About: Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p

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rdf:type	Item
description	artículu científicu espublizáu en 2000 (ast) vědecký článek publikovaný v roce 2000 (cs) 2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw) wüsseschaftlicher Artikel, wo im April 2000 veröffentlicht worden isch (gsw) 2000 թվականի ապրիլին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована у квітні 2000 (uk) im April 2000 veröffentlichter wissenschaftlicher Artikel (de) vedecký článok (publikovaný 2000/04/11) (sk) مقالة علمية (نشرت في 11-4-2000) (ar) wetenschappelijk artikel (gepubliceerd op 2000/04/11) (nl) scientific journal article (en) article scientifique publié en avril 2000 (fr)
publication date	wds:Q28492952-63741FCB-AA0E-4AFE-AA60-B87F43EA093A
publication date	2000-04-11 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28492952-AD207F94-664B-42F2-922D-952D75B3578A
language of work or name	English
author name string	wds:Q28492952-0E2EF33C-EF3E-4FE2-8BC9-A147B9F5775D wds:Q28492952-40F08F22-62A5-4AE5-A92F-00067DB4DAF1 wds:Q28492952-810A70A5-6AA9-4D6A-9F66-3C51D5F67655 wds:Q28492952-CE9AD71F-E4EF-494B-9509-7CFA458DF9D2 wds:Q28492952-DDA0CE4F-772D-4191-B794-EB3D417EFFB8
author name string	C. D. Poulter D. H. Wong E. K. Dolence J. M. Dolence L. E. Steward
rdfs:label	Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (en) Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (nl) Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (ast)
skos:prefLabel	Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (en) Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (nl) Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (ast)
name	Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (en) Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (nl) Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (ast)
title	wds:Q28492952-A9BEBE26-D4D1-4951-9006-DD7755B7D266
title	Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p (en)
page(s)	wds:Q28492952-1CCC4D92-0F82-43B3-A6D3-9CABB51EE54C
page(s)	4096–4104
instance of	wds:Q28492952-5F0A2682-7862-4FE2-A456-3ED6CD3E14F9
instance of	scholarly article
main subject	wds:Q28492952-76A8A0F1-439D-4FFA-8F1E-2C88C64A25A2
main subject	Saccharomyces cerevisiae
PubMed ID	wds:Q28492952-7D4D8700-698D-4BA5-92CD-EFA45C1434BD
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10747800
PubMed ID	10747800
published in	wds:Q28492952-FB65612F-B7AD-48A6-9894-AAE3E6A4FF65
published in	Biochemistry
issue	wds:Q28492952-742D8032-228C-4433-8586-08F0FD29A3D1
volume	wds:Q28492952-51BBEF6E-5938-4F4A-82F3-58C48AD2E3CB
issue	14
volume	39
DOI	wds:Q28492952-7CBBBCCB-2180-4506-8636-FC86A56CD344
DOI	http://dx.doi.org/10.1021/BI9923611
DOI	10.1021/BI9923611
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28492952
is cites work of	USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases HIV protease inhibitors block streptolysin S production The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities Structure of the integral membrane protein CAAX protease Ste24p Human Ras converting enzyme endoproteolytic specificity at the P2' and P3' positions of K-Ras-derived peptides Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues Mechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1 Small-molecule inhibitors of the Rce1p CaaX protease Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones Topology of the yeast Ras converting enzyme as inferred from cysteine accessibility studies Heterologous expression studies of Saccharomyces cerevisiae reveal two distinct trypanosomatid CaaX protease activities and identify their potential targets Therapeutic intervention based on protein prenylation and associated modifications The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes Mechanisms of nickel toxicity in microorganisms Characteristics affecting expression and solubilization of yeast membrane proteins AtFACE-2, a functional prenylated protein protease from Arabidopsis thaliana related to mammalian Ras-converting enzymes. Expansion of type II CAAX proteases reveals evolutionary origin of γ-secretase subunit APH-1 Staphylococcus aureus mutants with increased lysostaphin resistance Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity A novel RCE1 isoform is required for H-Ras plasma membrane localization and is regulated by USP17. Protein prenyltransferases: anchor size, pseudogenes and parasites ABI domain-containing proteins contribute to surface protein display and cell division in Staphylococcus aureus The abi proteins and their involvement in bacteriocin self-immunity A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans. 8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells. Rce1: mechanism and inhibition. Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer's disease. Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases. Photoaffinity labeling of Ras converting enzyme using peptide substrates that incorporate benzoylphenylalanine (Bpa) residues: improved labeling and structural implications Control of Staphylococcus aureus Quorum Sensing by a Membrane-Embedded Peptidase Photoaffinity labeling of Ras converting enzyme 1 (Rce1p) using a benzophenone-containing peptide substrate Lipid and sulfur substituted prenylcysteine analogs as human Icmt inhibitors Sequence dependence and differential expression of Ggamma5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells
is cites work of	wds:Q27677111-30CD5ADE-1284-4574-85DB-06D98DE5B7D7 wds:Q34207482-4B057EAD-EA32-4FC5-94ED-FF34654438E6 wds:Q33943379-547F5271-A8BF-473F-B370-265C1D3047EB wds:Q35990361-7F19BB47-3A04-4A5E-8318-C314493ACD26 wds:Q73852862-B96BB683-0B2F-4E35-AB6D-0632BFE5DAA3

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