1998
Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis
Stone K, Deangelis R, LoPresti M, Jones J, Papov V, Williams K. Use of liquid chromatography‐electrospray ionization‐tandem mass spectrometry (LC‐ESI‐MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. Electrophoresis 1998, 19: 1046-1052. PMID: 9638951, DOI: 10.1002/elps.1150190620.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate-polyacrylamide gel electrophoresisQuadrupole ion trap mass spectrometerIon trap mass spectrometerDodecyl sulfate-polyacrylamide gel electrophoresisLow pmol levelSulfate-polyacrylamide gel electrophoresisIonization tandem mass spectrometryTrap mass spectrometerLiquid chromatography-electrospray ionization-tandem mass spectrometryLiquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) analysisMS/MS approachProtein identificationIonization tandem mass spectrometry analysisFmol levelFacile approachMass spectrometry analysisMass spectrometerEng et alMass spectrometryPmol levelLC-MS/MS approachTryptic digestMS approachSpectrometry analysisGel electrophoresis
1989
Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles
Merrill B, Barnett S, LeStourgeon W, Williams K. Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Research 1989, 17: 8441-8449. PMID: 2587210, PMCID: PMC335017, DOI: 10.1093/nar/17.21.8441.Peer-Reviewed Original ResearchConceptsInsert sequenceHeterogeneous nuclear ribonucleoprotein particleSingle transcription unitAlternative splicing mechanismNuclear ribonucleoprotein particleAmino acid sequencingResidue insertHnRNP proteinsTranscription unitTryptic peptide mappingSplicing mechanismPrimary structure differencesC2 proteinSDS-polyacrylamide gel electrophoresisNuclear ribonucleoproteinProtein C1Ribonucleoprotein particleUntranslated regionPrimary structurePolyacrylamide gel electrophoresisAmino acidsPeptide mappingGel electrophoresisMolecular weight differencesProteinThe 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
Acidic lipids enhance cathepsin D cleavage of the myelin basic protein
Williams K, Williams N, Konigsberg W, Yu R. Acidic lipids enhance cathepsin D cleavage of the myelin basic protein. Journal Of Neuroscience Research 1986, 15: 137-145. PMID: 2421004, DOI: 10.1002/jnr.490150203.Peer-Reviewed Original Research