2011
Differential but Competitive Binding of Nogo Protein and Class I Major Histocompatibility Complex (MHCI) to the PIR-B Ectodomain Provides an Inhibition of Cells*
Matsushita H, Endo S, Kobayashi E, Sakamoto Y, Kobayashi K, Kitaguchi K, Kuroki K, Söderhäll A, Maenaka K, Nakamura A, Strittmatter SM, Takai T. Differential but Competitive Binding of Nogo Protein and Class I Major Histocompatibility Complex (MHCI) to the PIR-B Ectodomain Provides an Inhibition of Cells*. Journal Of Biological Chemistry 2011, 286: 25739-25747. PMID: 21636572, PMCID: PMC3138294, DOI: 10.1074/jbc.m110.157859.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta 2-MicroglobulinBinding, CompetitiveFemaleHistocompatibility Antigens Class IHLA AntigensHLA-G AntigensHumansImmunologic FactorsInterleukin-6LipopolysaccharidesMast CellsMiceMice, Inbred C57BLMyelin ProteinsMyelin-Associated GlycoproteinNeurotransmitter AgentsNogo ProteinsProtein Structure, TertiaryRatsReceptors, ImmunologicSubstrate SpecificityConceptsMajor histocompatibility complexRecent unexpected findingsClass I major histocompatibility complexI major histocompatibility complexInterleukin-6 releaseClass I MHC moleculesC-terminal ectodomainNovel inhibitory roleCultured mast cellsI MHC moleculesTerminal domainPeripheral toleranceInhibitory receptorsInhibition of cellMast cellsOutgrowth inhibitorB cellsMyeloid cellsImmune systemMHC moleculesNeurite regenerationNovel mechanismNogo proteinEctodomainInhibitory role
1988
Characterization of a neutral, divalent cation-sensitive endopeptidase: a possible role in neuropeptide processing.
Supattapone S, Strittmatter SM, Fricker LD, Snyder SH. Characterization of a neutral, divalent cation-sensitive endopeptidase: a possible role in neuropeptide processing. Brain Research 1988, 427: 173-81. PMID: 3382941, DOI: 10.1016/0169-328x(88)90063-0.Peer-Reviewed Original ResearchConceptsCorpus striatumBrain regionsTissue distributionBovine adrenal chromaffin granulesAdrenal chromaffin granulesHomogeneous tissue distributionPossible roleNeuropeptide processingDensity gradient fractionationSucrose density gradient fractionationEndopeptidaseLeu-ArgChromaffin granulesHigh levelsBasic amino acidsTrypsin-like endopeptidaseEnzyme activityHippocampusStriatum
1985
A rat brain isozyme of angiotensin-converting enzyme. Unique specificity for amidated peptide substrates.
Strittmatter SM, Thiele EA, Kapiloff MS, Snyder SH. A rat brain isozyme of angiotensin-converting enzyme. Unique specificity for amidated peptide substrates. Journal Of Biological Chemistry 1985, 260: 9825-9832. PMID: 2991265, DOI: 10.1016/s0021-9258(17)39310-9.Peer-Reviewed Original ResearchConceptsBrain ACESubstance PLung ACERat brain corpus striatumSubstance KMet-NH2Substance P 5Hormone-releasing hormoneLung enzymeThyrotropin-releasing hormoneAngiotensin-converting enzymeSubstance P 1Striatonigral pathwayCorpus striatumRat lungAmidated peptidesLungStriatal enzymeACE isozymeGly-LeuBrain enzymeBrain isozymeSimilar extentImmunological propertiesACESubstance K and substance P as possible endogenous substrates of angiotensin converting enzyme in the brain
Thiele E, Strittmatter S, Snyder S. Substance K and substance P as possible endogenous substrates of angiotensin converting enzyme in the brain. Biochemical And Biophysical Research Communications 1985, 128: 317-324. PMID: 2580530, DOI: 10.1016/0006-291x(85)91681-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainIsoenzymesLungModels, ChemicalNerve Tissue ProteinsNeurokinin APeptidyl-Dipeptidase ASubstance PSubstrate Specificity
1984
A fluorometric assay for angiotensin-converting enzyme activity
Kapiloff M, Strittmatter S, Fricker L, Snyder S. A fluorometric assay for angiotensin-converting enzyme activity. Analytical Biochemistry 1984, 140: 293-302. PMID: 6091493, DOI: 10.1016/0003-2697(84)90167-2.Peer-Reviewed Original Research