{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dong Y"],"funding":["NIDDK NIH HHS","NCRR NIH HHS","NHLBI NIH HHS"],"pagination":["4349-64"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4665789"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["125(12)"],"pubmed_abstract":["Tumor angiogenesis is critical for cancer progression. In multiple murine models, endothelium-specific epsin deficiency abrogates tumor progression by shifting the balance of VEGFR2 signaling toward uncontrolled tumor angiogenesis, resulting in dysfunctional tumor vasculature. Here, we designed a tumor endothelium-targeting chimeric peptide (UPI) for the purpose of inhibiting endogenous tumor endothelial epsins by competitively binding activated VEGFR2. We determined that the UPI peptide specifically targets tumor endothelial VEGFR2 through an unconventional binding mechanism that is driven by unique residues present only in the epsin ubiquitin-interacting motif (UIM) and the VEGFR2 kinase domain. In murine models of neoangiogenesis, UPI peptide increased VEGF-driven angiogenesis and neova"],"journal":["The Journal of clinical investigation"],"pubmed_title":["Motif mimetic of epsin perturbs tumor growth and metastasis."],"pmcid":["PMC4665789"],"funding_grant_id":["R01 HL093242","1F31HL127982-01","P20 RR018758","SC1 DK104821","P01 HL085607","R01 HL130845","F32 HL121954","R01 HL137229","R01 HL118676","R01HL-093242","F31 HL127982","P01HL085607","SC1DK104821","1 F32 HL121954-01A1"],"pubmed_authors":["Lupu F","Yu L","Dong Y","Rahman HN","Wu H","Liu X","Liu Y","Song K","Brophy ML","Saunders D","Chang B","Towner R","Xia L","Dong J","Pasula S","Mehta-D'Souza P","Srinivasan RS","Silasi-Mansat R","Boerboom D","Chen H","Song H","Hahn S","Njoku C","McManus J","McEver RP","Cai X","Tessneer KL"],"additional_accession":[]},"is_claimable":false,"name":"Motif mimetic of epsin perturbs tumor growth and metastasis.","description":"Tumor angiogenesis is critical for cancer progression. In multiple murine models, endothelium-specific epsin deficiency abrogates tumor progression by shifting the balance of VEGFR2 signaling toward uncontrolled tumor angiogenesis, resulting in dysfunctional tumor vasculature. Here, we designed a tumor endothelium-targeting chimeric peptide (UPI) for the purpose of inhibiting endogenous tumor endothelial epsins by competitively binding activated VEGFR2. We determined that the UPI peptide specifically targets tumor endothelial VEGFR2 through an unconventional binding mechanism that is driven by unique residues present only in the epsin ubiquitin-interacting motif (UIM) and the VEGFR2 kinase domain. In murine models of neoangiogenesis, UPI peptide increased VEGF-driven angiogenesis and neova","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Dec","modification":"2026-05-05T07:20:05.159Z","creation":"2026-04-07T21:30:56.184Z"},"accession":"S-EPMC4665789","cross_references":{"pubmed":["26571402"],"doi":["10.1172/jci80349","10.1172/JCI80349"]}}