Peter Moore, PhD
Professor Emeritus of ChemistryCards
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Chemistry
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Professor Emeritus of Chemistry
Appointments
Education & Training
- PhD
- Harvard University (1966)
Research
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Overview
By protein standards, our understanding of RNA structure and function is primitive because it was technically difficult to determine RNA structures for many years. Consequently, even though the technical problems have been overcome, there are lots of RNAs—many of them recently discovered—for which we do not have structures, and hence cannot fully explain their functional properties. The Moore group studies RNA structure/function using NMR and X-ray crystallography as well as molecular biological techniques. The structures being investigated today include: 1) those that form when box H/ACA snoRNAs interact with the rRNA sequences they target for pseudouridylation; and 2) the ribosomal proteins/mRNA complexes responsible for the autogenous regulation of ribosomal protein synthesis. We are also trying to identify the sources of the species specificity shown by many of the antibiotics that inhibit ribosome activity by binding to highly conserved rRNA sequences, and to determine the three-dimensional structure of the eukaryotic ribosome.
Research at a Glance
Yale Co-Authors
Frequent collaborators of Peter Moore's published research.
Publications Timeline
A big-picture view of Peter Moore's research output by year.
Jimin Wang, PhD
18Publications
2,671Citations
Publications
2021
Identification of Mg2+ ions next to nucleotides in cryo-EM maps using electrostatic potential maps
Wang J, Natchiar SK, Moore PB, Klaholz BP. Identification of Mg2+ ions next to nucleotides in cryo-EM maps using electrostatic potential maps. Acta Crystallographica Section D, Structural Biology 2021, 77: 534-539. PMID: 33825713, PMCID: PMC8025889, DOI: 10.1107/s2059798321001893.Peer-Reviewed Original ResearchCitationsAltmetric
2009
Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui▿
Gürel G, Blaha G, Steitz TA, Moore PB. Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui▿. Antimicrobial Agents And Chemotherapy 2009, 53: 5010-5014. PMID: 19738021, PMCID: PMC2786347, DOI: 10.1128/aac.00817-09.Peer-Reviewed Original ResearchCitationsAltmetricU2504 Determines the Species Specificity of the A-Site Cleft Antibiotics: The Structures of Tiamulin, Homoharringtonine, and Bruceantin Bound to the Ribosome
Gürel G, Blaha G, Moore PB, Steitz TA. U2504 Determines the Species Specificity of the A-Site Cleft Antibiotics: The Structures of Tiamulin, Homoharringtonine, and Bruceantin Bound to the Ribosome. Journal Of Molecular Biology 2009, 389: 146-156. PMID: 19362093, PMCID: PMC2682339, DOI: 10.1016/j.jmb.2009.04.005.Peer-Reviewed Original ResearchCitationsAltmetric
2008
Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit.
Ippolito JA, Kanyo ZF, Wang D, Franceschi FJ, Moore PB, Steitz TA, Duffy EM. Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit. Journal Of Medicinal Chemistry 2008, 51: 3353-6. PMID: 18494460, DOI: 10.1021/jm800379d.Peer-Reviewed Original ResearchMutations Outside the Anisomycin-Binding Site Can Make Ribosomes Drug-Resistant
Blaha G, Gürel G, Schroeder SJ, Moore PB, Steitz TA. Mutations Outside the Anisomycin-Binding Site Can Make Ribosomes Drug-Resistant. Journal Of Molecular Biology 2008, 379: 505-519. PMID: 18455733, PMCID: PMC2442718, DOI: 10.1016/j.jmb.2008.03.075.Peer-Reviewed Original ResearchCitationsAltmetric
2006
The Geometry of the Ribosomal Polypeptide Exit Tunnel
Voss NR, Gerstein M, Steitz TA, Moore PB. The Geometry of the Ribosomal Polypeptide Exit Tunnel. Journal Of Molecular Biology 2006, 360: 893-906. PMID: 16784753, DOI: 10.1016/j.jmb.2006.05.023.Peer-Reviewed Original ResearchCitationsAltmetric
2005
Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted
Tu D, Blaha G, Moore PB, Steitz TA. Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted. Extremophiles 2005, 9: 427-435. PMID: 15970993, DOI: 10.1007/s00792-005-0459-y.Peer-Reviewed Original ResearchCitationsMeSH KeywordsBase SequenceBlotting, SouthernChromosome MappingCrystallography, X-RayDNADNA PrimersElectronsEscherichia coli ProteinsGene DeletionGenetic TechniquesHaloarcula marismortuiModels, ChemicalModels, GeneticModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationOperonPlasmidsReverse Transcriptase Polymerase Chain ReactionRibosomal ProteinsRNA-Binding ProteinsRNA, RibosomalRNA, Ribosomal, 23SrRNA OperonSucroseThe ribosome revealed
Moore PB, Steitz TA. The ribosome revealed. Trends In Biochemical Sciences 2005, 30: 281-283. PMID: 15950868, DOI: 10.1016/j.tibs.2005.04.006.Peer-Reviewed Original ResearchCitationsStructures of MLSBK Antibiotics Bound to Mutated Large Ribosomal Subunits Provide a Structural Explanation for Resistance
Tu D, Blaha G, Moore PB, Steitz TA. Structures of MLSBK Antibiotics Bound to Mutated Large Ribosomal Subunits Provide a Structural Explanation for Resistance. Cell 2005, 121: 257-270. PMID: 15851032, DOI: 10.1016/j.cell.2005.02.005.Peer-Reviewed Original ResearchCitationsAltmetric
2004
The contribution of metal ions to the structural stability of the large ribosomal subunit
Klein DJ, Moore PB, Steitz TA. The contribution of metal ions to the structural stability of the large ribosomal subunit. RNA 2004, 10: 1366-1379. PMID: 15317974, PMCID: PMC1370624, DOI: 10.1261/rna.7390804.Peer-Reviewed Original ResearchCitationsAltmetric
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