2019
Mutations in TFAP2B and previously unimplicated genes of the BMP, Wnt, and Hedgehog pathways in syndromic craniosynostosis
Timberlake AT, Jin SC, Nelson-Williams C, Wu R, Furey CG, Islam B, Haider S, Loring E, Galm A, Steinbacher D, Larysz D, Staffenberg D, Flores R, Rodriguez E, Boggon T, Persing J, Lifton R, Lifton RP, Gunel M, Mane S, Bilguvar K, Gerstein M, Loring E, Nelson-Williams C, Lopez F, Knight J. Mutations in TFAP2B and previously unimplicated genes of the BMP, Wnt, and Hedgehog pathways in syndromic craniosynostosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 15116-15121. PMID: 31292255, PMCID: PMC6660739, DOI: 10.1073/pnas.1902041116.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAlpha CateninChildChild, PreschoolCraniosynostosesExomeExome SequencingFemaleGene ExpressionGlypicansHistone AcetyltransferasesHumansMaleMutationNuclear ProteinsPedigreeRisk AssessmentSignal TransductionSkullSOXC Transcription FactorsTranscription Factor AP-2Zinc Finger Protein Gli2ConceptsRare damaging mutationsSyndromic craniosynostosisCongenital anomaliesDamaging mutationsSyndromic casesExome sequencingAdditional congenital anomaliesFrequent congenital anomaliesDamaging de novo mutationsNeural crest cell migrationDamaging de novoCrest cell migrationCS patientsMutation burdenChromatin modifiersSubsequent childrenTranscription factorsDe novo mutationsCS casesCS geneHedgehog pathwayDisease locusPremature fusionFunction mutationsCraniosynostosis
2017
Disruptions in asymmetric centrosome inheritance and WDR62-Aurora kinase B interactions in primary microcephaly
Sgourdou P, Mishra-Gorur K, Saotome I, Henagariu O, Tuysuz B, Campos C, Ishigame K, Giannikou K, Quon JL, Sestan N, Caglayan AO, Gunel M, Louvi A. Disruptions in asymmetric centrosome inheritance and WDR62-Aurora kinase B interactions in primary microcephaly. Scientific Reports 2017, 7: 43708. PMID: 28272472, PMCID: PMC5341122, DOI: 10.1038/srep43708.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAurora Kinase BBrainCell CycleCell Cycle ProteinsCell DifferentiationCell ProliferationCentrosomeConsanguinityDisease Models, AnimalEpistasis, GeneticFluorescent Antibody TechniqueGene ExpressionHumansInheritance PatternsMaleMiceMice, KnockoutMicrocephalyMutationNerve Tissue ProteinsNeural Stem CellsPedigreeWhole Genome SequencingConceptsChromosome passenger complexPatient-derived fibroblastsCentrosome inheritanceNeocortical progenitorsDisease-associated mutant formsSpindle pole localizationAurora kinase BPassenger complexMitotic progressionMouse orthologDiverse functionsMutant formsWD repeat domain 62Key regulatorCPC componentsKinase BPole localizationPrimary microcephalyLate neurogenesisRecessive mutationsNeuronal differentiationWDR62Severe brain malformationsReduced proliferationNeocortical development
2015
A congenital disorder of deglycosylation: Biochemical characterization of N-glycanase 1 deficiency in patient fibroblasts
He P, Grotzke JE, Ng BG, Gunel M, Jafar-Nejad H, Cresswell P, Enns GM, Freeze HH. A congenital disorder of deglycosylation: Biochemical characterization of N-glycanase 1 deficiency in patient fibroblasts. Glycobiology 2015, 25: 836-844. PMID: 25900930, PMCID: PMC4487302, DOI: 10.1093/glycob/cwv024.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsDevelopmental DisabilitiesEnzyme AssaysExonsEye Diseases, HereditaryFibroblastsGene ExpressionGenes, ReporterHepatic InsufficiencyHumansLacrimal Apparatus DiseasesLuminescent ProteinsMutationPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePeripheral Nervous System DiseasesPrimary Cell CultureSeizuresConceptsAbnormal liver functionPatient fibroblastsPeripheral neuropathyLiver functionPatient-derived fibroblastsDevelopmental delayCongenital disorderN-glycanase 1 (NGLY1) deficiencyVenus fluorescencePronounced reductionFibroblastsN-glycanase 1Enzymatic activityMutationsNGLY1NeuropathyPatientsSeizuresAlacrimaActivity
2005
Expression of Structural Proteins and Angiogenic Factors in Normal Arterial and Unruptured and Ruptured Aneurysm Walls
Kılıc T, Sohrabifar M, Kurtkaya Ö, Yildirim Ö, Elmaci I, Günel M, Pamir MN. Expression of Structural Proteins and Angiogenic Factors in Normal Arterial and Unruptured and Ruptured Aneurysm Walls. Neurosurgery 2005, 57: 997-1007. PMID: 16284569, DOI: 10.1227/01.neu.0000180812.77621.6c.Peer-Reviewed Original ResearchConceptsStructural proteinsGrowth factorPattern of expressionCertain structural proteinsAngiogenic growth factorsLevel of expressionNormal vessel wallGrowth factor alpha expressionAngiogenic factorsProteinBiological mediatorsExpressionFibronectinVessel wallLamininNovel findingsIntracranial aneurysm formationPairs of specimensAneurysmal specimensTissue groupsFormationMediators
2002
KRIT1, a gene mutated in cerebral cavernous malformation, encodes a microtubule-associated protein
Gunel M, Laurans MS, Shin D, DiLuna ML, Voorhees J, Choate K, Nelson-Williams C, Lifton RP. KRIT1, a gene mutated in cerebral cavernous malformation, encodes a microtubule-associated protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 10677-10682. PMID: 12140362, PMCID: PMC125011, DOI: 10.1073/pnas.122354499.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAortaCattleCells, CulturedCentral Nervous System Vascular MalformationsChlorocebus aethiopsCOS CellsEndothelium, VascularGene ExpressionMicrotubule-Associated ProteinsMicrotubulesMitosisMolecular Sequence DataMutagenesisPrecipitin TestsProto-Oncogene ProteinsRadiographyTubulinConceptsCerebral cavernous malformationsCavernous malformationsCerebral cavernous malformation lesionsMicrotubule-associated proteinsProtein-1 alphaAutosomal dominant diseaseEndothelial tube formationCerebral hemorrhageCerebral capillariesEndothelial cellsDominant diseaseMalformationsTube formationPlus endsSite of cytokinesisSpindle pole bodyEvidence of interactionGene 1Possible roleCell-matrix interactionsKRIT1Late phaseEnds of microtubulesEndothelial cell shapePole body