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Targeting of K-Ras 4B by S-trans,trans-farnesyl thiosalicylic acid
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title
Targeting of K-Ras 4B by S-trans,trans-farnesyl thiosalicylic acid
(English)
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author name string
G Elad
series ordinal
1
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A Paz
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2
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R Haklai
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3
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D Marciano
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4
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A Cox
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5
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Y Kloog
series ordinal
6
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language of work or name
English
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publication date
9 December 1999
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published in
Biochimica et Biophysica Acta
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volume
1452
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issue
3
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page(s)
228-42
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cites work
Proteins regulating Ras and its relatives
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Ras-dependent growth factor regulation of MEK kinase in PC12 cells
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Function and regulation of ras.
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Ras effectors
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Ras signaling in tumor necrosis factor-induced apoptosis.
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ras genes
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p21ras: An oncoprotein functioning in growth factor-induced signal transduction
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants
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p21ras is modified by a farnesyl isoprenoid
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A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins.
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All ras proteins are polyisoprenylated but only some are palmitoylated
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Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity
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Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein
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Lipid-binding characteristics of the polybasic carboxy-terminal sequence of K-ras4B
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Unexpectedly strong binding of a large metal ion (Bi3+) to human serum transferrin
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Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
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Functional rafts in cell membranes
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Reduction of caveolin and caveolae in oncogenically transformed cells
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Farnesyl derivatives of rigid carboxylic acids-inhibitors of ras-dependent cell growth
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Selective inhibition of Ras-dependent cell growth by farnesylthiosalisylic acid
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Dislodgment and accelerated degradation of Ras.
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7 January 2021
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Stringent structural requirements for anti-Ras activity of S-prenyl analogues
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro.
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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Characterization of Ha-ras, N-ras, Ki-Ras4A, and Ki-Ras4B as in vitro substrates for farnesyl protein transferase and geranylgeranyl protein transferase type I
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K- and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors
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Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
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Farnesol modification of Kirsten-ras exon 4B protein is essential for transformation
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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Mutation and analysis of prenylation signal sequences
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Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation
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How MAP kinases are regulated
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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7 January 2021
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The Ras antagonist S-farnesylthiosalicylic acid induces inhibition of MAPK activation
1 reference
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells
1 reference
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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7 January 2021
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inferred from DOI database lookup
Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor
1 reference
stated in
Crossref
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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7 January 2021
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A new functional Ras antagonist inhibits human pancreatic tumor growth in nude mice
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Evidence for a high affinity, saturable, prenylation-dependent p21Ha-ras binding site in plasma membranes
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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Membrane interactions of a constitutively active GFP-Ki-Ras 4B and their role in signaling. Evidence from lateral mobility studies.
1 reference
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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GM3-enriched Microdomain Involved in Cell Adhesion and Signal Transduction through Carbohydrate-Carbohydrate Interaction in Mouse Melanoma B16 Cells
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Modulation of phagosome biogenesis by Legionella pneumophila creates an organelle permissive for intracellular growth
1 reference
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Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
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https://api.crossref.org/works/10.1016%2FS0167-4889%2899%2900144-5
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Identifiers
DOI
10.1016/S0167-4889(99)00144-5
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PubMed publication ID
10590312
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ResearchGate publication ID
12711656
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