(Q57007437)

English

Synthesis of characteristic lipopeptides of the human N-Ras protein and their evaluation as possible inhibitors of protein farnesyl transferase

scientific article published on 01 January 1997

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scholarly article

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1 November 2019

Synthesis of characteristic lipopeptides of the human N-Ras protein and their evaluation as possible inhibitors of protein farnesyl transferase (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9043659%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

Herbert Waldmann

6

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1 November 2019

author name string

P Stöber

1

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1 November 2019

M Schelhaas

2

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1 November 2019

E Nägele

3

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1 November 2019

P Hagenbuch

4

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1 November 2019

J Rétey

5

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1 November 2019

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1 January 1997

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1 November 2019

Bioorganic & Medicinal Chemistry

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1 November 2019

5

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1 November 2019

1

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1 November 2019

75-83

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1 November 2019

The pathway to signal achievement

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A biochemical function for ras--at last

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Farnesyl transferase inhibitors: the successes and surprises of a new class of potential cancer chemotherapeutics

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Development of highly potent inhibitors of Ras farnesyltransferase possessing cellular and in vivo activity.

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Potent, cell active, non-thiol tetrapeptide inhibitors of farnesyltransferase.

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Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice

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Steady-state kinetic mechanism of Ras farnesyl:protein transferase

1 reference

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7 January 2021

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Synthesis of the Palmitoylated and Farnesylated C-Terminal Lipohexapeptide of the Human N-Ras Protein by Employing an Enzymatically Removable Urethane Protecting Group

1 reference

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7 January 2021

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Enzymatic Synthesis of Peptides andRas Lipopeptides Employing Choline Ester as a Solubilizing, Protecting, and Activating Group

1 reference

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7 January 2021

based on heuristic

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All ras proteins are polyisoprenylated but only some are palmitoylated

1 reference

https://api.crossref.org/works/10.1016%2FS0968-0896%2896%2900213-1

7 January 2021

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Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart.

1 reference

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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Farnesyl-protein transferase and geranylgeranyl-protein transferase assays using phosphocellulose paper absorption

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Assay of proteins in the presence of interfering materials

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Detergent-solubilization, purification, and characterization of membrane-bound 3-hydroxy-3-methylglutaryl-coenzyme A reductase from radish seedlings

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Identifiers

10.1016/S0968-0896(96)00213-1

1 reference

Europe PubMed Central

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1 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9043659%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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