2024
Flaviviruses manipulate mitochondrial processes to evade the innate immune response
Boytz R, Keita K, Pawlak J, Laurent-Rolle M. Flaviviruses manipulate mitochondrial processes to evade the innate immune response. Npj Viruses 2024, 2: 47. PMID: 39371935, PMCID: PMC11452341, DOI: 10.1038/s44298-024-00057-x.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMitochondrial processesAntiviral signaling proteinProgrammed Cell DeathRegulate various aspectsInnate immune response to viral infectionEukaryotic organellesResponse to viral infectionMitochondrial biologyInnate immune responseMitochondrial morphologyCellular processesSignaling proteinsCell deathImmune response to viral infectionInnate immunityMitochondriaCalcium homeostasisFlavivirusesViral infectionImmune responseOrganellesPathogensDynamic structureProteinHomeostasis
2018
Towards dynamic structure of biological complexes at atomic resolution by cryo-EM
Zhang K. Towards dynamic structure of biological complexes at atomic resolution by cryo-EM. Chinese Physics B 2018, 27: 066801. DOI: 10.1088/1674-1056/27/6/066801.Peer-Reviewed Original Research
2004
Exchange of DNA Base Pairs that Coincides with Recognition of Homology Promoted by E. coli RecA Protein
Folta-Stogniew E, O'Malley S, Gupta R, Anderson KS, Radding CM. Exchange of DNA Base Pairs that Coincides with Recognition of Homology Promoted by E. coli RecA Protein. Molecular Cell 2004, 15: 965-975. PMID: 15383285, DOI: 10.1016/j.molcel.2004.08.017.Peer-Reviewed Original ResearchConceptsE. coli RecA proteinRecognition of homologyColi RecA proteinRecA proteinBase pairsStrand exchangeSynaptic complexDouble-strand breaksT base pairsStopped-flow fluorescenceGenetic recombinationSingle strandsHomologyUnresolved mechanismDuplex DNADNA base pairsDNARate of exchangeProteinDynamic structureComplexesStrandsBasis exchangeRate of formationMechanism
2003
Curariform Antagonists Bind in Different Orientations to Acetylcholine-binding Protein*
Gao F, Bern N, Little A, Wang HL, Hansen SB, Talley TT, Taylor P, Sine SM. Curariform Antagonists Bind in Different Orientations to Acetylcholine-binding Protein*. Journal Of Biological Chemistry 2003, 278: 23020-23026. PMID: 12682067, PMCID: PMC3191914, DOI: 10.1074/jbc.m301151200.Peer-Reviewed Original ResearchConceptsAcetylcholine-binding proteinDocking orientationTrp-53Site residuesSubunit interfaceLigand bindingProtein flexibilityAChBPNicotinic acetylcholine receptorsSide chainsTyr-89Binding sitesMutagenesisReceptor binding sitesAcetylcholine receptorsProteinSimilar ligandsDynamic structureBindingStructure-activity relationshipsMolecular dynamics simulationsEquivalent nitrogenComputational methodsStructural levelDistinct orientations
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