2007
LRRTM1 on chromosome 2p12 is a maternally suppressed gene that is associated paternally with handedness and schizophrenia
Francks C, Maegawa S, Laurén J, Abrahams BS, Velayos-Baeza A, Medland SE, Colella S, Groszer M, McAuley EZ, Caffrey TM, Timmusk T, Pruunsild P, Koppel I, Lind PA, Matsumoto-Itaba N, Nicod J, Xiong L, Joober R, Enard W, Krinsky B, Nanba E, Richardson AJ, Riley BP, Martin NG, Strittmatter SM, Möller HJ, Rujescu D, St Clair D, Muglia P, Roos JL, Fisher SE, Wade-Martins R, Rouleau GA, Stein JF, Karayiorgou M, Geschwind DH, Ragoussis J, Kendler KS, Airaksinen MS, Oshimura M, DeLisi LE, Monaco AP. LRRTM1 on chromosome 2p12 is a maternally suppressed gene that is associated paternally with handedness and schizophrenia. Molecular Psychiatry 2007, 12: 1129-1139. PMID: 17667961, PMCID: PMC2990633, DOI: 10.1038/sj.mp.4002053.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCell Line, TransformedChromosomes, Human, Pair 2Family HealthFemaleFunctional LateralityGene Expression Regulation, DevelopmentalGenetic Predisposition to DiseaseGenotypeHumansIn Situ HybridizationKaryotypingMaleMembrane ProteinsMiceNerve Tissue ProteinsSchizophreniaSubcellular FractionsConceptsHuman brain asymmetryPutative genetic effectsEvolutionary originImprinted genesChromosome 2p12Candidate genesBehavioral evolutionHuman handednessNeuronal differentiationBrain asymmetryLRRTM1Specific forebrain structuresSchizophrenia/schizoaffective disorderGenetic effectsGenesSame haplotypePotential genetic influencesDirect confirmatory evidenceCommon neurodevelopmental disorderFunction underliesForebrain structuresSchizoaffective disorderHaplotypesSignificant associationNeuropsychiatric disordersThe CRMP Family of Proteins and Their Role in Sema3A Signaling
Schmidt EF, Strittmatter SM. The CRMP Family of Proteins and Their Role in Sema3A Signaling. Advances In Experimental Medicine And Biology 2007, 600: 1-11. PMID: 17607942, PMCID: PMC2853248, DOI: 10.1007/978-0-387-70956-7_1.Peer-Reviewed Original ResearchConceptsMonomeric G proteinsLarge intracellular domainNeuropilin-1Class A plexinsRepulsive axon guidance cuesCurrent knowledgeSema3A signalingVertebrate semaphorinsAxon guidance cuesCellular processesSignal transductionBinding partnerIntracellular domainMediator proteinsProtein turnoverCRMP proteinsF-actinCellular responsesCytosolic phosphoproteinG proteinsNeuronal differentiationRedox proteinsReceptor complexCellular effectsCell membrane
2003
Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling
Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. Structural bases for CRMP function in plexin‐dependent semaphorin3A signaling. The EMBO Journal 2003, 23: 9-22. PMID: 14685275, PMCID: PMC1271659, DOI: 10.1038/sj.emboj.7600021.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsCell Adhesion MoleculesCell LineChick EmbryoChlorocebus aethiopsCOS CellsCrystallography, X-RayGanglia, SpinalHumansHydrogen BondingImmunophilinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphoproteinsProtein Structure, SecondaryProtein Structure, TertiaryReceptors, Cell SurfaceRecombinant Fusion ProteinsSemaphorin-3ASequence Homology, Amino AcidSignal TransductionStructure-Activity RelationshipConceptsCollapsin response mediator proteinsStructure-based mutagenesisCOS-7 cellsSurface-exposed residuesTetrameric assemblyPhysical complexAxonal specificationMediator proteinsStructural basisFunctional domainsAlanine substitutionsActive proteinCytosolic phosphoproteinNeuronal differentiationAxonal repulsionAxonal guidanceReceptor componentsProteinStructural viewX-ray crystal structureCRMP1Sema3ACell contractionCellsNP1