2014
Automated Objective Determination of Percentage of Malignant Nuclei for Mutation Testing
Viray H, Coulter M, Li K, Lane K, Madan A, Mitchell K, Schalper K, Hoyt C, Rimm DL. Automated Objective Determination of Percentage of Malignant Nuclei for Mutation Testing. Applied Immunohistochemistry & Molecular Morphology 2014, 22: 363-371. PMID: 24162261, PMCID: PMC3999345, DOI: 10.1097/pai.0b013e318299a1f6.Peer-Reviewed Original ResearchConceptsCriterion standardMalignant cellsMalignant nucleiCompanion diagnostic testsTumor cell percentageMutation testingEosin-stained tissuesCell percentageInForm softwareHistologic specimensTumor tissueColon adenocarcinomaTumor cellsDiagnostic testsPotential future toolDNA mutation testingTissue sectionsContinuous variablesFurther validationPathologist estimationAnalytic sensitivityVariant resultsDNA mutationsBenign nucleiTissue
1991
Analysis of cDNA clones for Acanthamoeba profilin‐I and profilin‐II shows end to end homology with vertebrate profilins and a small family of profilin genes
Pollard T, Rimm D. Analysis of cDNA clones for Acanthamoeba profilin‐I and profilin‐II shows end to end homology with vertebrate profilins and a small family of profilin genes. Cytoskeleton 1991, 20: 169-177. PMID: 1751969, DOI: 10.1002/cm.970200209.Peer-Reviewed Original ResearchConceptsProfilin IIDNA sequencesProtein sequencesAcanthamoeba profilinGenomic DNA fragmentsFull-length cDNAFamily of proteinsProfilin geneAncestral precursorDifferent phylaInvariant residuesAdditional genesCDNA clonesLength cDNAConservative substitutionsPairwise identityDNA fragmentsSouthern blotNorthern blotGenesProfilinAmino acidsSmall familyCDNAConsiderable divergence
1990
Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites.
Rimm DL, Kaiser DA, Bhandari D, Maupin P, Kiehart DP, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites. Journal Of Cell Biology 1990, 111: 2405-2416. PMID: 1703536, PMCID: PMC2116414, DOI: 10.1083/jcb.111.6.2405.Peer-Reviewed Original Research
1989
Purification and characterization of an Acanthamoeba nuclear actin-binding protein.
Rimm DL, Pollard TD. Purification and characterization of an Acanthamoeba nuclear actin-binding protein. Journal Of Cell Biology 1989, 109: 585-591. PMID: 2760108, PMCID: PMC2115709, DOI: 10.1083/jcb.109.2.585.Peer-Reviewed Original ResearchConceptsActin-binding proteinsMyosin ITwo-dimensional peptide mapsAcanthamoeba myosin ICell fractionationATP-insensitive mannerCross-reactive proteinNuclear localizationAffinity-purified antibodiesAbsence of actinMyosin I.Actin filamentsProteinPeptide mapsMonoclonal antibodiesATPase activityPolyclonal antiserumProteolytic productsStokes radiusPolyclonal antibodiesCross-reactive monoclonal antibodiesColumn chromatographyPolypeptideActinDNALocation 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 antibodiesPolypeptide