2013
A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
Cabrero P, Richmond L, Nitabach M, Davies SA, Dow JA. A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells. Proceedings Of The Royal Society B 2013, 280: 20122943. PMID: 23446525, PMCID: PMC3619477, DOI: 10.1098/rspb.2012.2943.Peer-Reviewed Original ResearchMeSH KeywordsAequorinAnimalsApoproteinsCalcium SignalingChloridesDrosophila melanogasterDrosophila ProteinsGreen Fluorescent ProteinsInositol 1,4,5-Trisphosphate ReceptorsMalpighian TubulesModels, BiologicalNeuropeptidesPhospholipase C betaProtein EngineeringRecombinant ProteinsTyramineWater-Electrolyte BalanceConceptsTrisphosphate receptor geneCalcium signalsStellate cellsTranslational fusionInsect osmoregulationDistinct tissuesIntracellular calciumMode of actionPhospholipase CIntracellular calcium signalsReceptor geneIndependent mechanismsHalf-maximal activationTyramine-induced increaseUAS controlITPRTyramine actEndocrine controlRenal functionCellsNeuropeptides actPrincipal cellsKininsDrosophilaNorpA
2009
Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding
Sharma H, Yu S, Kong J, Wang J, Steitz TA. Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 16604-16609. PMID: 19805344, PMCID: PMC2745332, DOI: 10.1073/pnas.0908380106.Peer-Reviewed Original ResearchConceptsColi catabolite gene activator proteinEscherichia coli catabolite gene activator proteinCatabolite gene activator proteinC-helixConformational changesGene activator proteinDNA binding domainsDNA recognition helixEarlier biochemical dataLarge conformational changesSpecific DNA sequencesBinding of cAMPRecognition helixActivator proteinDNA sequencesDNA bindingBinding domainsActive DNAWT structureInactive formInactive structureBiochemical dataDifferent conformationsBindingConformation
2005
Crystal Structures of Proto-oncogene Kinase Pim1: A Target of Aberrant Somatic Hypermutations in Diffuse Large Cell Lymphoma
Kumar A, Mandiyan V, Suzuki Y, Zhang C, Rice J, Tsai J, Artis D, Ibrahim P, Bremer R. Crystal Structures of Proto-oncogene Kinase Pim1: A Target of Aberrant Somatic Hypermutations in Diffuse Large Cell Lymphoma. Journal Of Molecular Biology 2005, 348: 183-193. PMID: 15808862, DOI: 10.1016/j.jmb.2005.02.039.Peer-Reviewed Original ResearchMeSH KeywordsAdenylyl ImidodiphosphateAmino Acid SequenceApoproteinsCrystallography, X-RayHumansLymphoma, Large B-Cell, DiffuseModels, MolecularMolecular Sequence DataMutationProtein BindingProtein ConformationProtein Serine-Threonine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-pim-1Sequence AlignmentConceptsKinase activitySerine/threonine kinaseAberrant somatic hypermutationSomatic hypermutationKinase inhibitor scaffoldN-terminal lobePim1 mutantsTypical kinasesCo-crystal structureThreonine kinaseProtein kinaseBackbone hydrogen bondsKinase PIM1Apo formBiological functionsProline residuesPIM1 inhibitorsNovel chemical classUnique structural featuresLow molecular massInhibitor scaffoldsCell survivalMolecular massPosition 123PIM1
1997
In situ expression of PLP/DM‐20, MBP, and CNP during embryonic and postnatal development of the jimpy mutant and of transgenic mice overexpressing PLP
Peyron F, Timsit S, Thomas J, Kagawa T, Ikenaka K, Zalc B. In situ expression of PLP/DM‐20, MBP, and CNP during embryonic and postnatal development of the jimpy mutant and of transgenic mice overexpressing PLP. Journal Of Neuroscience Research 1997, 50: 190-201. PMID: 9373029, DOI: 10.1002/(sici)1097-4547(19971015)50:2<190::aid-jnr8>3.0.co;2-a.Peer-Reviewed Original ResearchConceptsPLP/DMCyclic nucleotide phosphodiesteraseDM-20PLP geneMyelin basic proteinDM-20 mRNAPattern of expressionEmbryonic developmentLevel of expressionJimpy mutantPeripheral nervous systemTransgenic micePrecursors of oligodendrocytesSpatiotemporal expressionDistinct poolsNeural tubeCentral nervous system
1996
Antigen‐specific TGF‐β1 Secretion with Bovine Myelin Oral Tolerization in Multiple Sclerosis
FUKAURA H, KENT S, PIETRUSEWICZ M, KHOURY S, WEINER H, HAFLER D. Antigen‐specific TGF‐β1 Secretion with Bovine Myelin Oral Tolerization in Multiple Sclerosis. Annals Of The New York Academy Of Sciences 1996, 778: 251-257. PMID: 8610978, DOI: 10.1111/j.1749-6632.1996.tb21133.x.Peer-Reviewed Original ResearchConceptsRelapsing-remitting MS patientsHuman autoimmune diseasesOral tolerizationMultiple sclerosisAutoimmune diseasesT cell linesMS patientsCytokine secretionT cellsAutoreactive T-cell populationsAutoreactive T cellsT cell populationsT-cell fractionCNS white matterFed patientsIL-4Inflammatory responseΒ1 secretionIFN-gammaTolerizationWhite matterPatientsSclerosisBovine myelinSecretion
1990
T-cell recognition of an immuno-dominant myelin basic protein epitope in multiple sclerosis
Ota K, Matsui M, Milford E, Mackin G, Weiner H, Hafler D. T-cell recognition of an immuno-dominant myelin basic protein epitope in multiple sclerosis. Nature 1990, 346: 183-187. PMID: 1694970, DOI: 10.1038/346183a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigen-Presenting CellsApoproteinsAutoantigensCells, CulturedEpitopesHLA-DR AntigensHumansIn Vitro TechniquesMajor Histocompatibility ComplexMolecular Sequence DataMultiple SclerosisMyelin Basic ProteinMyelin ProteinsMyelin Proteolipid ProteinPeptide FragmentsT-LymphocytesConceptsMultiple sclerosis patientsT cell linesMyelin basic proteinMultiple sclerosisSclerosis patientsT cellsVivo-activated T cellsShort-term T cell linesMyelin basic protein epitopeBasic proteinExperimental autoimmune encephalomyelitisDifferent T-cell linesCentral nervous systemMultiple sclerosis subjectsT cell recognitionT cell specificityAutoimmune encephalomyelitisImmune involvementAutoimmune diseasesPotential autoantigensNormal controlsNervous systemNeurological diseasesSclerosisPatientsA novel function for zinc(II) in a nucleic acid-binding protein. Contribution of zinc(II) toward the cooperativity of bacteriophage T4 gene 32 protein binding.
Nadler S, Roberts W, Shamoo Y, Williams K. A novel function for zinc(II) in a nucleic acid-binding protein. Contribution of zinc(II) toward the cooperativity of bacteriophage T4 gene 32 protein binding. Journal Of Biological Chemistry 1990, 265: 10389-10394. PMID: 2113053, DOI: 10.1016/s0021-9258(18)86958-7.Peer-Reviewed Original Research
1987
The function of zinc in gene 32 protein from T4.
Giedroc D, Keating K, Williams K, Coleman J. The function of zinc in gene 32 protein from T4. Biochemistry 1987, 26: 5251-9. PMID: 3314985, DOI: 10.1021/bi00391a007.Peer-Reviewed Original Research
1973
Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins Carboxymethylated with Enriched [2-13C]Bromoacetate
Nigen A, Keim P, Marshall R, Morrow J, Vigna R, Gurd F. Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins Carboxymethylated with Enriched [2-13C]Bromoacetate. Journal Of Biological Chemistry 1973, 248: 3724-3732. PMID: 4735715, DOI: 10.1016/s0021-9258(19)43986-0.Peer-Reviewed Original Research
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