The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities.
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Protein prenyltransferasesMutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residuesA carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylationStructure of the integral membrane protein CAAX protease Ste24p.Mechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1New regulators of drug sensitivity in the family of yeast zinc cluster proteins.Small-molecule inhibitors of the Rce1p CaaX proteaseThe multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor.Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides.Chemical inhibition of CaaX protease activity disrupts yeast Ras localization.Roles of C-terminal processing, and involvement in transacylation reaction of human group IVC phospholipase A2 (cPLA2gamma)Prelamin A farnesylation and progeroid syndromesThematic review series: lipid posttranslational modifications. Fighting parasitic disease by blocking protein farnesylationTowards the systematic mapping and engineering of the protein prenylation machinery in Saccharomyces cerevisiaeBiochemical studies of Zmpste24-deficient miceYeast genes controlling responses to topogenic signals in a model transmembrane protein.Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity.Sequence dependence and differential expression of Ggamma5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells.The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes.Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases.A combination of metabolic labeling and 2D-DIGE analysis in response to a farnesyltransferase inhibitor facilitates the discovery of new prenylated proteins.Therapeutic intervention based on protein prenylation and associated modificationsPrelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.Protein prenyltransferases: anchor size, pseudogenes and parasites.Inhibitors of protein geranylgeranyltransferase-I lead to prelamin A accumulation in cells by inhibiting ZMPSTE24Greasing the protein biosynthesis machinery of photoreceptor neurons: Role for postprenylation processing of proteins.Type-I prenyl protease function is required in the male germline of Drosophila melanogaster.Characterization of a novel microcin that kills enterohemorrhagic Escherichia coli O157:H7 and O26.Biogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.HIV-protease inhibitors block the enzymatic activity of purified Ste24p.Severe mandibuloacral dysplasia caused by novel compound heterozygous ZMPSTE24 mutations in two Japanese siblings.Heterologous expression studies of Saccharomyces cerevisiae reveal two distinct trypanosomatid CaaX protease activities and identify their potential targets.ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders.A shunt pathway limits the CaaX processing of Hsp40 Ydj1p and regulates Ydj1p-dependent phenotypes.A novel role of the yeast CaaX protease Ste24 in chitin synthesis.Saccharomyces cerevisiae a-factor mutants reveal residues critical for processing, activity, and export.Proteolytic processing of certain CaaX motifs can occur in the absence of the Rce1p and Ste24p CaaX proteases.The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity.AtFACE-2, a functional prenylated protein protease from Arabidopsis thaliana related to mammalian Ras-converting enzymes.Purification, functional reconstitution, and characterization of the Saccharomyces cerevisiae isoprenylcysteine carboxylmethyltransferase Ste14p.
P2860
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P2860
The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities.
description
2000 nî lūn-bûn
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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2000 թվականի հունիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年学术文章
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2000年学术文章
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The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@ast
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@en
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@nl
type
label
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@ast
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@en
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@nl
prefLabel
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@ast
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@en
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@nl
P2093
P2860
P3181
P1476
The CaaX proteases, Afc1p and ...... tinct substrate specificities.
@en
P2093
C D Poulter
C E Trueblood
E A Picologlou
V L Boyartchuk
P2860
P304
P3181
P356
10.1128/MCB.20.12.4381-4392.2000
P407
P577
2000-06-01T00:00:00Z