2024
The BICD2 dynein cargo adaptor binds to the HPV16 L2 capsid protein and promotes HPV infection
Speckhart K, Choi J, DiMaio D, Tsai B. The BICD2 dynein cargo adaptor binds to the HPV16 L2 capsid protein and promotes HPV infection. PLOS Pathogens 2024, 20: e1012289. PMID: 38829892, PMCID: PMC11230635, DOI: 10.1371/journal.ppat.1012289.Peer-Reviewed Original ResearchTrans Golgi networkL2 capsid proteinPromote infectionCapsid proteinIn vitro binding studiesDynein adaptorsGolgi networkCargo adaptorsBICD2 functionDynein motorsC-terminusDyneinSupport infectionMolecular basisBICD2EndosomesAdaptorProteinBinding studiesCell-basedVirusShort segmentHuman papillomavirusGolgiInfection
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
1971
A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Myers G, Blank H, Söll D. A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1971, 246: 4955-4964. PMID: 4936720, DOI: 10.1016/s0021-9258(18)61956-8.Peer-Reviewed Original ResearchConceptsEscherichia coli KSeryl-tRNA synthetaseLeucyl-tRNA synthetaseRibonucleic acidTransfer ribonucleic acidValyl-tRNA synthetaseTRNA recognitionColi KSynthetase-tRNA complexIsoacceptorsAmino acidsEquilibrium binding studiesPing-pong typeTRNASynthetaseEnzymeKm valuesSubstrate inhibitionBasic similaritiesBinding studiesSerylAcidATPSame bufferSequence
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