Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
about
tRNAs as antibiotic targetsUltratight crystal packing of a 10 kDa proteinIdentifying ligand-binding hot spots in proteins using brominated fragmentsIdentification of distinct thiopeptide-antibiotic precursor lead compounds using translation machinery assaysManipulation of thiocillin variants by prepeptide gene replacement: structure, conformation, and activity of heterocycle substitution mutants.Thiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Codon randomization for rapid exploration of chemical space in thiopeptide antibiotic variants.Elongation factor Tu-targeted antibiotics: four different structures, two mechanisms of action.Identification of local conformational similarity in structurally variable regions of homologous proteins using protein blocksA comprehensive review of glycosylated bacterial natural products.Mechanism of action of and mechanism of reduced susceptibility to the novel anti-Clostridium difficile compound LFF571EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways.Elucidating and engineering thiopeptide biosynthesis.Elongation factor Ts directly facilitates the formation and disassembly of the Escherichia coli elongation factor Tu·GTP·aminoacyl-tRNA ternary complex.The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffoldsRecent advances in the chemistry and biology of naturally occurring antibiotics.Amino acid changes in elongation factor Tu of Mycoplasma pneumoniae and Mycoplasma genitalium influence fibronectin binding.Decoding Mammalian Ribosome-mRNA States by Translational GTPase ComplexesGeneration of thiocillin variants by prepeptide gene replacement and in vivo processing by Bacillus cereus.Recent advances in thiopeptide antibiotic biosynthesis.Biosynthesis of thiopeptide antibiotics and their pathway engineering.Prospects for new antibiotics: a molecule-centered perspective.Elfamycins: inhibitors of elongation factor-Tu.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.A Derivative of the Thiopeptide GE2270A Highly Selective against Propionibacterium acnes.Elongation factor Tu3 (EF-Tu3) from the kirromycin producer Streptomyces ramocissimus Is resistant to three classes of EF-Tu-specific inhibitors.Energetics of activation of GTP hydrolysis on the ribosome.Ribosomal Natural Products, Tailored To Fit.
P2860
Q26822430-BA7F7BC6-240F-4F45-9E48-78886B994DE6Q27676943-5F3561E3-9341-4B09-85BB-0FF7BBFCE142Q27679833-CC557E61-14DF-4F44-BC3A-FA93E9987436Q33513784-4CC6EE7D-C48D-4A40-BFCE-7ADAF4001FEBQ33901399-9C9470EF-A30E-4283-8D51-6F6381036D55Q34107147-8138CF2D-9695-4978-AB90-69D06239CF71Q34312732-D976D212-AF27-4167-B15F-65D66FABC248Q34520644-CDF12772-3412-4B81-AE38-C993EF6CA2FAQ34552393-122F8B6A-6EFF-4B91-B402-958FD70369FAQ34698788-02E43823-9BFE-4BF0-A2C4-7DB3A747AE02Q36029831-288F21B4-15BC-4E8F-88A7-BA8FC43191C5Q36171778-147C1E3E-6D92-41FD-A585-759CFF636225Q36228050-B02603F2-8849-4939-AC8A-2ACD004DF74AQ36369930-79BC9414-D7EA-4826-B1FB-8C7E48B5C99DQ36832738-E670E27E-4E5F-42AA-A5F0-77F46DDEC679Q36884001-A8778873-5816-4954-BFA6-1EF4B49C45A2Q37313939-67F4A178-E4AF-4346-B8A0-32B270C0C466Q37333462-C2B6CE9F-16BE-4B7E-9026-118E3472AE28Q37430049-449ED066-CA0B-424C-9DBE-91B89DC26578Q37455595-46FBFB44-363C-481A-9861-3D4A5F838D0FQ37683518-4A0F8E01-4D51-4436-9BB1-BFEC34DE78F5Q38068336-634EC56F-6451-4D89-B394-AC8DDA7957CDQ38113689-B46CAA6D-94E1-430A-8DD3-54BA1788476FQ38657231-B5AE61AE-553C-422B-A3DB-8D51D79338D5Q38751212-5052D577-57F4-40C9-8FFC-701D69C1FC67Q42109273-27485041-CE1C-4B7B-8764-72486461EA1EQ42845267-E3B44BB1-09AF-4065-8B39-42F79B17A74DQ44541570-12FB816E-C701-4D15-A451-7BDE0F1B8ED9Q47953416-2A43B4B9-85A9-4C18-8756-8768442050D3
P2860
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
description
im Juni 2006 veröffentlicher wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в червні 2006
@uk
name
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@en
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@nl
type
label
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@en
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@nl
prefLabel
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@en
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@nl
P2093
P356
P1433
P1476
Structural Basis of the Action of Pulvomycin and GE2270 A on Elongation Factor Tu†,‡
@en
P2093
Andrea Parmeggiani
Ivo M. Krab
Jens Nyborg
Rikke C. Nielsen
Sumio Okamura
P304
P356
10.1021/BI0525122
P407
P50
P577
2006-06-01T00:00:00Z