(Q41126022)

27 September 2017

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title

Farnesyltransferase inhibitors and anti-Ras therapy (English)

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27 September 2017

5

L Sepp-Lorenzino

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27 September 2017

J B Gibbs

1

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27 September 2017

N E Kohl

2

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27 September 2017

K S Koblan

3

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27 September 2017

C A Omer

4

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27 September 2017

N Rosen

6

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27 September 2017

N J Anthony

7

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27 September 2017

M W Conner

8

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27 September 2017

S J deSolms

9

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27 September 2017

T M Williams

10

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27 September 2017

S L Graham

11

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27 September 2017

G D Hartman

12

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27 September 2017

A Oliff

13

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27 September 2017

language of work or name

English

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publication date

1 January 1996

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Breast Cancer Research and Treatment

27 September 2017

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27 September 2017

38

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27 September 2017

75-83

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27 September 2017

1

1 reference

https://scigraph.springernature.com/pub.10.1007/bf01803786

27 September 2017

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cites work

Farnesyltransferase inhibition causes morphological reversion of ras-transformed cells by a complex mechanism that involves regulation of the actin cytoskeleton

1 reference

Crossref

https://api.crossref.org/works/10.1007%2FBF01803786

Pathways of Ras function: connections to the actin cytoskeleton.

21 January 2018

1 reference

12 December 2020

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

1 reference

12 December 2020

Altered growth of human colon cancer cell lines disrupted at activated Ki-ras

1 reference

12 December 2020

PxF, a prenylated protein of peroxisomes.

1 reference

12 December 2020

Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro

1 reference

12 December 2020

Protein prenylation: more than just glue?

1 reference

12 December 2020

Pseudopeptide inhibitors of Ras farnesyl-protein transferase

1 reference

12 December 2020

Activators and effectors of ras p21 proteins

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12 December 2020

Regulators and Effectors of ras Proteins

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12 December 2020

Protein isoprenylation and methylation at carboxyl-terminal cysteine residues

1 reference

12 December 2020

Phosphinyl acid-based bisubstrate analog inhibitors of Ras farnesyl protein transferase

1 reference

12 December 2020

Identification of Ras farnesyltransferase inhibitors by microbial screening

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12 December 2020

Inhibitors of Ras farnesyltransferases

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12 December 2020

Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice

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12 December 2020

Function and regulation of ras.

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12 December 2020

Selective inhibition of farnesyl-protein transferase blocks ras processing in vivo.

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12 December 2020

Steady-state kinetic mechanism of Ras farnesyl:protein transferase

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12 December 2020

Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor

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12 December 2020

Ras C-terminal processing enzymes--new drug targets?

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12 December 2020

Phosphatidylinositol-3-OH kinase as a direct target of Ras

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12 December 2020

Pharmacological probes of Ras function

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12 December 2020

Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells

1 reference

12 December 2020

Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic

1 reference

12 December 2020

Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions.

1 reference

12 December 2020

Structural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target

1 reference

12 December 2020

SH2 and SH3 domains: from structure to function

1 reference

12 December 2020

High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc.

1 reference

12 December 2020

The structure of Ras protein: a model for a universal molecular switch

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF01803786

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Dimensions Publication ID

27 September 2017

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1 reference