Lipid posttranslational modifications. Farnesyl transferase inhibitors. - Wikidata - awgldk - TriplyDB

Lipid posttranslational modifications. Farnesyl transferase inhibitors.

Lipid posttranslational modifications. Farnesyl transferase inhibitors.

http://www.wikidata.org/entity/Q34651253

about

The protein farnesyltransferase regulates HDAC6 activity in a microtubule-dependent manner Neurologic features of Hutchinson-Gilford progeria syndrome after lonafarnib treatment Viral infection and human disease--insights from minimotifs A farnesyltransferase inhibitor prevents both the onset and late progression of cardiovascular disease in a progeria mouse model Farnesyl transferase inhibitor resistance probed by target mutagenesis The value of genomics in dissecting the RAS-network and in guiding therapeutics for RAS-driven cancers KRAS Mutant Pancreatic Cancer: No Lone Path to an Effective Treatment The clinically relevant pharmacogenomic changes in acute myelogenous leukemia The RASopathies Activated Ras as a Therapeutic Target: Constraints on Directly Targeting Ras Isoforms and Wild-Type versus Mutated Proteins Efficacy, Pharmacokinetics, and Metabolism of Tetrahydroquinoline Inhibitors of Plasmodium falciparum Protein Farnesyltransferase Structure of Protein Geranylgeranyltransferase-I from the Human Pathogen Candida albicans Complexed with a Lipid Substrate Structural Basis for Binding and Selectivity of Antimalarial and Anticancer Ethylenediamine Inhibitors to Protein Farnesyltransferase Structure-guided development of selective RabGGTase inhibitors Structures of Cryptococcus neoformans Protein Farnesyltransferase Reveal Strategies for Developing Inhibitors That Target Fungal Pathogens Crystal structures of the fungal pathogenAspergillus fumigatusprotein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design The FNTB promoter polymorphism rs11623866 as a potential predictive biomarker for lonafarnib treatment of ovarian cancer patients.Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III activity and chitin chain length The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding Rasd1, a small G protein with a big role in the hypothalamic response to neuronal activation A yeast-based genomic strategy highlights the cell protein networks altered by FTase inhibitor peptidomimetics The intermediate-activity (L597V)BRAF mutant acts as an epistatic modifier of oncogenic RAS by enhancing signaling through the RAF/MEK/ERK pathway Sequence dependence and differential expression of Ggamma5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells.Evaluation of protein farnesyltransferase substrate specificity using synthetic peptide libraries.Synthesis and screening of a CaaL peptide library versus FTase reveals a surprising number of substrates Measurement of protein farnesylation and geranylgeranylation in vitro, in cultured cells and in biopsies, and the effects of prenyl transferase inhibitors Targeting the protein prenyltransferases efficiently reduces tumor development in mice with K-RAS-induced lung cancer.Overexpression of RASD1 inhibits glioma cell migration/invasion and inactivates the AKT/mTOR signaling pathway Driven to death: Inhibition of farnesylation increases Ras activity and promotes growth arrest and cell death [corrected]Therapeutic intervention based on protein prenylation and associated modifications Statins and neuroprotection: a prescription to move the field forward Clinical trial of a farnesyltransferase inhibitor in children with Hutchinson-Gilford progeria syndrome.Combinatorial modulation of protein prenylation Amide-modified prenylcysteine based Icmt inhibitors: Structure-activity relationships, kinetic analysis and cellular characterization Costello and cardio-facio-cutaneous syndromes: Moving toward clinical trials in RASopathies.Dysregulation of apoptotic signaling in cancer: molecular mechanisms and therapeutic opportunities Molecular bases of progeroid syndromes.Structure-based design and synthesis of potent, ethylenediamine-based, mammalian farnesyltransferase inhibitors as anticancer agents Targeting Rho-GTPases in immune cell migration and inflammation.Farnesyl transferase expression determines clinical response to the docetaxel-lonafarnib combination in patients with advanced malignancies.

P2860

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P2860

Lipid posttranslational modifications. Farnesyl transferase inhibitors.

http://www.wikidata.org/entity/Q34651253

description

2005 nî lūn-bûn

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2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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JLR.R500012-JLR200

P1433

Journal of Lipid Research

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Lipid posttranslational modifications. Farnesyl transferase inhibitors.

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P2093

Andrea D Basso

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Paul Kirschmeier

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W Robert Bishop

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P2860

Prenylated prelamin A interacts with Narf, a novel nuclear protein

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

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

Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit

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

DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras

CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis

Regulation of TSC2 by 14-3-3 binding

Identification of dominant negative mutants of Rheb GTPase and their use to implicate the involvement of human Rheb in the activation of p70S6K

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling

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15-31

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scholarly article

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10.1194/JLR.R500012-JLR200

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1

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47

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2005-11-08T00:00:00Z

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16278491

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