{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Delinois LJ"],"funding":["NIDDK NIH HHS","National Institute of Diabetes and Digestive and Kidney Diseases","NCI NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["2185-2192"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7722079"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(22)"],"pubmed_abstract":["Malignant gliomas are the most lethal form of primary brain tumors. Despite advances in cancer therapy, the prognosis of glioma patients has remained poor. Cytochrome c (Cytc), an endogenous heme-based protein, holds tremendous potential to treat gliomas because of its innate capacity to trigger apoptosis. To this end, a hybrid cytochrome c-chlorotoxin (Cytc-CTX) protein was biosynthesized to enable cellular uptake of the cell impenetrable Cytc using CTX transporters. A nucleotide sequence containing 1 : 1 Cytc and CTX was constructed and separated by a hexahistidine-tag and an enterokinase cleavage site. The sequence was cloned into a pBTR1 plasmid, expressed in Escherichia coli, purified via 2-dimensional chromatography. The identity and size of the protein were determined by Western blo"],"journal":["ChemMedChem"],"pubmed_title":["A Cytochrome c-Chlorotoxin Hybrid Protein as a Possible Antiglioma Drug."],"pmcid":["PMC7722079"],"funding_grant_id":["R25 GM061151","SC1 CA190504","P20GM103642","P20 GM103642","R25 DK098067"],"pubmed_authors":["Delinois LJ","Villalobos-Santos JC","Miller J","Peon H","Ramirez-Paz J","Tinoco AD","Griebenow KH"],"additional_accession":[]},"is_claimable":false,"name":"A Cytochrome c-Chlorotoxin Hybrid Protein as a Possible Antiglioma Drug.","description":"Malignant gliomas are the most lethal form of primary brain tumors. Despite advances in cancer therapy, the prognosis of glioma patients has remained poor. Cytochrome c (Cytc), an endogenous heme-based protein, holds tremendous potential to treat gliomas because of its innate capacity to trigger apoptosis. To this end, a hybrid cytochrome c-chlorotoxin (Cytc-CTX) protein was biosynthesized to enable cellular uptake of the cell impenetrable Cytc using CTX transporters. A nucleotide sequence containing 1 : 1 Cytc and CTX was constructed and separated by a hexahistidine-tag and an enterokinase cleavage site. The sequence was cloned into a pBTR1 plasmid, expressed in Escherichia coli, purified via 2-dimensional chromatography. The identity and size of the protein were determined by Western blo","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2025-04-21T21:34:59.467Z","creation":"2022-02-11T12:53:22.724Z"},"accession":"S-EPMC7722079","cross_references":{"pubmed":["32918396"],"doi":["10.1002/cmdc.202000373"]}}