2009
RodZ, a component of the bacterial core morphogenic apparatus
Alyahya SA, Alexander R, Costa T, Henriques AO, Emonet T, Jacobs-Wagner C. RodZ, a component of the bacterial core morphogenic apparatus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 1239-1244. PMID: 19164570, PMCID: PMC2633561, DOI: 10.1073/pnas.0810794106.Peer-Reviewed Original ResearchConceptsCell morphogenesisExtracellular C-terminal domainBacterial cell morphogenesisConservation of functionTerminal cytoplasmic domainC-terminal domainN-terminal domainMultiple sequence alignmentMreB cytoskeletonBacterial kingdomAncient functionCaulobacter crescentusGrowth machineryLocalization determinantsHelix motifRodZTransmembrane sequenceBacterial phylaCytoplasmic domainGenomic analysisTerminal domainMolecular basisPeptidoglycan synthesisCellular formCell cycle
2008
The bovine papillomavirus E5 protein and the PDGF β receptor: It takes two to tango
Talbert-Slagle K, DiMaio D. The bovine papillomavirus E5 protein and the PDGF β receptor: It takes two to tango. Virology 2008, 384: 345-351. PMID: 18990418, PMCID: PMC2661243, DOI: 10.1016/j.virol.2008.09.033.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 proteinTransmembrane domainTransmembrane proteinTarget proteinsPlatelet-derived growth factor beta receptorArtificial transmembrane proteinsMembrane-spanning segmentsHuman erythropoietin receptorBPV E5 proteinGrowth factor beta receptorCellular receptor tyrosine kinasesLigand-independent activationReceptor tyrosine kinasesGenetic screenPDGF β-receptorNovel proteinTransmembrane sequenceCellular proteinsMitogenic signalingHydrophobic proteinsReceptor dimerizationLarger target proteinsErythropoietin receptorSmall proteins
1997
Molecular Mechanism of Membrane Protein Integration into the Endoplasmic Reticulum
Mothes W, Heinrich S, Graf R, Nilsson I, von Heijne G, Brunner J, Rapoport T. Molecular Mechanism of Membrane Protein Integration into the Endoplasmic Reticulum. Cell 1997, 89: 523-533. PMID: 9160744, DOI: 10.1016/s0092-8674(00)80234-2.Peer-Reviewed Original ResearchConceptsTranslocation channelCytosolic domainTransmembrane sequenceMembrane proteinsMolecular mechanismsEndoplasmic reticulumHydrophobic transmembrane sequenceMembrane protein integrationHydrophilic polypeptide segmentsProtein integrationLipid environmentPolypeptide segmentsProteinReticulumLipid phaseSequenceMembraneRibosomesCytosolFoldingDomainMechanismAssemblySignificant implicationsTranslation
1988
Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression
Kwon B, Wakulchik M, Haq A, Halaban R, Kestler D. Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression. Biochemical And Biophysical Research Communications 1988, 153: 1301-1309. PMID: 3134020, DOI: 10.1016/s0006-291x(88)81370-6.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAcid sequenceTyrosinase cDNAPotential N-glycosylation sitesMouse genomic cloneHistidine-rich regionMouse tyrosinase geneN-glycosylation sitesLevels of transcriptsCopper-binding siteMouse tyrosinase cDNADeduced proteinGenomic clonesTransmembrane sequenceHuman tyrosinase cDNACDNA clonesMouse tyrosinaseTyrosinase geneGene expressionSequence analysisAmino acidsHuman tyrosinaseClonesCDNAMelanoma cells
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply