Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
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The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimeticsHomodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures.Structure of mammalian protein geranylgeranyltransferase type-ICrystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosisReaction path of protein farnesyltransferase at atomic resolutionStructure of tRNA Dimethylallyltransferase: RNA Modification through a ChannelStructural Basis for Binding and Selectivity of Antimalarial and Anticancer Ethylenediamine Inhibitors to Protein FarnesyltransferaseCrystal Structure of Heterodimeric Hexaprenyl Diphosphate Synthase from Micrococcus luteus B-P 26 Reveals That the Small Subunit Is Directly Involved in the Product Chain Length RegulationStructures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal PathogensCrystal structures of the fungal pathogenAspergillus fumigatusprotein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug designLysine(164)alpha of protein farnesyltransferase is important for both CaaX substrate binding and catalysisGauging a hydrocarbon ruler by an intrinsic exciton probe.A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxinRole of isoprenoid lipids on the heterotrimeric G protein gamma subunit in determining effector activation.The CaaX specificities of Arabidopsis protein prenyltransferases explain era1 and ggb phenotypesThe alpha-subunit of protein prenyltransferases is a member of the tetratricopeptide repeat family.Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma bruceiStructure, mechanism and function of prenyltransferases.Farnesyltransferase--new insights into the zinc-coordination sphere paradigm: evidence for a carboxylate-shift mechanism.Farnesyl diphosphate analogues with aryl moieties are efficient alternate substrates for protein farnesyltransferaseLipid posttranslational modifications. Farnesyl transferase inhibitors.Lipid-modified proteins as biomarkers for cardiovascular disease: a review.Thematic review series: lipid posttranslational modifications. geranylgeranylation of Rab GTPases.Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies.Novel route to chaetomellic acid A and analogues: serendipitous discovery of a more competent FTase inhibitor.A mutant form of human protein farnesyltransferase exhibits increased resistance to farnesyltransferase inhibitors.Protein farnesylation is critical for maintaining normal cell morphology and canavanine resistance in Schizosaccharomyces pombe.Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity.Computational studies of the farnesyltransferase ternary complex part II: the conformational activation of farnesyldiphosphate.Successful molecular dynamics simulation of the zinc-bound farnesyltransferase using the cationic dummy atom approach.Finding a needle in the haystack: computational modeling of Mg2+ binding in the active site of protein farnesyltransferase.Computational studies of the farnesyltransferase ternary complex part I: substrate binding.Cloning and characterisation of chlorophyll synthase from Avena sativa.Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand.Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.In Silico–Based Structural Analysis of Arylthiophene Derivatives for FTase Inhibitory Activity, hERG, and Other Toxic EffectsStructural feature study of benzofuran derivatives as farnesyltransferase inhibitorsCrystal Structure of Type-III Geranylgeranyl Pyrophosphate Synthase fromSaccharomyces cerevisiaeand the Mechanism of Product Chain Length Determination
P2860
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P2860
Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@ast
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@en
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@nl
type
label
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@ast
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@en
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@nl
prefLabel
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@ast
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@en
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@nl
P2093
P356
P1433
P1476
Cocrystal structure of protein ...... farnesyl diphosphate substrate
@en
P2093
P304
P356
10.1021/BI980708E
P407
P577
1998-07-07T00:00:00Z