About: Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases

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About: Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases Goto Sponge NotDistinct Permalink

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1993 (ast) vědecký článek publikovaný v roce 1993 (cs) 1993 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в травні 1993 (uk) 1993 թվականի մայիսին հրատարակված գիտական հոդված (hy) article scientifique publié en 1993 (fr) scientific journal article (en) im Mai 1993 veröffentlicher wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1993/05/18) (nl) vedecký článok (publikovaný 1993/05/18) (sk) مقالة علمية (نشرت في 18-5-1993) (ar)
publication date	wds:Q28116052-5B6EFA98-72A9-4EFD-88CD-8B77F48FCF41
publication date	1993-05-18 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28116052-CFC78B9D-72A5-4745-B825-FE252B9832B7
language of work or name	English
author name string	wds:Q28116052-0CEF2939-0768-4A51-A0BB-E84801E4C3B8 wds:Q28116052-11872464-A7F7-40CF-80E9-A613B4056D4F wds:Q28116052-24E42A70-129D-48B0-BE8F-AA35C0ABEA22 wds:Q28116052-437DFAD5-F20A-472F-9843-7AD1538E9F89 wds:Q28116052-7DA58453-3148-48C6-BC8F-DB9BDF9E565B wds:Q28116052-CE8532B6-10E2-4F70-A2C0-596DF9355BFB wds:Q28116052-D3E3425D-C967-4EBA-BF5A-F339D7D3E117 wds:Q28116052-D8B2D97C-C6E8-46B1-9BA7-6ACE226F737D
OpenCitations bibliographic resource ID	wds:Q28116052-735DCD16-907B-4698-885C-35ED51DB5823
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/2627013
author name string	J. B. Gibbs G. C. Prendergast C. M. Allen S. Powers C. A. Omer R. E. Diehl A. M. Kral N. E. Kohl
OpenCitations bibliographic resource ID	2627013
rdfs:label	Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (en) Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (nl) Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (ast)
skos:prefLabel	Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (en) Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (nl) Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (ast)
name	Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (en) Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (nl) Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (ast)
title	wds:Q28116052-4A3F7B91-35C0-411D-84A6-D26913ECBB38
title	Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases (en)
page(s)	wds:Q28116052-84BD0D5E-B03F-45E7-8DA9-AB6AC7A2176A
page(s)	5167–5176
instance of	wds:Q28116052-FAB075B8-0919-4A4C-B183-D5918500D0A0
instance of	scholarly article
PubMed ID	wds:Q28116052-8F071879-8B75-4D6A-AF70-718B6911EB51
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8494894
PubMed ID	8494894
published in	wds:Q28116052-DD0E71C5-E691-41EA-8FB5-068C85DF820B
published in	Biochemistry
issue	wds:Q28116052-E33BCC42-C796-470D-8182-641E2F0BA80D
volume	wds:Q28116052-666A7336-A9C8-4090-AEE8-B3E08A295B39
issue	19
volume	32
DOI	wds:Q28116052-E91011A1-118B-40CB-A07D-5A7265A3E2EC
DOI	http://dx.doi.org/10.1021/BI00070A028
DOI	10.1021/BI00070A028
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28116052
is cites work of	Context-dependent substrate recognition by protein farnesyltransferase. Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase Amino acid substitutions that convert the protein substrate specificity of farnesyltransferase to that of geranylgeranyltransferase type I. Resistance to a protein farnesyltransferase inhibitor in Plasmodium falciparum Novel tricyclic inhibitors of farnesyl protein transferase. Biochemical characterization and inhibition of Ras modification in transfected Cos cells Protein prenylation in eukaryotic microorganisms: genetics, biology and biochemistry A minimalist substrate for enzymatic peptide and protein conjugation. Protein prenyltransferases Prenylation of Ras GTPase superfamily proteins and their function in immunobiology. Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation Farnesyltransferase inhibitors and anti-Ras therapy Probing the hydrophobic pocket of farnesyltransferase: aromatic substitution of CAAX peptidomimetics leads to highly potent inhibitors The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I Single prenyl-binding site on protein prenyl transferases Farnesyltransferase inhibitors: targeting the molecular basis of cancer Protein prenylation: enzymes, therapeutics, and biotechnology applications Disruption of oncogenic K-Ras4B processing and signaling by a potent geranylgeranyltransferase I inhibitor Expression and characterization of protein geranylgeranyltransferase type I from the pathogenic yeast Candida albicans and identification of yeast selective enzyme inhibitors Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities src-homology 2 (SH2) domain ligation as an allosteric regulator: modulation of phosphoinositide-specific phospholipase C gamma 1 structure and activity Investigation of S-farnesyl transferase substrate specificity with combinatorial tetrapeptide libraries. A novel subtype of G-protein-coupled receptor kinase, GRK7, in teleost cone photoreceptors. Enzyme-catalyzed methyl transfers to thiols: the role of zinc. Identification of a cysteine residue essential for activity of protein farnesyltransferase. Cys299 is exposed only upon removal of zinc from the enzyme. Mutational analysis of conserved residues of the beta-subunit of human farnesyl:protein transferase Protein farnesyltransferase from Trypanosoma brucei. A heterodimer of 61- and 65-kda subunits as a new target for antiparasite therapeutics Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice Synthesis, Properties, and Applications of Diazotrifluropropanoyl-Containing Photoactive Analogs of Farnesyl Diphosphate Containing Modified Linkages for Enhanced Stability Synthesis of a-factor peptide from Saccharomyces cerevisiae and photoactive analogues via Fmoc solid phase methodology A photoactive isoprenoid diphosphate analogue containing a stable phosphonate linkage: synthesis and biochemical studies with prenyltransferases A versatile photoactivatable probe designed to label the diphosphate binding site of farnesyl diphosphate utilizing enzymes The farnesyltransferase inhibitor manumycin A is a novel trypanocide with a complex mode of action including major effects on mitochondria. Fusidienol: A novel inhibitor of Ras farnesyl-protein transferase from Fusidium griseum Kampanols: novel Ras farnesyl-protein transferase inhibitors from Stachybotrys kampalensis A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase

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