2022
Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins
Putnam EE, Abellon-Ruiz J, Killinger BJ, Rosnow JJ, Wexler AG, Folta-Stogniew E, Wright AT, van den Berg B, Goodman AL. Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins. MBio 2022, 13: e02845-21. PMID: 35227073, PMCID: PMC8941943, DOI: 10.1128/mbio.02845-21.Peer-Reviewed Original ResearchConceptsComplex microbial communitiesHuman gut commensalTerminal globular domainModel organismsGut microbiomeMicrobial communitiesCompetitive fitnessTransport systemStructural homologsAccessory proteinsNew proteinsAdditional proteinsTransport proteinsGlobular domainUnknown functionMultiple transport systemsSystem lociKey roleGut commensalsProteinDiverse repertoireRelated moleculesMajor groupsFitnessOrganisms
2016
Secretion from Myeloid Cells: Secretory Lysosomes
Griffiths G. Secretion from Myeloid Cells: Secretory Lysosomes. Microbiology Spectrum 2016, 4: 10.1128/microbiolspec.mchd-0030-2016. PMID: 27726815, DOI: 10.1128/microbiolspec.mchd-0030-2016.Peer-Reviewed Original ResearchConceptsUnusual secretory organelleCell typesSpecialized cell typesSecretory lysosomesSecretory organellesAdditional proteinsAntimicrobial peptidesLysosomal compartmentMyeloid cellsCell lysisAzurophilic granulesEffector mechanismsLysosomesExtra proteinSpecialized functionsProteinCytotoxic T cellsMicrobial deathPlatelet von Willebrand factorTriggering inflammationCellsVon Willebrand factorDegradation functionEffectorMyeloid lineage
2012
Receptors and Other Signaling Proteins Required for Serotonin Control of Locomotion in Caenorhabditis elegans
Gürel G, Gustafson MA, Pepper JS, Horvitz HR, Koelle MR. Receptors and Other Signaling Proteins Required for Serotonin Control of Locomotion in Caenorhabditis elegans. Genetics 2012, 192: 1359-1371. PMID: 23023001, PMCID: PMC3512144, DOI: 10.1534/genetics.112.142125.Peer-Reviewed Original ResearchConceptsCaenorhabditis elegansLarge-scale genetic screensSer-4Direct postsynaptic targetsGenetic screenC. elegansSignaling proteinsGenetic systemNon-overlapping setsAdditional proteinsExtrasynaptic signalsMolecular mechanismsElegansSerotonin responseGenesRelease sitesMod 1Multiple receptorsProteinSerotonin controlSerotonergic neuronsPostsynaptic targetsSerotonin functionReceptorsSerotonin receptors
2010
The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells
Huranová M, Ivani I, Benda A, Poser I, Brody Y, Hof M, Shav-Tal Y, Neugebauer KM, Staněk D. The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells. Journal Of Cell Biology 2010, 191: 75-86. PMID: 20921136, PMCID: PMC2953428, DOI: 10.1083/jcb.201004030.Peer-Reviewed Original ResearchConceptsSmall nuclear RNP particlesPrecursor messenger RNA splicingMessenger RNA splicingBinding of U1Live-cell imagingRate of splicingNuclear RNP particlesLarge ribonucleoproteinSnRNP componentsRNA splicingSpliceosome assemblyAdditional proteinsRNP particlesHuman cellsSplicingLiving cellsCell nucleiDifferential interactionsEndogenous levelsSpliceosomeMRNARibonucleoproteinCell imagingCore componentCellsA fast, single-vesicle fusion assay mimics physiological SNARE requirements
Karatekin E, Di Giovanni J, Iborra C, Coleman J, O'Shaughnessy B, Seagar M, Rothman JE. A fast, single-vesicle fusion assay mimics physiological SNARE requirements. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 3517-3521. PMID: 20133592, PMCID: PMC2840481, DOI: 10.1073/pnas.0914723107.Peer-Reviewed Original Research
1995
Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex.
Rimm DL, Koslov ER, Kebriaei P, Cianci CD, Morrow JS. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 8813-8817. PMID: 7568023, PMCID: PMC41057, DOI: 10.1073/pnas.92.19.8813.Peer-Reviewed Original ResearchConceptsF-actinBundling proteinE-cadherin-mediated cell-cell contactsHomotypic cell-cell adhesionBundles F-actinEpithelial cell polarityCortical actin cytoskeletonCell-cell adhesionActin-binding proteinsFull-length proteinE-cadherinCell-cell contactMembrane adhesion complexesBundles actinCell polarityHierarchy of interactionsActin cytoskeletonAdhesion complexesCytoplasmic domainCosedimentation assaysSedimentation assaysAdditional proteinsMolecular basisActin filamentsActin complex
1993
Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins.
O'Brien C, Margelot K, Wolin S. Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7250-7254. PMID: 7688474, PMCID: PMC47114, DOI: 10.1073/pnas.90.15.7250.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinSmall ribonucleoproteinHuman Y RNAsSmall RNA moleculesXenopus egg extractsAmino acid sequenceY-RNAsHY3 RNAsVertebrate speciesMammalian cellsRo RNPsSubcellular locationRNA componentCytoplasmic ribonucleoproteinHY5 RNAAdditional proteinsRNA moleculesAcid sequenceHuman RNAEgg extractsEntire proteinConserved stemOocyte cytoplasmRibonucleoprotein
1988
[17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins
Lohmann S, De Camilli P, Walter U. [17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins. Methods In Enzymology 1988, 159: 183-193. PMID: 2842584, DOI: 10.1016/0076-6879(88)59019-5.Peer-Reviewed Original ResearchConceptsRII subunitsCytosolic cAMP-dependent protein kinaseAdditional proteinsType II cAMP-dependent proteinCAMP-dependent protein kinaseCAMP-dependent proteinMicrotubule-associated proteinsRII overlayProtein kinaseSDS-polyacrylamide gel electrophoresisCertain proteinsNative stateProteinSteps of purificationGel electrophoresisSubunitsCellular structureAssay conditionsNonspecific interactionsRIIHigh affinityHigh enough affinityLight microscopyKinaseAffinity
1985
A leader peptide is sufficient to direct mitochondrial import of a chimeric protein.
Horwich A, Kalousek F, Mellman I, Rosenberg L. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. The EMBO Journal 1985, 4: 1129-1135. PMID: 3891325, PMCID: PMC554314, DOI: 10.1002/j.1460-2075.1985.tb03750.x.Peer-Reviewed Original ResearchConceptsChimeric precursor proteinsMitochondrial importLeader peptideChimeric precursorsDihydrofolate reductaseMost mitochondrial proteinsPost-translational importMutant CHO cell linesCloned nucleotide sequencePrecursor proteinOrnithine transcarbamylaseCell-free systemCHO cell linesEnzyme dihydrofolate reductaseMitochondrial proteinsMitochondrial localizationRegulatory elementsLeader sequenceNucleotide sequenceStable transformantsAdditional proteinsSelectable markerChimeric proteinLarger precursorIntact cells
1983
Monoclonal antibodies specific for Leishmania tropica. I. Characterization of antigens associated with stage- and species-specific determinants.
Jaffe C, McMahon-Pratt D. Monoclonal antibodies specific for Leishmania tropica. I. Characterization of antigens associated with stage- and species-specific determinants. The Journal Of Immunology 1983, 131: 1987-93. PMID: 6194223, DOI: 10.4049/jimmunol.131.4.1987.Peer-Reviewed Original ResearchConceptsSpecies-specific determinantsPromastigote stageDifferent cell surface proteinsCell surface proteinsMonoclonal antibody bindsMembrane-enriched preparationsCell surface componentsL. tropica complexAdditional proteinsKilodalton proteinClone TTrypanosoma cruziSurface proteinsProteinMonoclonal antibodiesIntact promastigotesSurface componentsSolubilized 125IL. donovaniL. braziliensis braziliensisMajor promastigotesL. mexicana amazonensisPromastigotesI. CharacterizationCruzi
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