2017
Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima
An JY, Sharif H, Kang GB, Park KJ, Lee JG, Lee S, Jin MS, Song JJ, Wang J, Eom SH. Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima. Biochemical And Biophysical Research Communications 2017, 495: 1201-1207. PMID: 29180014, DOI: 10.1016/j.bbrc.2017.11.158.Peer-Reviewed Original ResearchConceptsPeriplasmic domainMisfolded membrane proteinsATP-dependent proteaseMembrane protein complexesResolution crystal structureHydrophobic membrane environmentMembrane homeostasisProtein complexesMembrane proteinsTransmembrane proteinMembrane environmentThermotoga maritimaStructural insightsFtsHProtease domainToxic proteinsProteinOligomerizationHigh energetic barrierDomainTranslocatesEnergetic barrierMaritimaHomeostasisCrystal structure
2010
Heterohexameric Ring Arrangement of the Eukaryotic Proteasomal ATPases: Implications for Proteasome Structure and Assembly
Tomko RJ, Funakoshi M, Schneider K, Wang J, Hochstrasser M. Heterohexameric Ring Arrangement of the Eukaryotic Proteasomal ATPases: Implications for Proteasome Structure and Assembly. Molecular Cell 2010, 38: 393-403. PMID: 20471945, PMCID: PMC2879271, DOI: 10.1016/j.molcel.2010.02.035.Peer-Reviewed Original Research
2008
Mechanism of Inhibition of Human Immunodeficiency Virus Type 1 Reverse Transcriptase by a Stavudine Analogue, 4′-Ethynyl Stavudine Triphosphate
Yang G, Wang J, Cheng Y, Dutschman GE, Tanaka H, Baba M, Cheng YC. Mechanism of Inhibition of Human Immunodeficiency Virus Type 1 Reverse Transcriptase by a Stavudine Analogue, 4′-Ethynyl Stavudine Triphosphate. Antimicrobial Agents And Chemotherapy 2008, 52: 2035-2042. PMID: 18391035, PMCID: PMC2415781, DOI: 10.1128/aac.00083-08.Peer-Reviewed Original ResearchConceptsM184V mutantNucleoside reverse transcriptase inhibitorHuman immunodeficiency virus type 1Immunodeficiency virus type 1Human immunodeficiency virus type 1 reverse transcriptaseReverse transcriptase inhibitorType 1 reverse transcriptaseVirus type 1Mechanism of inhibitionHIV-1 RTWild-type RTStavudine triphosphateTranscriptase inhibitorD4TD4TTPType 1WT RTMutant RTsReverse transcriptase
2002
The C-terminal Tails of HslU ATPase Act as a Molecular Switch for Activation of HslV Peptidase*
Seong IS, Kang MS, Choi MK, Lee JW, Koh OJ, Wang J, Eom SH, Chung CH. The C-terminal Tails of HslU ATPase Act as a Molecular Switch for Activation of HslV Peptidase*. Journal Of Biological Chemistry 2002, 277: 25976-25982. PMID: 12011053, DOI: 10.1074/jbc.m202793200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAmino Acid SubstitutionATP-Dependent ProteasesBinding SitesElectrophoresis, Polyacrylamide GelEndopeptidasesEnzyme ActivationHeat-Shock ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein ConformationSerine EndopeptidasesStructure-Activity RelationshipConceptsC-terminal tailHslV peptidaseHslVU complexC-terminusHexameric ringMolecular switchATP-dependent proteaseC-terminal 10 residuesAmino acidsProteolytic active sitesDodecamer consistingHslU hexamerHslU ATPaseTail peptideAxial poreATPase actsPolypeptide substratesSubstrate entryS proteasomeHslUCentral poreTerminusHslVPeptidaseCritical role