2023
Molecular Biology of Cytoplasmic Incompatibility Caused by Wolbachia Endosymbionts
Hochstrasser M. Molecular Biology of Cytoplasmic Incompatibility Caused by Wolbachia Endosymbionts. Annual Review Of Microbiology 2023, 77: 299-316. PMID: 37285552, DOI: 10.1146/annurev-micro-041020-024616.Peer-Reviewed Original ResearchConceptsCytoplasmic incompatibilityMale killingHost ubiquitin systemEndosymbiotic bacteriaFemale germlineEukaryotic cellsCognate partnersEmbryonic lethalityBicistronic operonUbiquitin systemDownstream genesWolbachia endosymbiontReproductive advantageCI inductionMolecular biologyInfected femalesEndosymbiontsInfections of malesReproductive alterationsDeubiquitylaseDeubiquitylasesOperonParthenogenesisArthropodsGermline
2000
Evolution and function of ubiquitin-like protein-conjugation systems
Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems. Nature Cell Biology 2000, 2: e153-e157. PMID: 10934491, DOI: 10.1038/35019643.Peer-Reviewed Original ResearchA viable ubiquitin‐activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae
Swanson R, Hochstrasser M. A viable ubiquitin‐activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae. FEBS Letters 2000, 477: 193-198. PMID: 10908719, DOI: 10.1016/s0014-5793(00)01802-0.Peer-Reviewed Original ResearchConceptsUbiquitin system functionActivation of ubiquitinUbiquitin-activating enzymeProteasome-independent degradationUbiquitin systemCellular processesPathway substrateMammalian cellsHypomorphic alleleProtein modificationEnzyme mutantsMutant allelesMembrane receptorsMutantsUbiquitinComparable mutantsSaccharomycesCell functionAllelesProteasomeYeastProteinEnzymeDegradationE1
1999
Structure and functional analyses of the 26S proteasome subunits from plants – Plant 26S proteasome
Fu H, Girod P, Doelling J, van Nocker S, Hochstrasser M, Finley D, Vierstra R. Structure and functional analyses of the 26S proteasome subunits from plants – Plant 26S proteasome. Molecular Biology Reports 1999, 26: 137-146. PMID: 10363660, DOI: 10.1023/a:1006926322501.Peer-Reviewed Original ResearchConceptsProteasome degrades ubiquitinated proteinsUbiquitin fusion degradation (UFD) pathwayStructure/function analysisAAA-ATPase subunitsC-terminal motifDegradation of proteinsRegulatory particle subunitsCore particlesPlant 26SRpn10 geneArabidopsis genesYeast counterpartMoss PhyscomitrellaArabidopsis thalianaPlant hormonesUbiquitin systemProteasome genesDevelopmental programHomologous recombinationProteolytic complexPlant subunitsReverse geneticsUbiquitinated proteinsUbiquitin conjugatesVivo function
1997
SUMO-1: Ubiquitin gains weight
Johnson P, Hochstrasser M. SUMO-1: Ubiquitin gains weight. Trends In Cell Biology 1997, 7: 408-413. PMID: 17708991, DOI: 10.1016/s0962-8924(97)01132-x.Peer-Reviewed Original ResearchNuclear pore complexUbiquitin-like proteinNucleocytoplasmic traffickingPore complexUbiquitin systemPolypeptide functionsProtein crucialSUMO-1Cell biologyDistant similaritySpecific proteinsMechanistic questionsProteinSubstrate degradationProteasomeRecent findingsUbiquitinTraffickingBiologyRoleModificationCrucialComplexesSimilarity
1996
UBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser M. UBIQUITIN-DEPENDENT PROTEIN DEGRADATION. Annual Review Of Genetics 1996, 30: 405-439. PMID: 8982460, DOI: 10.1146/annurev.genet.30.1.405.Peer-Reviewed Original ResearchConceptsRegulatory mechanismsUbiquitin-dependent protein degradationLarge enzyme familyAttachment of ubiquitinCellular regulatory mechanismsSignal transduction pathwaysHigh substrate specificityReceptor-mediated endocytosisPolypeptide ubiquitinProtein ubiquitinationUbiquitin systemTransduction pathwaysEnzyme familyUbiquitinated proteinsSubstrate specificityProtein modificationProtein degradationCell cycleProteasomeUbiquitinationKey transitionsUbiquitinShort peptidesProteinDeubiquitination
1995
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Current Opinion In Cell Biology 1995, 7: 215-223. PMID: 7612274, DOI: 10.1016/0955-0674(95)80031-x.Peer-Reviewed Original ResearchConceptsCellular regulatory mechanismsIntracellular protein degradationCell cycle progressionProtein ubiquitinationUbiquitin systemProtein degradationRegulatory mechanismsCycle progressionSpecific proteinsForeign proteinsLarge familyCell proliferationProteasomeRapid degradationProteinClass I MHC moleculesUbiquitinationDeubiquitinationUbiquitinI MHC moleculesProteolysisEnzymeKey stepDegradationRegulation
1993
The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
Papa F, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 1993, 366: 313-319. PMID: 8247125, DOI: 10.1038/366313a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsGenes, FungalHumansMiceMice, NudeMolecular Sequence DataMutationOncogene ProteinsOncogene Proteins, FusionOncogenesOpen Reading FramesPhenotypeProto-Oncogene ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitin ThiolesteraseUbiquitins
1992
Ubiquitin and intracellular protein degradation
Hochstrasser M. Ubiquitin and intracellular protein degradation. Current Opinion In Cell Biology 1992, 4: 1024-1031. PMID: 1336669, DOI: 10.1016/0955-0674(92)90135-y.Peer-Reviewed Original ResearchConceptsEukaryotic cell regulationConjugation of ubiquitinUbiquitin systemProteolytic targetingProtein degradationIntracellular proteinsProtein turnoverCell regulationDiverse arrayUbiquitinCentral roleProteinEukaryotesMajor routeUbiquitinationProteaseEnzymeDegradationPathwayRegulationRecent workTargetingTurnoverPeptides