About: Protein prenylation: molecular mechanisms and functional consequences

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scientific article (publication date: 1996)

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rdf:type	Item
description	artículu científicu espublizáu en 1996 (ast) 1996 թուականին հրատարակուած գիտական յօդուած (hyw) 1996 թվականին հրատարակված գիտական հոդված (hy) مقالة علمية (نشرت عام 1996) (ar) наукова стаття, опублікована в 1996 (uk) wetenschappelijk artikel (gepubliceerd in 1996) (nl) scientific article (publication date: 1996) (en) article scientifique publié en 1996 (fr) im Januar 1996 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q29618038-8D6B5A7A-5BCC-4224-B566-39BA4FECF2E1
publication date	1996-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q29618038-A1CF02DF-DE82-4697-8EB1-AC715BE06107
language of work or name	English
author name string	wds:Q29618038-06640EB2-05B1-4FA2-AE4B-7F6AD3DF0BA2 wds:Q29618038-C53D0025-5B19-4A90-975A-498669BCF6CA
OpenCitations bibliographic resource ID	wds:Q29618038-63EFFE6F-40EF-4D4D-BAFC-57ADCF69D910
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3388740
author name string	Casey PJ Zhang FL
OpenCitations bibliographic resource ID	3388740
rdfs:label	Protein prenylation: molecular mechanisms and functional consequences (en) Protein prenylation: molecular mechanisms and functional consequences (ast)
skos:prefLabel	Protein prenylation: molecular mechanisms and functional consequences (en) Protein prenylation: molecular mechanisms and functional consequences (ast)
name	Protein prenylation: molecular mechanisms and functional consequences (en) Protein prenylation: molecular mechanisms and functional consequences (ast)
title	wds:Q29618038-019BFDBB-F704-413B-AE3D-848FE1655664
title	Protein prenylation: molecular mechanisms and functional consequences (en)
page(s)	wds:Q29618038-0D03DC2C-A3F7-463D-938A-17E571260A6A
page(s)	241-69
instance of	wds:Q29618038-372F7F96-240E-4DF3-A82F-7CD49B8C01D9 wds:Q29618038-ab6b3b2b-e467-4e84-aead-36d13e748921
instance of	review article scholarly article
PubMed ID	wds:Q29618038-12F92120-48A0-4988-B83B-BFD3AEDFF5C1
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8811180
PubMed ID	8811180
published in	wds:Q29618038-66252C88-BF33-4A3E-92E0-F54B2243E3B8
published in	Annual Review of Biochemistry
volume	wds:Q29618038-8D1B34C7-2985-4B83-8469-9A6A8FBFE1FC
volume	65
DOI	wds:Q29618038-9B84FF49-AE48-4C0C-8A27-676784D4F801
DOI	http://dx.doi.org/10.1146/ANNUREV.BI.65.070196.001325
DOI	10.1146/ANNUREV.BI.65.070196.001325
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q29618038
is cites work of	Regulation of dendritic branching and filopodia formation in hippocampal neurons by specific acylated protein motifs Prenylated prelamin A interacts with Narf, a novel nuclear protein Cloning and characterization of a mammalian prenyl protein-specific protease Immunomodulatory synergy by combination of atorvastatin and glatiramer acetate in treatment of CNS autoimmunity Combined medication of lovastatin with rolipram suppresses severity of experimental autoimmune encephalomyelitis Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity A tagging-via-substrate approach to detect the farnesylated proteome using two-dimensional electrophoresis coupled with Western blotting Protein prenylation: a pivotal posttranslational process Statin's excitoprotection is mediated by sAPP and the subsequent attenuation of calpain-induced truncation events, likely via rho-ROCK signaling. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases A novel proteinase, SNOWY COTYLEDON4, is required for photosynthetic acclimation to higher light intensities in Arabidopsis. Effects of statins and farnesyl transferase inhibitors on ERK phosphorylation, apoptosis and cell viability in non-small lung cancer cells Development of farsenyl transferase inhibitors as anticancer agents Comparison of the PTS1- and Rab8b-binding properties of Pex5p and Pex5Rp/TRIP8b Peroxisomal lactate dehydrogenase is generated by translational readthrough in mammals Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesis Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane Prenylation-dependent association of Ki-Ras with microtubules. Evidence for a role in subcellular trafficking Comparative analysis of Drosophila and mammalian complexins as fusion clamps and facilitators of neurotransmitter release. Zinc-binding cysteines: diverse functions and structural motifs. Stimulation of neutrophils by prenylcysteine analogs: Ca(2+) release and influx Structural determinants involved in the formation and activation of G protein betagamma dimers Statin drugs and dietary isoprenoids as antithrombotic agents. The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase Protein palmitoylation: a regulator of neuronal development and function Bisphosphonate mechanism of action Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome Fission yeast mod5p regulates polarized growth through anchoring of tea1p at cell tips Gliotoxin is a dual inhibitor of farnesyltransferase and geranylgeranyltransferase I with antitumor activity against breast cancer in vivo. The pharmacology of bisphosphonates and new insights into their mechanisms of action Targeting protein prenylation for cancer therapy Synthesis of palmitoylated Ras-peptides and -proteins Cell-cycle and developmental regulation of TbRAB31 localisation, a GTP-locked Rab protein from Trypanosoma brucei. Farnesylation mediates brassinosteroid biosynthesis to regulate abscisic acid responses The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis Rosuvastatin, inflammation, C-reactive protein, JUPITER, and primary prevention of cardiovascular disease--a perspective Post-translational modifications of intermediate filament proteins: mechanisms and functions Investigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activity Geranylgeranyltransferase I inhibitors target RalB to inhibit anchorage-dependent growth and induce apoptosis and RalA to inhibit anchorage-independent growth Novel approaches to the treatment of non-small cell lung cancer. Context-dependent substrate recognition by protein farnesyltransferase. Cloning, expression, and cellular localization of a human prenylcysteine lyase Isolation and characterization of a prenylcysteine lyase from bovine brain Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol Molecular cloning and characterization of CLICK-III/CaMKIgamma, a novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase (CaMK) Is obesity an inflammatory condition? Modulation of statin-activated shedding of Alzheimer APP ectodomain by ROCK Lovastatin inhibits formation of AA amyloid Implication of geranylgeranyltransferase I in synapse formation Prenylation of the floral transcription factor APETALA1 modulates its function.

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