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Physiol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0455","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1080\/01635581.2014.939291","article-title":"Resveratrol: inhibitory effects on metastatic cell behaviors and voltage-gated Na+ channel activity in rat prostate cancer in vitro","volume":"66","author":"Fraser","year":"2014","journal-title":"Nutr. Cancer"},{"key":"10.1016\/j.ceca.2019.05.003_bib0460","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1111\/j.1476-5381.2008.00059.x","article-title":"Eicosapentaenoic acid inhibits voltage-gated sodium channels and invasiveness in prostate cancer cells","volume":"56","author":"Nakajima","year":"2009","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0465","doi-asserted-by":"crossref","first-page":"2985","DOI":"10.3892\/ol.2016.4941","article-title":"Effects of Hedera helix L. Extracts on rat prostate cancer cell proliferation and motilit","volume":"12","author":"Gumushan-Aktas","year":"2016","journal-title":"Oncol. Lett."},{"key":"10.1016\/j.ceca.2019.05.003_bib0470","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1002\/(SICI)1097-4652(199804)175:1<50::AID-JCP6>3.0.CO;2-B","article-title":"Electrophysiological characterization of voltage-gated Na+ current expressed in the highly metastatic Mat-LyLu cell line of rat prostate cancer","volume":"175","author":"Grimes","year":"1998","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0475","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.jprot.2014.04.035","article-title":"A proteomic analysis of the early secondary molecular effects caused by Cn2 scorpion toxin on neuroblastoma cells","volume":"111","author":"Escalona","year":"2014","journal-title":"J. Proteomics"},{"key":"10.1016\/j.ceca.2019.05.003_bib0480","doi-asserted-by":"crossref","first-page":"20326","DOI":"10.1074\/jbc.M600565200","article-title":"Resurgent current and voltage sensor trapping enhanced activation by a beta-scorpion toxin solely in Nav1.6 channel. Significance in mice Purkinje neurons","volume":"281","author":"Schiavon","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0485","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1081\/PB-120015456","article-title":"Isolation, purification, and Nterminal partial sequence of an antitumor peptide from the venom of the Chinese scorpion Buthus martensii Karsch","volume":"32","author":"Liu","year":"2002","journal-title":"Prep. Biochem. Biotechnol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0490","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.peptides.2013.10.023","article-title":"Purification, characterization, and bioactivity of a new analgesic-antitumor peptide from Chinese scorpion Buthus martensii Karsch","volume":"53","author":"Shao","year":"2014","journal-title":"Peptides"},{"key":"10.1016\/j.ceca.2019.05.003_bib0495","doi-asserted-by":"crossref","first-page":"483","DOI":"10.3892\/ol.2012.1049","article-title":"Analgesic-antitumor peptide induces apoptosis and inhibits the proliferation of SW480 human colon cancer cells","volume":"5","author":"Gu","year":"2013","journal-title":"Oncol. Lett."},{"key":"10.1016\/j.ceca.2019.05.003_bib0500","first-page":"228","article-title":"Production and antitumor efficacy of recombinant Buthus martensii Karsch AGAP","volume":"4","author":"Liu","year":"2009","journal-title":"Asian J. Tradit. 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Physiol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0525","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1038\/sj.pcan.4500796","article-title":"A potential novel marker for human prostate cancer: voltage-gated sodium channel expression in vivo","volume":"8","author":"Diss","year":"2005","journal-title":"Prostate Cancer Prostatic Dis."},{"key":"10.1016\/j.ceca.2019.05.003_bib0530","doi-asserted-by":"crossref","first-page":"5381","DOI":"10.1158\/1078-0432.CCR-05-0327","article-title":"Voltage-gated sodium channel expression and potentiation of human breast cancer metastasis","volume":"11","author":"Fraser","year":"2005","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0535","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/s00232-005-0747-6","article-title":"Small-cell lung cancer (human): potentiation of endocytic membrane activity by voltage-gated Na+ channel expression in vitro","volume":"204","author":"Onganer","year":"2005","journal-title":"J. Membr. Biol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0540","doi-asserted-by":"crossref","first-page":"849","DOI":"10.3390\/cancers7020813","article-title":"Voltage-gated ion channels in Cancer cell proliferation","volume":"7","author":"Rao","year":"2015","journal-title":"Cancers"},{"key":"10.1016\/j.ceca.2019.05.003_bib0545","first-page":"147","article-title":"Electrical potential measurements in human breast Cancer and benign lesions","volume":"15","author":"Marino","year":"1994","journal-title":"TBI"},{"key":"10.1016\/j.ceca.2019.05.003_bib0550","doi-asserted-by":"crossref","first-page":"e652","DOI":"10.1038\/cddis.2013.174","article-title":"Potassium channel activation inhibits proliferation of breast cancer cells by activating a senescence program","volume":"4","author":"Lansu","year":"2019","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.ceca.2019.05.003_bib0555","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0306-4522(03)00425-1","article-title":"Activation of vo\u2009ltage-sensitive sodium channels during oxygen deprivation leads to apoptotic neuronal death","volume":"126","author":"Banasiak","year":"2004","journal-title":"Neuroscience"},{"key":"10.1016\/j.ceca.2019.05.003_bib0560","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1085\/jgp.95.4.591","article-title":"Relationships between the neuronal sodium\/potassium pump and energy metabolism. Effects of K+, Na+, and adenosine triphosphate in isolated brain synaptosomes","volume":"95","author":"Ereci\u0144ska","year":"1990","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0565","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/BF00768844","article-title":"Cl-, Na +, and H + Fluxes during the Acidification of Rabbit Reticulocyte Endocytic Vesicles","volume":"23","author":"Gaete","year":"1991","journal-title":"J. Bioenerg. Biomembr."},{"issue":"December (8)","key":"10.1016\/j.ceca.2019.05.003_bib0570","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1038\/sj.bjp.0707513","article-title":"Potentiation of E-4031-induced torsade de pointes by HMR1556 or ATX-II is not predicted by action potential short-term variability or triangulation","volume":"152","author":"Michael","year":"2007","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0575","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/S0006-8993(97)01149-9","article-title":"Intracellular acidification induced by membrane depolarization in rat hippocampal slices: roles of intracellular Ca2+ and glycolysis","volume":"780","author":"Zhan","year":"1998","journal-title":"Brain Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0580","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/S0361-9230(99)00246-4","article-title":"Sodium overload through voltage-dependent Na+ channels induces necrosis and apoptosis of rat superior cervical ganglion cells in vitro","volume":"51","author":"Koike","year":"2000","journal-title":"Brain Res. Bull."},{"key":"10.1016\/j.ceca.2019.05.003_bib0585","doi-asserted-by":"crossref","first-page":"1892","DOI":"10.1038\/sj.bjc.6690617","article-title":"Acidic environment causes apoptosis by increasing caspase activity","volume":"80","author":"Park","year":"1999","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.ceca.2019.05.003_bib0590","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.neuroscience.2003.08.030","article-title":"Role and regulation of p53 in depolarization-induced neuronal death","volume":"122","author":"Jordan","year":"2003","journal-title":"Neuroscience"},{"key":"10.1016\/j.ceca.2019.05.003_bib0595","doi-asserted-by":"crossref","first-page":"39176","DOI":"10.1074\/jbc.M303516200","article-title":"Uncoupling cell shrinkage from apoptosis reveals that Na+ influx is required for volume loss during programmed cell death","volume":"278","author":"Bortner","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0600","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0306-4522(03)00425-1","article-title":"Activation of voltage-sensitive sodium channels during oxygen deprivation leads to apoptotic neuronal death","volume":"126","author":"Banasiak","year":"2004","journal-title":"Neuroscience"},{"key":"10.1016\/j.ceca.2019.05.003_bib0605","doi-asserted-by":"crossref","first-page":"2532","DOI":"10.1016\/j.bbamem.2014.10.030","article-title":"Ion channels in the regulation of apoptosis","volume":"1848","author":"Kondratskyi","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ceca.2019.05.003_bib0610","doi-asserted-by":"crossref","first-page":"3221","DOI":"10.1002\/1873-3468.12357","article-title":"The 2 scorpion toxin Bot IX is a potent member of the \u03b1-like family and has a unique N3 terminal sequence extension","volume":"590","author":"Martin-Eauclaire","year":"2016","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ceca.2019.05.003_bib0615","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1042\/BJ20060035","article-title":"Chinese-scorpion (Buthus martensi Karsch) toxin BmK alphaIV, a novel modulator of sodium channels: from genomic organization to functional analysis","volume":"399","author":"Chai","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.ceca.2019.05.003_bib0620","doi-asserted-by":"crossref","first-page":"2534","DOI":"10.3390\/toxins7072534","article-title":"Revealing the function and the structural model of Ts4: insights into the \"Non-Toxic\" toxin from Tityus serrulatus venom","volume":"7","author":"Pucca","year":"2015","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.ceca.2019.05.003_bib0625","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s12264-012-1234-6","article-title":"Pharmacological kinetics of BmK AS, a sodium channel site 4-specific modulator on Nav1.3","volume":"28","author":"Liu","year":"2012","journal-title":"Neurosci. Bull."},{"key":"10.1016\/j.ceca.2019.05.003_bib0630","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1124\/mol.106.022970","article-title":"Potent modulation of the voltage-gated sodium channel Nav1.7 by OD1, a toxin from the scorpion Odonthobuthus doriae","volume":"70","author":"Maertens","year":"2006","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0635","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1016\/j.pain.2013.03.037","article-title":"The scorpion toxin Amm VIII induces pain hypersensitivity through gain-of-function of TTX-sensitive Na+ channels","volume":"154","author":"Abbas","year":"2013","journal-title":"Pain"},{"key":"10.1016\/j.ceca.2019.05.003_bib0640","doi-asserted-by":"crossref","first-page":"7775","DOI":"10.1021\/bi300776g","article-title":"Binding modes and functional surface of anti-mammalian scorpion \u03b1-toxins to sodium channels","volume":"51","author":"Chen","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.ceca.2019.05.003_bib0645","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1085\/jgp.201110720","article-title":"Scorpion \u03b2-toxin interference with NaV channel voltage sensor gives rise to excitatory and depressant modes","volume":"139","author":"Leipold","year":"2012","journal-title":"Gen Physiol"},{"key":"10.1016\/j.ceca.2019.05.003_bib0650","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1016\/j.bbapap.2012.01.003","article-title":"Solution structure of native and recombinant expressed toxin CssII from the venom of the scorpion Centruroides suffusus suffusus, and their effects on Nav1.5 sodium channels","volume":"1824","author":"Saucedo","year":"2012","journal-title":"Biochim. 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Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0665","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.toxicon.2012.03.022","article-title":"Mapping of scorpion toxin receptor sites at voltage-gated sodium channels","volume":"60","author":"Gurevitz","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.ceca.2019.05.003_bib0670","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0041-0101(02)00294-5","article-title":"The selectivity of scorpion alpha-toxins for sodium channel subtypes is determined by subtle variations at the interacting surface","volume":"41","author":"Gordon","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.ceca.2019.05.003_bib0675","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1111\/j.1742-4658.2007.05737.x","article-title":"The unique pharmacology of the scorpion alpha-like toxin Lqh3 is associated with its flexible C-tail","volume":"274","author":"Karbat","year":"2007","journal-title":"FEBS J."},{"key":"10.1016\/j.ceca.2019.05.003_bib0680","doi-asserted-by":"crossref","first-page":"572","DOI":"10.2741\/4121","article-title":"Scorpion beta-toxins and voltage-gated sodium channels: interactions and effects","volume":"18","author":"Pedraza Escalona","year":"2013","journal-title":"Front. Biosci. (Landmark Ed)"},{"key":"10.1016\/j.ceca.2019.05.003_bib0685","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1002\/psc.744","article-title":"Deduction of functional peptide motifs in scorpion toxins","volume":"12","author":"Tan","year":"2006","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0690","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.ijbiomac.2017.01.020","article-title":"The roles of conserved aromatic residues (Tyr5 and Tyr42) in interaction of scorpion toxin BmK AGP-SYPU1 with human Nav1.7","volume":"99","author":"Meng","year":"2017","journal-title":"Int. J. Biol. 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Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0710","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1016\/j.cellsig.2008.06.006","article-title":"Both EGFR kinase and Src-related tyrosine kinases regulate human ether-a-go-go-elated gene potassium channels","volume":"20","author":"Zhang","year":"2008","journal-title":"Cell. Signal."},{"key":"10.1016\/j.ceca.2019.05.003_bib0715","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.tcb.2006.10.003","article-title":"A. Complex functional interaction between integrin receptors and ion channels","volume":"16","author":"Arcangeli","year":"2006","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0720","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1085\/jgp.20028607","article-title":"Molecular proximity of Kv1.3 voltage-gated potassium channels and beta1-integrins on the plasma membrane of melanoma cells: effects of cell adherence and channel blockers","volume":"120","author":"Vira","year":"2002","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0725","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.ejphar.2010.10.066","article-title":"Anti-proliferative effect of Kv1.3 blockers in A549 human lung adenocarcinoma in vitro and in vivo","volume":"651","author":"Jang","year":"2011","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0730","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1002\/emmm.201200235","article-title":"Inhibitors of mitochondrial Kv1.3 channels induce Bax\/Bak-independent death of cancer cells","volume":"4","author":"Leanza","year":"2012","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.ceca.2019.05.003_bib0735","doi-asserted-by":"crossref","DOI":"10.1098\/rstb.2013.0094","article-title":"Potassium channels in cell cycle and cell proliferation","volume":"369","author":"Urrego","year":"2014","journal-title":"Philos. Trans. R. Soc. Lond., B, Biol. Sci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0740","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/jnr.20240","article-title":"Role for Calcium-A\u2009ctivated Potassium Channels (BK) in Growth Control of Human Malignant Glioma Cells","volume":"78","author":"Weaver","year":"2004","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0745","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1002\/ddr.20467","article-title":"The lymphocyte potassium channels Kv1.3 and KCa3.1 as targets for immunosuppression","volume":"72","author":"Lam","year":"2011","journal-title":"Drug Dev. Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0750","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/jnr.20240","article-title":"Role for calcium-activated potassium channels (BK) in growth control of human malignant glioma cells","volume":"78","author":"Weaver","year":"2004","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0755","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1159\/000016309","article-title":"K+ channel-dependent migration of fibroblasts and human melanoma cells","volume":"9","author":"Schwab","year":"1999","journal-title":"Cell. Physiol. Biochem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0760","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1111\/j.1460-9568.2004.03265.x","article-title":"Functional importance of Ca2+-activated K+ channels for lysophosphatidic acid-induced microglial migration","volume":"19","author":"Schilling","year":"2004","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0765","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1085\/jgp.91.3.317","article-title":"Charybdotoxin block of single Ca2+-activated K+ channels. Effects of channel gating, voltage, and ionic strength, the Charybdotoxin block of single Ca2+-activated K+ channels","volume":"91","author":"Anderson","year":"1988","journal-title":"J. Gen. Physiol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0770","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1023\/A:1008892620231","article-title":"Dipole moments of scorpion toxins direct the interaction towards small-or large-conductance Ca 2+-activated K+ channels","volume":"4","author":"Fremont","year":"1997","journal-title":"Lett. Pept. Sci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0775","doi-asserted-by":"crossref","first-page":"4302","DOI":"10.1074\/jbc.272.7.4302","article-title":"On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures","volume":"272","author":"Dauplais","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0780","doi-asserted-by":"crossref","first-page":"2503","DOI":"10.2174\/138161208785777441","article-title":"Animal toxins acting on voltage-gated potassium channels","volume":"14","author":"Mouhat","year":"2008","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.ceca.2019.05.003_bib0785","doi-asserted-by":"crossref","first-page":"15834","DOI":"10.1021\/bi051656d","article-title":"Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex","volume":"44","author":"Yu","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.ceca.2019.05.003_bib0790","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.00594","article-title":"Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel","volume":"2","author":"Banerjee","year":"2013","journal-title":"Elife"},{"key":"10.1016\/j.ceca.2019.05.003_bib0795","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1016\/S0306-4522(97)00456-9","article-title":"Expression of voltage-activated chloride currents in acute slices of human gliomas","volume":"83","author":"Ullrich","year":"1998","journal-title":"Neuroscience"},{"key":"10.1016\/j.ceca.2019.05.003_bib0800","doi-asserted-by":"crossref","first-page":"5942","DOI":"10.1523\/JNEUROSCI.19-14-05942.1999","article-title":"Modulation of glioma cell migration and invasion using Cl\u2212 and K+ ion channel blockers","volume":"19","author":"Soroceanu","year":"1999","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0805","doi-asserted-by":"crossref","first-page":"779","DOI":"10.3181\/0711-MR-308","article-title":"An unexpected role for ion channels in brain tumor metastasis","volume":"233","author":"Sontheimer","year":"2008","journal-title":"Exp. Biol. Med."},{"key":"10.1016\/j.ceca.2019.05.003_bib0810","series-title":"Chlorotoxin Protein (ab60871), Product Datasheet","author":"Abcam","year":"2007"},{"key":"10.1016\/j.ceca.2019.05.003_bib0815","first-page":"580","article-title":"Imaging glioma extent with 131I-TM-601","volume":"46","author":"Hockaday","year":"2005","journal-title":"J. Nucl. Med."},{"key":"10.1016\/j.ceca.2019.05.003_bib0820","doi-asserted-by":"crossref","first-page":"3644","DOI":"10.1200\/JCO.2005.05.4569","article-title":"Phase I single-dose study of intracavitary-administered iodine-131-TM-601 in adults with recurrent high-grade glioma","volume":"24","author":"Mamelak","year":"2006","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.ceca.2019.05.003_bib0825","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1110\/ps.062416606","article-title":"Statistical potential for assessment and prediction of protein structures","volume":"15","author":"Shen","year":"2006","journal-title":"Protein Sci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0830","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.jocn.2016.04.012","article-title":"Glioblastoma multiforme targeted therapy: the Chlorotoxin story","volume":"33","author":"Cohen-Inbar","year":"2016","journal-title":"J. Clin. Neurosci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0835","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1111\/jpi.12239","article-title":"Doxorubicin resistance in breast cancer is driven by light at night\u2010induced disruption of the circadian melatonin signal","volume":"59","author":"Xiang","year":"2015","journal-title":"J. Pineal Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0840","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.jinorgbio.2012.02.012","article-title":"Platinum (IV)-chlorotoxin (CTX) conjugates for targeting cancer cells","volume":"110","author":"Graf","year":"2012","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0845","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.canlet.2009.10.011","article-title":"BmKCT toxin inhibits glioma proliferation and tumor metastasis","volume":"291","author":"Fan","year":"2010","journal-title":"Cancer Lett."},{"key":"10.1016\/j.ceca.2019.05.003_bib0850","doi-asserted-by":"crossref","first-page":"4135","DOI":"10.1074\/jbc.M205662200","article-title":"Chlorotoxin inhibits glioma cells invasion via matrix metalloproteinase-2","volume":"278","author":"Deshane","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0855","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1097\/00001756-199604100-00013","article-title":"Human astrocytoma cells express a unique chloride current","volume":"7","author":"Ullrich","year":"1996","journal-title":"Neuroreport"},{"key":"10.1016\/j.ceca.2019.05.003_bib0860","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/nrn3765","article-title":"A neurocentric perspective on glioma invasion","volume":"15","author":"Cuddapah","year":"2014","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.ceca.2019.05.003_bib0865","doi-asserted-by":"crossref","first-page":"19799","DOI":"10.1038\/srep19799","article-title":"N.E. Savaskan. Identification of two novel Chlorotoxin derivatives CA4 and CTX-23 with chemotherapeutic and anti-angiogenic potential","volume":"6","author":"Xu","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ceca.2019.05.003_bib0870","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/152659","article-title":"Chlorotoxin-Fc fusion inhibits release of MMP-2 from pancreatic cancer cells","author":"El-Ghlban","year":"2014","journal-title":"Biomed Res. Int."},{"key":"10.1016\/j.ceca.2019.05.003_bib0875","doi-asserted-by":"crossref","first-page":"5908","DOI":"10.1016\/j.biomaterials.2014.03.077","article-title":"The impact of a chlorotoxin-modified liposome system on receptor MMP-2 and the receptor-associated protein ClC-3","volume":"35","author":"Qin","year":"2014","journal-title":"Biomaterials"},{"key":"10.1016\/j.ceca.2019.05.003_bib0880","first-page":"4515","article-title":"Invasion of human glioma cells is regulated by multiple chloride channels including ClC-3","volume":"30","author":"Chi Hang Lui","year":"2010","journal-title":"Anticancer Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0885","doi-asserted-by":"crossref","first-page":"2815","DOI":"10.1080\/07391102.2016.1231633","article-title":"In Silico prediction of the molecular basis of ClTx and AaCTx interaction with matrix metalloproteinase-2 (MMP-2) to inhibit glioma cell invasion","volume":"35","author":"Othman","year":"2017","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.ceca.2019.05.003_bib0890","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/S0092-8674(00)81235-0","article-title":"Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3","volume":"85","author":"Brooks","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.ceca.2019.05.003_bib0895","doi-asserted-by":"crossref","first-page":"22939","DOI":"10.1074\/jbc.C115.671107","article-title":"Matrix metalloproteinase (MMP) proteolysis of the extracellular loop of voltage-gated sodium channels and potential alterations in pain signaling","volume":"290","author":"Remacle","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0900","doi-asserted-by":"crossref","first-page":"22116","DOI":"10.1074\/jbc.270.38.22116","article-title":"Identification of calcium release-triggering and blocking regions of the II-III loop of the skeletal muscle dihydropyridine receptor","volume":"270","author":"el-Hayek","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0905","doi-asserted-by":"crossref","first-page":"4013","DOI":"10.1074\/jbc.C400433200","article-title":"Maurocalcine and domain A of the II-III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor","volume":"280","author":"Altafaj","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0910","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.3390\/ph3041093","article-title":"Imperatoxin A, a Cell-Penetrating Peptide from Scorpion Venom, as a Probe of Ca2+-Release Channels\/Ryanodine Receptors","volume":"3","author":"Gurrola","year":"2010","journal-title":"Pharmaceuticals Basel (Basel)"},{"key":"10.1016\/j.ceca.2019.05.003_bib0915","doi-asserted-by":"crossref","first-page":"27048","DOI":"10.1074\/jbc.M804727200","article-title":"Waard design of a disulfide-less, pharmacologically inert, and chemically competent analog of Maurocalcine for the efficient transport of impermeant compounds into cells","volume":"283","author":"Ram","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib0920","doi-asserted-by":"crossref","first-page":"12833","DOI":"10.1074\/jbc.M412521200","article-title":"Transduction of the scorpion toxin maurocalcine into cells. 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Res."},{"key":"10.1016\/j.ceca.2019.05.003_bib0945","doi-asserted-by":"crossref","first-page":"4336","DOI":"10.1021\/acs.molpharmaceut.5b00531","article-title":"A novel platinum-maurocalcine conjugate induces apoptosis of human glioblastoma cells by acting through the ROS-ERK\/AKT-p53 pathway","volume":"12","author":"Aroui","year":"2015","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.ceca.2019.05.003_bib0950","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.biocel.2016.05.013","article-title":"PTEN-regulated AKT\/FoxO3a\/Bim signaling contributes to Human cell glioblastoma apoptosis by platinum-maurocalcin conjugate","volume":"77","author":"Aroui","year":"2016","journal-title":"Int. J. Biochem. 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Chem."},{"key":"10.1016\/j.ceca.2019.05.003_bib1015","doi-asserted-by":"crossref","first-page":"7858","DOI":"10.1038\/sj.onc.1206895","article-title":"Expression of the Ca2+-selective cation channel TRPV6 in human prostate cancer: a novel prognostic marker for tumor progression","volume":"22","author":"Fixemer","year":"2003","journal-title":"Oncogene"},{"key":"10.1016\/j.ceca.2019.05.003_bib1020","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1007\/s10637-017-0438-z","article-title":"First-in-human phase I study of SOR-C13, a TRPV6 calcium channel inhibitor, in patients with advanced solid tumors","volume":"35","author":"Fu","year":"2017","journal-title":"Invest. New Drugs"},{"key":"10.1016\/j.ceca.2019.05.003_bib1025","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1093\/jnci\/djq217","article-title":"Essential role of TRPC6 channels in G2\/M phase transition and development of human glioma","volume":"102","author":"Ding","year":"2010","journal-title":"J. Natl. 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