Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens - Wikidata - wikimedia - TriplyDB

Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens

Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens

http://www.wikidata.org/entity/Q27671538

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Virulence-Associated Enzymes of Cryptococcus neoformans Crystal structures of the fungal pathogenAspergillus fumigatusprotein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design All about that fat: Lipid modification of proteins in Cryptococcus neoformans In vitro antifungal activity of farnesyltransferase inhibitors against clinical isolates of Aspergillus and Candida Rapid analysis of protein farnesyltransferase substrate specificity using peptide libraries and isoprenoid diphosphate analogues.Antifungal activity of topical microemulsion containing a thiophene derivative.Elucidating drug resistance in human fungal pathogens.Crystal structure of E. coli lipoprotein diacylglyceryl transferase.Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications.Relative Contributions of Prenylation and Postprenylation Processing in Cryptococcus neoformans Pathogenesis.Restricted substrate specificity for the geranylgeranyltransferase-I enzyme in Cryptococcus neoformans: implications for virulence.Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.Exploration of Aspergillus fumigatus Ras pathways for novel antifungal drug targets.ram1 gene, encoding a subunit of farnesyltransferase, contributes to growth, antifungal susceptibility to amphotericin B of Aspergillus fumigatus.The antifungal pipeline: a reality check.Ras-Mediated Signal Transduction and Virulence in Human Pathogenic Fungi.Exploring the putative self-binding property of the human farnesyltransferase alpha-subunit.Stress Adaptation.The Aspergillus fumigatus farnesyltransferase β-subunit, RamA, mediates growth, virulence, and antifungal susceptibility.Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Efficient farnesylation of an extended C-terminal C(x)3X sequence motif expands the scope of the prenylated proteome.New Horizons in Antifungal Therapy.Lonafarnib synergizes with azoles against Aspergillus spp. and Exophiala spp.Targeting protein localization for anti-infective therapy.Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer's disease.

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Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens

http://www.wikidata.org/entity/Q27671538

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2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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JBC.M111.250506

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Journal of Biological Chemistry

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Structures of Cryptococcus neo ...... s That Target Fungal Pathogens

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Connie B Nichols

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Homme W Hellinga

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J Andrew Alspaugh

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Lorena S Beese

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Michael A Hast

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Shannon M Kelly

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Stephanie M Armstrong

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P2860

The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics

Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity

Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes

Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity

Structure of mammalian protein geranylgeranyltransferase type-I

Processing of X-ray diffraction data collected in oscillation mode

Tricyclic farnesyl protein transferase inhibitors: crystallographic and calorimetric studies of structure-activity relationships

The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures

Reaction path of protein farnesyltransferase at atomic resolution

Caged Protein Prenyltransferase Substrates: Tools for Understanding Protein Prenylation

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4989301

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10.1074/JBC.M111.250506

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40

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2011-10-07T00:00:00Z

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protein farnesyltransferase, putative

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3186413

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