2017
Use of a Targeted Urine Proteome Assay (TUPA) to identify protein biomarkers of delayed recovery after kidney transplant
Williams KR, Colangelo CM, Hou L, Chung L, Belcher JM, Abbott T, Hall IE, Zhao H, Cantley LG, Parikh CR. Use of a Targeted Urine Proteome Assay (TUPA) to identify protein biomarkers of delayed recovery after kidney transplant. Proteomics Clinical Applications 2017, 11 PMID: 28261998, PMCID: PMC5549272, DOI: 10.1002/prca.201600132.Peer-Reviewed Original ResearchMeSH KeywordsBiomarkersDelayed Graft FunctionGene Expression RegulationHumansKidney TransplantationProteomicsUrinalysisConceptsImmediate graft functionKidney transplantGraft functionLong-term graft outcomeMore effective treatmentsProtein biomarkersIGF patientsGraft outcomeIGF levelsPoor outcomeEffective treatmentKidney implantationClinical relevanceBiomarker panelPotential biomarkersUrine proteomeDGFTransplantBiomarkersPatientsOutcomesTreatmentEarly stagesAssaysPrognosis
1989
Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions.
Shamoo Y, Ghosaini L, Keating K, Williams K, Sturtevant J, Konigsberg W. Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions. Biochemistry 1989, 28: 7409-17. PMID: 2684276, DOI: 10.1021/bi00444a039.Peer-Reviewed Original ResearchMeSH KeywordsCalorimetry, Differential ScanningCircular DichroismDNA, Single-StrandedDNA, ViralDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliGene Expression RegulationGenes, ViralMutationNucleic Acid DenaturationPoly dA-dTPoly TProtein DenaturationTemperatureThermodynamicsT-PhagesTrypsinTyrosineViral ProteinsZincThe 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis
Rush J, Lin T, Quinones M, Spicer E, Douglas I, Williams K, Konigsberg W. The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis. Journal Of Biological Chemistry 1989, 264: 10943-10953. PMID: 2786875, DOI: 10.1016/s0021-9258(18)60410-7.Peer-Reviewed Original ResearchConceptsAccessory proteinsATP hydrolysisDNA-dependent ATP hydrolysisT4 DNA polymerase accessory proteinsDNA polymerase accessory proteinPolymerase accessory proteinsTotal cellular proteinAccessory protein complexProtein complexesCellular proteinsPlasmid resultsSubunitsProteinATPase activityOverexpression plasmidProductive interactionInduction of cellsPlasmidSpecific activityComplexesSubcomplexInductionGenesOverexpressionATPase
1986
Cloning of T4 gene 32 and expression of the wild-type protein under lambda promoter PL regulation in Escherichia coli.
Shamoo Y, Adari H, Konigsberg W, Williams K, Chase J. Cloning of T4 gene 32 and expression of the wild-type protein under lambda promoter PL regulation in Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8844-8848. PMID: 2947239, PMCID: PMC387029, DOI: 10.1073/pnas.83.23.8844.Peer-Reviewed Original ResearchConceptsGene 32T4 gene 32Bacteriophage T4 gene 32T4 DNA replicationWild-type proteinWild-type geneHost cell viabilityTranslational regulationCodon TAGDNA replicationNative promoterPromoter PLAutoregulatory regionRich sequencesRestriction fragmentsEscherichia coliTranscriptsCell viabilityProteinRegulationSynthetic oligodeoxynucleotidesDeleterious effectsCloningMutagenesisG32P
1984
Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation.
Williams K, Murphy J, Chase J. Characterization of the structural and functional defect in the Escherichia coli single-stranded DNA binding protein encoded by the ssb-1 mutant gene. Expression of the ssb-1 gene under lambda pL regulation. Journal Of Biological Chemistry 1984, 259: 11804-11811. PMID: 6384214, DOI: 10.1016/s0021-9258(20)71283-4.Peer-Reviewed Original ResearchConceptsWild-type SSBMutant proteinsSSB-1Solid-phase protein sequencingSsb-1 mutationSSB-1 proteinHelix-destabilizing proteinNormal cellular concentrationTryptic peptide analysisSubstitution of tyrosineSingle-strand DNAProtein sequencingDNA sequencesMutant geneResidues 55Thermal melting transitionCellular concentrationTemperature inductionTetrameric structureEscherichia coliProteinGenesProtein concentrationPeptide analysisT transition