2007
The reticulons: a family of proteins with diverse functions
Yang YS, Strittmatter SM. The reticulons: a family of proteins with diverse functions. Genome Biology 2007, 8: 234. PMID: 18177508, PMCID: PMC2246256, DOI: 10.1186/gb-2007-8-12-234.Peer-Reviewed Original ResearchConceptsDiverse functionsEndoplasmic reticulum-Golgi traffickingReticulon homology domainMembrane-associated proteinsAmino-terminal domainFamily of proteinsEukaryotic kingdomsMembrane morphogenesisHomology domainHydrophilic loopReticulon 4Reticulon familyReticulonsDiversity of structuresExpression patternsVesicle formationEndoplasmic reticulumAmino acidsCell surfaceHydrophobic regionAxon growthDiverse groupNeurodegenerative diseasesProteinAmyotrophic lateral sclerosis
2006
Rtn1p Is Involved in Structuring the Cortical Endoplasmic Reticulum
De Craene J, Coleman J, Estrada de Martin P, Pypaert M, Anderson S, Yates J, Ferro-Novick S, Novick P. Rtn1p Is Involved in Structuring the Cortical Endoplasmic Reticulum. Molecular Biology Of The Cell 2006, 17: 3009-3020. PMID: 16624861, PMCID: PMC1483037, DOI: 10.1091/mbc.e06-01-0080.Peer-Reviewed Original ResearchConceptsCortical endoplasmic reticulumEndoplasmic reticulumNuclear envelopeCortical ER networkReticular endoplasmic reticulumMembrane-spanning domainsExocyst functionYeast mutantsProtein associatesBud tipProteomic screenYeast budER morphologyCell cortexHydrophilic loopSystematic screenSecretory vesiclesRtn1pER structureER networkExocystProteinModest accumulationReticulumOverexpression
2000
Physical and genetic interaction of filamin with presenilin in Drosophila
Guo Y, Zhang S, Sokol N, Cooley L, Boulianne G. Physical and genetic interaction of filamin with presenilin in Drosophila. Journal Of Cell Science 2000, 113: 3499-3508. PMID: 10984440, DOI: 10.1242/jcs.113.19.3499.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAlzheimer DiseaseAmino Acid SequenceAnimalsBlotting, WesternCarrier ProteinsCloning, MolecularContractile ProteinsDrosophila melanogasterEmbryo, NonmammalianFemaleFilaminsGene Expression Regulation, DevelopmentalHumansInsect ProteinsLarvaMaleMembrane ProteinsMicrofilament ProteinsMolecular Sequence DataPresenilin-1Presenilin-2Protein BindingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTwo-Hybrid System TechniquesConceptsN-terminal actin-binding domainOverall amino acid identityOverexpression of presenilinFamilial Alzheimer's diseaseTransmembrane domain proteinActin-binding domainAmino acid identityLarge hydrophilic loopDrosophila filaminDomain proteinsGenetic interactionsAlternative splicingHydrophilic loopAcid identityTerminal domainDrosophilaHuman filaminChromosome 3Spliced formsFilaminAdult phenotypeLoop regionPresenilinNovel familyLong form
1994
Membrane topology of the epithelial sodium channel in intact cells
Canessa C, Merillat A, Rossier B. Membrane topology of the epithelial sodium channel in intact cells. American Journal Of Physiology 1994, 267: c1682-c1690. PMID: 7810611, DOI: 10.1152/ajpcell.1994.267.6.c1682.Peer-Reviewed Original ResearchConceptsLarge hydrophilic loopHydrophilic loopIntact cellsMembrane topologyEpithelial sodium channelPutative transmembrane domainsStop-transfer signalAmiloride-sensitive epithelial sodium channelCell-free translation assaysShort NH2Transmembrane domainMembrane insertionHomologous subunitsXenopus laevis oocytesTranslation assaysSodium channelsGlycosylation sitesCOOH terminusCytoplasmic sideFunctional expressionTerminal endSubunitsHydrophilic NH2Laevis oocytesAlpha-rENaC
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