The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: development of novel inhibitors.
about
Small-molecule inhibitors of the Rce1p CaaX proteaseChemical inhibition of CaaX protease activity disrupts yeast Ras localization.Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation.Amide-substituted farnesylcysteine analogs as inhibitors of human isoprenylcysteine carboxyl methyltransferase.Therapeutic intervention based on protein prenylation and associated modificationsAmide-modified prenylcysteine based Icmt inhibitors: Structure-activity relationships, kinetic analysis and cellular characterizationPrelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.Quantitative structure-activity relationship (QSAR) of indoloacetamides as inhibitors of human isoprenylcysteine carboxyl methyltransferase.Synthesis of desthio prenylcysteine analogs: sulfur is important for biological activityA potent HIV protease inhibitor, darunavir, does not inhibit ZMPSTE24 or lead to an accumulation of farnesyl-prelamin A in cells.Inactivating Icmt ameliorates K-RAS-induced myeloproliferative disease.Solid-phase synthesis of prenylcysteine analogsHeterologous expression studies of Saccharomyces cerevisiae reveal two distinct trypanosomatid CaaX protease activities and identify their potential targets.Diazirine-containing photoactivatable isoprenoid: synthesis and application in studies with isoprenylcysteine carboxyl methyltransferaseIsoprenyl carboxyl methyltransferase inhibitors: a brief review including recent patents.Evaluation of substrate and inhibitor binding to yeast and human isoprenylcysteine carboxyl methyltransferases (Icmts) using biotinylated benzophenone-containing photoaffinity probes.Lipid and sulfur substituted prenylcysteine analogs as human Icmt inhibitors.Functional oligomerization of the Saccharomyces cerevisiae isoprenylcysteine carboxyl methyltransferase, Ste14p.S-Farnesyl-Thiopropionic Acid (FTPA) Triazoles as Potent Inhibitors of Isoprenylcysteine Carboxyl Methyltransferase.Mutational analysis of the integral membrane methyltransferase isoprenylcysteine carboxyl methyltransferase (ICMT) reveals potential substrate binding sites.Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT.
P2860
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P2860
The isoprenoid substrate specificity of isoprenylcysteine carboxylmethyltransferase: development of novel inhibitors.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@ast
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@en
type
label
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@ast
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@en
prefLabel
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@ast
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@en
P2093
P2860
P356
P1476
The isoprenoid substrate speci ...... velopment of novel inhibitors.
@en
P2093
Brian S Henriksen
Christine A Hrycyna
Jessica L Anderson
Richard A Gibbs
P2860
P304
29454-29461
P356
10.1074/JBC.M504982200
P407
P577
2005-06-09T00:00:00Z