Publication:
A small molecule identified through an in silico screen inhibits Aurora B–INCENP interaction

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dc.contributor.departmentN/A
dc.contributor.departmentN/A
dc.contributor.departmentN/A
dc.contributor.departmentDepartment of Chemical and Biological Engineering
dc.contributor.departmentDepartment of Molecular Biology and Genetics
dc.contributor.kuauthorÜnsal, Esra
dc.contributor.kuauthorHarmanda, Büşra
dc.contributor.kuauthorErman, Burak
dc.contributor.kuprofileMaster Student
dc.contributor.kuprofileN/A
dc.contributor.kuprofilePhD Student
dc.contributor.kuprofileFaculty Member
dc.contributor.kuprofileFaculty Member
dc.contributor.otherDepartment of Chemical and Biological Engineering
dc.contributor.otherDepartment of Molecular Biology and Genetics
dc.contributor.schoolcollegeinstituteGraduate School of Sciences and Engineering
dc.contributor.schoolcollegeinstituteN/A
dc.contributor.schoolcollegeinstituteGraduate School of Sciences and Engineering
dc.contributor.schoolcollegeinstituteCollege of Engineering
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.yokidN/A
dc.contributor.yokidN/A
dc.contributor.yokidN/A
dc.contributor.yokid179997
dc.contributor.yokid105301
dc.date.accessioned2024-11-09T23:23:34Z
dc.date.issued2016
dc.description.abstractAurora B is a serine/threonine kinase that has a central role in the regulation of mitosis. The observation of Aurora B overexpression in cancer makes it a promising target to develop antitumoral inhibitors. We describe a new potential inhibitor that exclusively targets the interaction site of Aurora B and its activator INCENP. We performed a structure-based virtual screening and determined five potential candidates of 200000 compounds, which selectively bind to the Aurora B
dc.description.indexedbyWoS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue6
dc.description.openaccessNO
dc.description.sponsorshipEMBO (European Molecular Biology Organization) Installation Grant, European Union Marie Curie Career Integration Grant N. Ozlu is funded by EMBO (European Molecular Biology Organization) Installation Grant, European Union Marie Curie Career Integration Grant. Authors would like to thank Hyman Laboratory (MPI-CBG, Dresden) for the HeLa Kyoto cells stably expressing Aurora B-LAP-tagged BAC transgenes and Drs Nazan Saner and Aynur Kaya-Copur for the critical reading of the manuscript.
dc.description.volume88
dc.identifier.doi10.1111/cbdd.12816
dc.identifier.eissn1747-0285
dc.identifier.issn1747-0277
dc.identifier.scopus2-s2.0-84982233931
dc.identifier.urihttp://dx.doi.org/10.1111/cbdd.12816
dc.identifier.urihttps://hdl.handle.net/20.500.14288/11265
dc.identifier.wos387362800001
dc.keywordsAurora B kinase
dc.keywordsSelective kinase inhibitor
dc.keywordsStructure-based virtual screening
dc.keywordsProtein data-bank
dc.keywordsCell-division
dc.keywordsA activation
dc.keywordsKinase
dc.keywordsSpindle
dc.keywordsPhosphorylation
dc.keywordsGrowth
dc.keywordsTPX2
dc.keywordsCytokinesis
dc.keywordsHesperadin
dc.languageEnglish
dc.publisherWiley
dc.sourceChemical Biology and Drug Design
dc.subjectBiochemistry
dc.subjectMolecular biology
dc.subjectClinical chemistry
dc.subjectPharmacology
dc.subjectPharmacy
dc.titleA small molecule identified through an in silico screen inhibits Aurora B–INCENP interaction
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.authoridN/A
local.contributor.authoridN/A
local.contributor.authorid0000-0003-1159-5698
local.contributor.authorid0000-0002-2496-6059
local.contributor.authorid0000-0002-5157-8780
local.contributor.kuauthorÜnsal, Esra
local.contributor.kuauthorDeğirmenci, Bahar
local.contributor.kuauthorHarmanda, Büşra
local.contributor.kuauthorErman, Burak
local.contributor.kuauthorÖzlü, Nurhan
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relation.isOrgUnitOfPublication.latestForDiscoveryaee2d329-aabe-4b58-ba67-09dbf8575547

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