical analysis
inferredcites →https://doi.org/10.7150/ijbs.28834openalex-snapshot
Calpain-2 Enhances Non-Small Cell Lung Cancer Progression and Chemoresistance to Paclitaxel via EGFR-pAKT Pathway
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.3390/ijms262110501openalex-snapshot
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inferred← citeshttps://doi.org/10.3390/life13030854openalex-snapshot
Phosphorylation of Calpastatin Negatively Regulates the Activity of Calpain
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600125openalex-snapshot
Additional file 1 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600128openalex-snapshot
Additional file 2 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600131openalex-snapshot
Additional file 3 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600134openalex-snapshot
Additional file 4 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600140openalex-snapshot
Additional file 5 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600143openalex-snapshot
Additional file 6 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600146openalex-snapshot
Additional file 7 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600149openalex-snapshot
Additional file 8 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600152openalex-snapshot
Additional file 9 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600155openalex-snapshot
Additional file 10 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600158openalex-snapshot
Additional file 11 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600161openalex-snapshot
Additional file 12 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600164openalex-snapshot
Additional file 13 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600167openalex-snapshot
Additional file 14 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26600170openalex-snapshot
Additional file 15 of Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis
inferred← citeshttps://doi.org/10.6084/m9.figshare.26675585openalex-snapshot
Additional file 1 of T-type voltage-gated channels, Na+/Ca2+-exchanger, and calpain-2 promote photoreceptor cell death in inherited retinal degeneration
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