2013
In Vitro and In Vivo Comparison of Two Suprachoroidal ShuntsComparison of Two Suprachoroidal Shunts
Oatts JT, Zhang Z, Tseng H, Shields MB, Sinard JH, Loewen NA. In Vitro and In Vivo Comparison of Two Suprachoroidal ShuntsComparison of Two Suprachoroidal Shunts. Investigative Ophthalmology & Visual Science 2013, 54: 5416-5423. PMID: 23847318, PMCID: PMC4141703, DOI: 10.1167/iovs.13-11853.Peer-Reviewed Original Research
2009
Factor VII–Verteporfin for Targeted Photodynamic Therapy in a Rat Model of Choroidal Neovascularization
Lu F, Hu Z, Sinard J, Garen A, Adelman RA. Factor VII–Verteporfin for Targeted Photodynamic Therapy in a Rat Model of Choroidal Neovascularization. Investigative Ophthalmology & Visual Science 2009, 50: 3890-3896. PMID: 19357351, DOI: 10.1167/iovs.08-2833.Peer-Reviewed Original ResearchConceptsVisudyne photodynamic therapyChoroidal neovascularizationCNV lesionsTargeted photodynamic therapyDay 7Rat modelSafety of PDTPhotodynamic therapyOcular side effectsBrown Norway ratsFrequency of leakageFluorescein angiographyEfficacious doseHistopathologic evaluationLaser photocoagulationSide effectsFactor VIIDay 14LesionsNormal vasculatureRatsEndothelial cellsTherapyDoseNeovascularization
1990
Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions.
Sinard JH, Rimm DL, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. Journal Of Cell Biology 1990, 111: 2417-2426. PMID: 2177477, PMCID: PMC2116375, DOI: 10.1083/jcb.111.6.2417.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaAnimalsBase SequenceBinding SitesChromatographyChromatography, DEAE-CelluloseChromatography, GelChromosome DeletionCloning, MolecularDurapatiteElectrophoresis, Polyacrylamide GelEscherichia coliHydroxyapatitesKineticsMacromolecular SubstancesMagnesiumMicroscopy, ElectronMolecular Sequence DataMolecular WeightMyosinsPotassium ChlorideRecombinant Fusion ProteinsScattering, RadiationConceptsFusion proteinMyosin IIMyosin-II tailAntiparallel tetramersAmino acidsAmino acid residuesNative myosin IIRecombinant fusion proteinSequence altersAcid residuesTail sequencesNH2-terminalNonhelical domainAcanthamoeba myosin IIFunctional regionsProteinParacrystal formationAntiparallel dimerAssembly propertiesDimerization mechanismResiduesTerminal deletionDeletionAssemblyTight packingA Stopped‐flow/rapid‐freezing machine with millisecond time resolution to prepare intermediates in biochemical reactions for electron microscopy
Pollard T, Maupin P, Sinard J, Huxley H. A Stopped‐flow/rapid‐freezing machine with millisecond time resolution to prepare intermediates in biochemical reactions for electron microscopy. Microscopy Research And Technique 1990, 16: 160-166. PMID: 2213238, DOI: 10.1002/jemt.1060160206.Peer-Reviewed Original ResearchAcanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction.
Sinard JH, Pollard TD. Acanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction. Journal Of Biological Chemistry 1990, 265: 3654-3660. PMID: 2303471, DOI: 10.1016/s0021-9258(19)39643-7.Peer-Reviewed Original Research
1989
The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II.
Sinard JH, Pollard TD. The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II. Journal Of Cell Biology 1989, 109: 1529-1535. PMID: 2793932, PMCID: PMC2115825, DOI: 10.1083/jcb.109.4.1529.Peer-Reviewed Original ResearchConceptsLateral aggregationLow ionic strengthSolution conditionsCritical concentrationIonic strengthLight scatteringMillimolar concentrationsAssembly propertiesAcidic pHExtent of assemblyMoleculesLower tendencyAssemblyMyosin II minifilamentsIonic conditionsPolymerizationMonomersMgCl2AggregationConcentrationMinifilamentsHigh concentrationsFurther modulationPolymerizesThe mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps.
Sinard JH, Stafford WF, Pollard TD. The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps. Journal Of Cell Biology 1989, 109: 1537-1547. PMID: 2793933, PMCID: PMC2115822, DOI: 10.1083/jcb.109.4.1537.Peer-Reviewed Original ResearchLocation of the head-tail junction of myosin.
Rimm DL, Sinard JH, Pollard TD. Location of the head-tail junction of myosin. Journal Of Cell Biology 1989, 108: 1783-1789. PMID: 2715178, PMCID: PMC2115540, DOI: 10.1083/jcb.108.5.1783.Peer-Reviewed Original ResearchConceptsMyosin IIHeptad repeatAcanthamoeba myosin IIHead-tail junctionCoiled-coil structureHydrophobic amino acidsNative myosin IIIdentical polypeptidesNH2 terminusMyosin-II tailNonmuscle myosinProteolytic separationLines of evidenceShort tailAmino acidsPosition 847RepeatsMyosinResiduesTailMyosin moleculesHeptadTerminusMonoclonal antibodiesPolypeptideMicroinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin‐II slows but does not stop cell locomotion
Sinard J, Pollard T. Microinjection into Acanthamoeba castellanii of monoclonal antibodies to myosin‐II slows but does not stop cell locomotion. Cytoskeleton 1989, 12: 42-52. PMID: 2523248, DOI: 10.1002/cm.970120106.Peer-Reviewed Original Research
1986
Characterization of alpha‐actinin from Acanthamoeba
Pollard T, Tseng P, Rimm D, Bichell D, Williams R, Sinard J, Sato M. Characterization of alpha‐actinin from Acanthamoeba. Cytoskeleton 1986, 6: 649-661. PMID: 2948678, DOI: 10.1002/cm.970060613.Peer-Reviewed Original ResearchConceptsCross-linking proteinsActin filamentsActin filament cross-linking proteinCross-link actin filamentsCross-links actin filamentsAmino acid compositionAmoeba proteinApparent molecular weightActin polymerizationGlobular domainElectrophoretic variantsNative proteinCell extractsActin monomersPure proteinProteinGel electrophoresisAmoebaeCytoplasmic matrixStokes radiusMolecular weightPolypeptideAcid compositionIndirect fluorescent antibody stainingAntibody staining