Protein prenylation: a pivotal posttranslational process.
about
Molecular mechanisms involved in farnesol-induced apoptosisRefinement and prediction of protein prenylation motifsRole of substrate dynamics in protein prenylation reactionsLamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathySynergistic induction of apoptosis by HMG-CoA reductase inhibitor and histone deacetylases inhibitor in HeLa cellsIdentification of a farnesol analog as a Ras function inhibitor using both an in vivo Ras activation sensor and a phenotypic screening approach.Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity.Reversible inactivation of the transcriptional function of P53 protein by farnesylation.Sequence dependence and differential expression of Ggamma5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells.Towards complete sets of farnesylated and geranylgeranylated proteins.Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities.Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner.Porcine Liver Carboxylesterase Requires Polyisoprenylation for High Affinity Binding to Cysteinyl Substrates.Rapid analysis of protein farnesyltransferase substrate specificity using peptide libraries and isoprenoid diphosphate analogues.Drosophila Tempura, a novel protein prenyltransferase α subunit, regulates notch signaling via Rab1 and Rab11.MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation.The human T-cell leukemia virus type 1 p13II protein: effects on mitochondrial function and cell growthAlteration of mevalonate pathway in proliferated vascular smooth muscle from diabetic mice: possible role in high-glucose-induced atherogenic process.Exploration of GGTase-I substrate requirements. Part 1: Synthesis and biochemical evaluation of novel aryl-modified geranylgeranyl diphosphate analogs.Exploration of GGTase-I substrate requirements. Part 2: Synthesis and biochemical analysis of novel saturated geranylgeranyl diphosphate analogs.Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications.Purification of prenylated proteins by affinity chromatography on cyclodextrin-modified agarose.Regulation of the brain isoprenoids farnesyl- and geranylgeranylpyrophosphate is altered in male Alzheimer patients.Cholesterol as a causative factor in Alzheimer's disease: a debatable hypothesis.Extolling the benefits of molecular therapeutic lipidation.Rho-kinase: regulation, (dys)function, and inhibition.Catch me if you can: challenges and applications of cross-linking approaches.Prenyltransferase Inhibitors: Treating Human Ailments from Cancer to Parasitic Infections.Menadione is a metabolite of oral vitamin K.The Role of Geranylgeranyltransferase I-Mediated Protein Prenylation in the Brain.Development of an image-based screening system for inhibitors of the plastidial MEP pathway and of protein geranylgeranylation.A trs20 mutation that mimics an SEDT-causing mutation blocks selective and non-selective autophagy: a model for TRAPP III organization.Exploring the biochemistry of the prenylome and its role in disease through proteomics: progress and potential.Artificially induced protein-membrane anchorage with cholesterol-based recognition agents as a new therapeutic concept.Increased resistance to a farnesyltransferase inhibitor by N-cadherin expression in Bcr/Abl-P190 lymphoblastic leukemia cells.K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes.Lovastatin inhibits formation of AA amyloid.Terminal lipophilization of a unique DNA dodecamer by various nucleolipid headgroups: Their incorporation into artificial lipid bilayers and hydrodynamic properties.Specific DNA duplex formation at an artificial lipid bilayer: fluorescence microscopy after Sybr Green I stainingPolyisoprenylation potentiates the inhibition of polyisoprenylated methylated protein methyl esterase and the cell degenerative effects of sulfonyl fluorides.
P2860
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P2860
Protein prenylation: a pivotal posttranslational process.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մարտին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Protein prenylation: a pivotal posttranslational process.
@ast
Protein prenylation: a pivotal posttranslational process.
@en
type
label
Protein prenylation: a pivotal posttranslational process.
@ast
Protein prenylation: a pivotal posttranslational process.
@en
prefLabel
Protein prenylation: a pivotal posttranslational process.
@ast
Protein prenylation: a pivotal posttranslational process.
@en
P1476
Protein prenylation: a pivotal posttranslational process.
@en
P356
10.1016/S0006-291X(03)00323-1
P407
P577
2003-03-01T00:00:00Z