2016
Inhibition of Poly-ADP-Ribosylation Fails to Increase Axonal Regeneration or Improve Functional Recovery after Adult Mammalian CNS Injury
Wang X, Sekine Y, Byrne AB, Cafferty WB, Hammarlund M, Strittmatter SM. Inhibition of Poly-ADP-Ribosylation Fails to Increase Axonal Regeneration or Improve Functional Recovery after Adult Mammalian CNS Injury. ENeuro 2016, 3: eneuro.0270-16.2016. PMID: 28032120, PMCID: PMC5187389, DOI: 10.1523/eneuro.0270-16.2016.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAxonsBenzimidazolesCells, CulturedCerebral CortexDisease Models, AnimalFemaleIsoenzymesMaleMice, 129 StrainMice, Inbred C57BLMice, TransgenicMotor ActivityNerve RegenerationOptic Nerve InjuriesPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsRecovery of FunctionSpinal Cord InjuriesThoracic VertebraeConceptsOptic nerve crush injuryNerve crush injuryThoracic spinal cordAxonal regenerationSpinal cordDorsal hemisectionCrush injuryFunctional recoveryPARP inhibitorsMotor function recoveryRecovery of functionPoly (ADP-ribose) polymeraseClinical PARP inhibitorsNeurological recoveryShort hairpin RNACNS traumaCNS injuryFunction recoveryAxonal regrowthSystemic administrationPharmacodynamic actionAxon regenerationTraumatic damageTherapeutic efficacyNeurological trauma
1987
Angiotensin converting enzyme immunohistochemistry in rat brain and pituitary gland: Correlation of isozyme type with cellular localization
Strittmatter SM, Snyder SH. Angiotensin converting enzyme immunohistochemistry in rat brain and pituitary gland: Correlation of isozyme type with cellular localization. Neuroscience 1987, 21: 407-420. PMID: 3039401, DOI: 10.1016/0306-4522(87)90131-x.Peer-Reviewed Original ResearchConceptsAngiotensin converting enzymeSubstantia nigraRat brainChoroid plexusPituitary glandPosterior pituitaryConverting enzymePituitary stalk sectionEntopeduncular nucleusSubfornical organCaudate putamenGlobus pallidusEnzyme immunoreactivityParaventricular nucleusAnterior pituitaryAngiotensinEnzyme inhibitorsPosterior lobeIntense stainingCell bodiesMonoclonal antibodiesDiffuse stainingEndothelial cellsEnzyme immunohistochemistryAntibody specificity
1985
Angiotensin-Converting Enzyme in the Testis and Epididymis: Differential Development and Pituitary Regulation of Isozymes*
STRITTMATTER S, THIELE E, DE SOUZA E, SNYDER S. Angiotensin-Converting Enzyme in the Testis and Epididymis: Differential Development and Pituitary Regulation of Isozymes*. Endocrinology 1985, 117: 1374-1379. PMID: 2992911, DOI: 10.1210/endo-117-4-1374.Peer-Reviewed Original ResearchA 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 Research