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Article ; Online: Accurate H3K27 methylation can be established de novo by SUZ12-directed PRC2.

Højfeldt, Jonas W / Laugesen, Anne / Willumsen, Berthe M / Damhofer, Helene / Hedehus, Lin / Tvardovskiy, Andrey / Mohammad, Faizaan / Jensen, Ole N / Helin, Kristian

Nature structural & molecular biology

2018 Volume 25, Issue 3, Page(s) 225–232

Abstract: Polycomb repressive complex 2 (PRC2) catalyzes methylation on lysine 27 of histone H3 (H3K27) and is required for maintaining transcriptional patterns and cellular identity, but the specification and maintenance of genomic PRC2 binding and H3K27 ... ...

Abstract	Polycomb repressive complex 2 (PRC2) catalyzes methylation on lysine 27 of histone H3 (H3K27) and is required for maintaining transcriptional patterns and cellular identity, but the specification and maintenance of genomic PRC2 binding and H3K27 methylation patterns remain incompletely understood. Epigenetic mechanisms have been proposed, wherein pre-existing H3K27 methylation directs recruitment and regulates the catalytic activity of PRC2 to support its own maintenance. Here we investigate whether such mechanisms are required for specifying H3K27 methylation patterns in mouse embryonic stem cells (mESCs). Through re-expression of PRC2 subunits in PRC2-knockout cells that have lost all H3K27 methylation, we demonstrate that methylation patterns can be accurately established de novo. We find that regional methylation kinetics correlate with original methylation patterns even in their absence, and specification of the genomic PRC2 binding pattern is retained and specifically dependent on the PRC2 core subunit SUZ12. Thus, the H3K27 methylation patterns in mESCs are not dependent on self-autonomous epigenetic inheritance.
MeSH term(s)	Animals ; Cells, Cultured ; CpG Islands ; Embryonic Stem Cells/metabolism ; Histones/metabolism ; Kinetics ; Methylation ; Mice ; Polycomb Repressive Complex 2/metabolism
Chemical Substances	Histones ; Suz12 protein, mouse ; Polycomb Repressive Complex 2 (EC 2.1.1.43)
Language	English
Publishing date	2018-02-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-018-0036-6
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Zs.A 4101: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 56: Show issues

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Article: High-density growth arrest in Ras-transformed cells: low Cdk kinase activities in spite of absence of p27(Kip) Cdk-complexes.

Groth, Anja / Willumsen, Berthe M

Cellular signalling

2005 Volume 17, Issue 9, Page(s) 1063–1073

Abstract: The ras oncogene transforms immortalized, contact-inhibited non-malignant murine fibroblasts into cells that are focus forming, exhibit increased saturation density, and are malignant in suitable hosts. Here, we examined changes in cell cycle control ... ...

Abstract	The ras oncogene transforms immortalized, contact-inhibited non-malignant murine fibroblasts into cells that are focus forming, exhibit increased saturation density, and are malignant in suitable hosts. Here, we examined changes in cell cycle control complexes as normal and Ras-transformed cells ceased to grow exponentially, to reveal the molecular basis for Ras-dependent focus formation. As normal cells entered density-dependent arrest, cyclin D1 decreased while cyclin D2 was induced and replaced D1 in Cdk4 complexes. Concomitantly, p27(Kip1) levels rose and the inhibitor accumulated in both Cdk4 and Cdk2 complexes, as these kinases were inactivated. Ras-transformed cells failed to arrest at normal saturation density and showed no significant alterations in cell control complexes at this point. Yet, at an elevated density the Ras-transformed cells ceased to proliferate and entered a quiescent-like state with low Cdk4 and Cdk2 activity. Surprisingly, this delayed arrest was molecularly distinct from contact inhibition of normal cells, as it occurred in the absence of p27(Kip1) induction and cyclin D1 levels remained high. This demonstrates that although oncogenic Ras efficiently disabled the normal response to contact inhibition, a separate back-up mechanism enforced cell cycle arrest at higher cell density.
MeSH term(s)	Animals ; CDC2-CDC28 Kinases/metabolism ; Cell Cycle Proteins/metabolism ; Cell Line, Transformed ; Cell Proliferation ; Contact Inhibition ; Cyclin D1/metabolism ; Cyclin D2 ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p27 ; Cyclin-Dependent Kinases/metabolism ; Cyclins/metabolism ; Mice ; NIH 3T3 Cells ; Oncogene Protein p21(ras)/metabolism ; Proto-Oncogene Proteins/metabolism ; Retinoblastoma Protein/metabolism ; Tumor Suppressor Proteins/metabolism
Chemical Substances	Ccnd2 protein, mouse ; Cdkn1b protein, mouse ; Cell Cycle Proteins ; Cyclin D2 ; Cyclins ; Proto-Oncogene Proteins ; Retinoblastoma Protein ; Tumor Suppressor Proteins ; Cyclin D1 (136601-57-5) ; Cyclin-Dependent Kinase Inhibitor p27 (147604-94-2) ; CDC2-CDC28 Kinases (EC 2.7.11.22) ; Cdk2 protein, mouse (EC 2.7.11.22) ; Cdk4 protein, mouse (EC 2.7.11.22) ; Cyclin-Dependent Kinase 2 (EC 2.7.11.22) ; Cyclin-Dependent Kinase 4 (EC 2.7.11.22) ; Cyclin-Dependent Kinases (EC 2.7.11.22) ; Oncogene Protein p21(ras) (EC 3.6.5.2)
Language	English
Publishing date	2005-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1002702-6
ISSN	0898-6568
ISSN	0898-6568
DOI	10.1016/j.cellsig.2004.11.021
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Article: Ras-inducible immortalized fibroblasts: focus formation without cell cycle deregulation.

Jacobsen, Kivin / Groth, Anja / Willumsen, Berthe M

Oncogene

2002 Volume 21, Issue 19, Page(s) 3058–3067

Abstract: The Ras oncogene transforms cultured murine fibroblasts into malignant, focus-forming cells, whose lack of contact inhibition is evidenced by high saturation densities. In order to investigate the reversibility of Ras transformation, as well as the ... ...

Abstract	The Ras oncogene transforms cultured murine fibroblasts into malignant, focus-forming cells, whose lack of contact inhibition is evidenced by high saturation densities. In order to investigate the reversibility of Ras transformation, as well as the kinetics of Ras-induced changes, cell lines that conditionally express oncogenic Ras were constructed. Both focus formation and increased saturation density were inducible and fully reversible. In exponentially growing cells, oncogenic Ras-expression had no effect on proliferation rates, Erk phosphorylation, or the level of cyclin D1, and Ras-induction did not confer serum-independent growth. As expected, growth to high density in uninduced cells led to quiescence with a low level of cyclin D1 and no active Erk; in this setting, Ras induction prevented full downregulation of cyclin D1 and inactivation of Erk. Our results show that Ras expression to a level sufficient for transformation leads to relatively subtle effects on known downstream targets, and that the focus formation and increased saturation density growth induced by Ras is not a result of growth factor independence.
MeSH term(s)	3T3 Cells/cytology ; Animals ; Cell Cycle ; Cell Division ; Cell Line, Transformed/cytology ; Cell Transformation, Viral/genetics ; Colony-Forming Units Assay ; Culture Media, Serum-Free/pharmacology ; Cyclin D1/biosynthesis ; Cyclin D1/physiology ; Genes, Viral ; Genes, ras ; MAP Kinase Signaling System ; Mice ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Oncogene Protein p21(ras)/physiology ; Phosphorylation ; Protein Processing, Post-Translational ; Recombinant Fusion Proteins/physiology ; Signal Transduction ; Transfection
Chemical Substances	Culture Media, Serum-Free ; Recombinant Fusion Proteins ; Cyclin D1 (136601-57-5) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Oncogene Protein p21(ras) (EC 3.6.5.2)
Language	English
Publishing date	2002-05-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/sj.onc.1205423
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Zs.A 2218: Show issues

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Article: EGFRvIII escapes down-regulation due to impaired internalization and sorting to lysosomes.

Grandal, Michael V / Zandi, Roza / Pedersen, Mikkel W / Willumsen, Berthe M / van Deurs, Bo / Poulsen, Hans S

Carcinogenesis

2007 Volume 28, Issue 7, Page(s) 1408–1417

Abstract: EGFRvIII is a mutant variant of the epidermal growth factor receptor (EGFR) found exclusively in various cancer types. EGFRvIII lacks a large part of the extracellular domain and is unable to bind ligands; however, the receptor is constitutively ... ...

Abstract	EGFRvIII is a mutant variant of the epidermal growth factor receptor (EGFR) found exclusively in various cancer types. EGFRvIII lacks a large part of the extracellular domain and is unable to bind ligands; however, the receptor is constitutively phosphorylated and able to activate downstream signaling pathways. Failure to attenuate signaling by receptor down-regulation could be one of the major mechanisms by which EGFRvIII becomes oncogenic. Using a cell system expressing either EGFR or EGFRvIII with no expression of other EGFR family members and with endogenous levels of key degradation proteins, we have investigated the down-regulation of EGFRvIII and compared it to that of EGFR. We show that, in contrast to EGFR, EGFRvIII is inefficiently degraded. EGFRvIII is internalized, but the internalization rate of the mutated receptor is significantly less than that of unstimulated EGFR. Moreover, internalized EGFRvIII is recycled rather than delivered to lysosomes. EGFRvIII binds the ubiquitin ligase c-Cbl via Grb2, whereas binding via phosphorylated tyrosine residue 1045 seems to be limited. Despite c-Cbl binding, the receptor fails to become effectively ubiquitinylated. Thus, our results suggest that the long lifetime of EGFRvIII is caused by inefficient internalization and impaired sorting to lysosomes due to lack of effective ubiquitinylation.
MeSH term(s)	Cell Line, Tumor ; Cell Membrane/metabolism ; Down-Regulation ; Endocytosis ; Epidermal Growth Factor/pharmacology ; GRB2 Adaptor Protein/metabolism ; Humans ; Lysosomes/metabolism ; Phosphorylation ; Protein Transport ; Proto-Oncogene Proteins c-cbl/metabolism ; Receptor, Epidermal Growth Factor/biosynthesis ; Receptor, Epidermal Growth Factor/genetics ; Signal Transduction ; Ubiquitins/metabolism
Chemical Substances	GRB2 Adaptor Protein ; Ubiquitins ; epidermal growth factor receptor VIII ; Epidermal Growth Factor (62229-50-9) ; Proto-Oncogene Proteins c-cbl (EC 2.3.2.27) ; Receptor, Epidermal Growth Factor (EC 2.7.10.1)
Language	English
Publishing date	2007-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603134-1
ISSN	1460-2180 ; 0143-3334
ISSN (online)	1460-2180
ISSN	0143-3334
DOI	10.1093/carcin/bgm058
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Zs.A 1558: Show issues

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Article: Suppression of integrin activation by activated Ras or Raf does not correlate with bulk activation of ERK MAP kinase.

Hughes, Paul E / Oertli, Beat / Hansen, Malene / Chou, Fan-Li / Willumsen, Berthe M / Ginsberg, Mark H

Molecular biology of the cell

2002 Volume 13, Issue 7, Page(s) 2256–2265

Abstract: The rapid modulation of ligand-binding affinity ("activation") is a central property of the integrin family of cell adhesion receptors. The Ras family of small GTP-binding proteins and their downstream effectors are key players in regulating integrin ... ...

Abstract	The rapid modulation of ligand-binding affinity ("activation") is a central property of the integrin family of cell adhesion receptors. The Ras family of small GTP-binding proteins and their downstream effectors are key players in regulating integrin activation. H-Ras can suppress integrin activation in fibroblasts via its downstream effector kinase, Raf-1. In contrast, to H-Ras, a closely related small GTP-binding protein R-Ras has the opposite activity, and promotes integrin activation. To gain insight into the regulation of integrin activation by Ras GTPases, we created a series of H-Ras/R-Ras chimeras. We found that a 35-amino acid stretch of H-Ras was required for full suppressive activity. Furthermore, the suppressive chimeras were weak activators of the ERK1/2 MAP kinase pathway, suggesting that the suppression of integrin activation may be independent of the activation of the bulk of ERK MAP kinase. Additional data demonstrating that the ability of H-Ras or Raf-1 to suppress integrin activation was unaffected by inhibition of bulk ERK1/2 MAP kinase activation supported this hypothesis. Thus, the suppression of integrin activation is a Raf kinase induced regulatory event that can be mediated independently of bulk activation of the ERK MAP-kinase pathway.
MeSH term(s)	Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/metabolism ; CHO Cells ; Cricetinae ; Enzyme Activation ; Flow Cytometry ; Integrin alpha5beta1/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; Platelet Glycoprotein GPIIb-IIIa Complex/metabolism ; Proto-Oncogene Proteins c-raf/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; ras Proteins/metabolism
Chemical Substances	Antibodies, Monoclonal ; Integrin alpha5beta1 ; Platelet Glycoprotein GPIIb-IIIa Complex ; Recombinant Fusion Proteins ; Proto-Oncogene Proteins c-raf (EC 2.7.11.1) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2002-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.01-10-0480
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: C-terminal sequences in R-Ras are involved in integrin regulation and in plasma membrane microdomain distribution.

Hansen, Malene / Prior, Ian A / Hughes, Paul E / Oertli, Beat / Chou, Fan-Li / Willumsen, Berthe M / Hancock, John F / Ginsberg, Mark H

Biochemical and biophysical research communications

2003 Volume 311, Issue 4, Page(s) 829–838

Abstract: The small GTPases R-Ras and H-Ras are highly homologous proteins with contrasting biological properties, for example, they differentially modulate integrin affinity: H-Ras suppresses integrin activation in fibroblasts whereas R-Ras can reverse this ... ...

Abstract	The small GTPases R-Ras and H-Ras are highly homologous proteins with contrasting biological properties, for example, they differentially modulate integrin affinity: H-Ras suppresses integrin activation in fibroblasts whereas R-Ras can reverse this effect of H-Ras. To gain insight into the sequences directing this divergent phenotype, we investigated a panel of H-Ras/R-Ras chimeras and found that sequences in the R-Ras hypervariable C-terminal region including amino acids 175-203 are required for the R-Ras ability to increase integrin activation in CHO cells; however, the proline-rich site in this region, previously reported to bind the adaptor protein Nck, was not essential for this effect. In addition, we found that the GTPase TC21 behaved similarly to R-Ras. Because the C-termini of Ras proteins can control their subcellular localization, we compared the localization of H-Ras and R-Ras. In contrast to H-Ras, which migrates out of lipid rafts upon activation, we found that activated R-Ras remained localized to lipid rafts. However, functionally distinct H-Ras/R-Ras chimeras containing different C-terminal R-Ras segments localized to lipid rafts irrespective of their integrin phenotype.
MeSH term(s)	Amino Acid Sequence ; Animals ; CHO Cells ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Chimera/metabolism ; Cricetinae ; Cricetulus ; GTP Phosphohydrolases/chemistry ; GTP Phosphohydrolases/classification ; GTP Phosphohydrolases/metabolism ; Homeostasis/physiology ; Integrins/metabolism ; Kidney/metabolism ; Membrane Microdomains/metabolism ; Molecular Sequence Data ; Protein Structure, Tertiary ; Species Specificity ; Structure-Activity Relationship ; ras Proteins/chemistry ; ras Proteins/classification ; ras Proteins/metabolism
Chemical Substances	Integrins ; GTP Phosphohydrolases (EC 3.6.1.-) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2003-11-04
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2003.10.074
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Zs.A 116: Show issues

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Article: Rho family GTP binding proteins are involved in the regulatory volume decrease process in NIH3T3 mouse fibroblasts.

Pedersen, Stine F / Beisner, Kristine H / Hougaard, Charlotte / Willumsen, Berthe M / Lambert, Ian H / Hoffmann, Else K

The Journal of physiology

2002 Volume 541, Issue Pt 3, Page(s) 779–796

Abstract: The role of Rho GTPases in the regulatory volume decrease (RVD) process following osmotic cell swelling is controversial and has so far only been investigated for the swelling-activated Cl- efflux. We investigated the involvement of RhoA in the RVD ... ...

Abstract	The role of Rho GTPases in the regulatory volume decrease (RVD) process following osmotic cell swelling is controversial and has so far only been investigated for the swelling-activated Cl- efflux. We investigated the involvement of RhoA in the RVD process in NIH3T3 mouse fibroblasts, using wild-type cells and three clones expressing constitutively active RhoA (RhoAV14). RhoAV14 expression resulted in an up to fourfold increase in the rate of RVD, measured by large-angle light scattering. The increase in RVD rate correlated with RhoAV14 expression. RVD in wild-type cells was unaffected by the Rho kinase inhibitor Y-27632 and the phosphatidyl-inositol 3 kinase (PI3K) inhibitor wortmannin. The maximal rates of swelling-activated K+ (86 Rb+ as tracer) and taurine ([3H]taurine as tracer) efflux after a 30 % reduction in extracellular osmolarity were increased about twofold in cells with maximal RhoAV14 expression compared to wild-type cells, but were unaffected by Y-27632. The volume set points for activation of release of both osmolytes appeared to be reduced by RhoAV14 expression. The maximal taurine efflux rate constant was potentiated by the tyrosine phosphatase inhibitor Na(3)VO(4), and inhibited by the tyrosine kinase inhibitor genistein. The magnitude of the swelling-activated Cl- current (I(Cl,swell) ) was higher in RhoAV14 than in wild-type cells after a 7.5 % reduction in extracellular osmolarity, but, in contrast to 86Rb+ and [3H]taurine efflux, similar in both strains after a 30 % reduction in extracellular osmolarity. I(Cl,swell) was inhibited by Y-27632 and strongly potentiated by the myosin light chain kinase inhibitors ML-7 and AV25. It is suggested that RhoA, although not the volume sensor per se, is an important upstream modulator shared by multiple swelling-activated channels on which RhoA exerts its effects via divergent signalling pathways.
MeSH term(s)	3T3 Cells ; Actins/metabolism ; Amides/pharmacology ; Animals ; Blotting, Western ; Cell Size/physiology ; Chloride Channel Agonists ; Chloride Channels/antagonists & inhibitors ; Chloride Channels/physiology ; Enzyme Inhibitors/pharmacology ; Fibroblasts/physiology ; Light ; Mice ; Potassium Channel Blockers/pharmacology ; Potassium Channels/agonists ; Potassium Channels/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors ; Protein-Tyrosine Kinases/metabolism ; Pyridines/pharmacology ; Rubidium ; Scattering, Radiation ; Signal Transduction/physiology ; Taurine/metabolism ; Transfection ; rho GTP-Binding Proteins/drug effects ; rho GTP-Binding Proteins/physiology
Chemical Substances	Actins ; Amides ; Chloride Channel Agonists ; Chloride Channels ; Enzyme Inhibitors ; Potassium Channel Blockers ; Potassium Channels ; Pyridines ; Y 27632 (138381-45-0) ; Taurine (1EQV5MLY3D) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; rho GTP-Binding Proteins (EC 3.6.5.2) ; Rubidium (MLT4718TJW)
Language	English
Publishing date	2002-06-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/jphysiol.2002.018887
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Article: R-Ras C-terminal sequences are sufficient to confer R-Ras specificity to H-Ras.

Hansen, Malene / Rusyn, Elena V / Hughes, Paul E / Ginsberg, Mark H / Cox, Adrienne D / Willumsen, Berthe M

Oncogene

2002 Volume 21, Issue 28, Page(s) 4448–4461

Abstract: Activated versions of the similar GTPases, H-Ras and R-Ras, have differing effects on biological phenotypes: Activated H-Ras strongly transforms many fibroblast cell lines causing dramatic changes in cell shape and cytoskeletal organization. In contrast, ...

Abstract	Activated versions of the similar GTPases, H-Ras and R-Ras, have differing effects on biological phenotypes: Activated H-Ras strongly transforms many fibroblast cell lines causing dramatic changes in cell shape and cytoskeletal organization. In contrast, R-Ras transforms fewer cell lines and the transformed cells display only some of the morphological changes associated with H-Ras transformation. H-Ras cells can survive in the absence of serum whereas R-Ras cells seem to die by an apoptotic-like mechanism in response to removal of serum. H-Ras can suppress integrin activation and R-Ras specifically antagonizes this effect. To map sequences responsible for these differences we have generated and investigated a panel of H-Ras and R-Ras chimeras. We found that the C-terminal 53 amino acids of R-Ras were necessary and sufficient to specify the contrasting biological properties of R-Ras with respect to focus morphology, reactive oxygen species (ROS) production and reversal of H-Ras-induced integrin suppression. Surprisingly, we found chimeras in which the focus formation and integrin-mediated phenotypes were separated, suggesting that different effectors could be involved in mediating these responses. An integrin profile of H-Ras and R-Ras cell pools showed no significant differences; both activated H-Ras and R-Ras expressing cells were found to have reduced beta(1) activity, suggesting that the activity state of the beta(1) subunit is not sufficient to direct an H-Ras transformed cell morphology.
MeSH term(s)	3T3 Cells ; Amino Acid Sequence ; Animals ; CHO Cells ; Cricetinae ; Fibronectins/metabolism ; GTP Phosphohydrolases/physiology ; Gene Deletion ; Genes, ras/physiology ; Luciferases/metabolism ; Mice ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; Plasmids ; Reactive Oxygen Species ; Recombinant Fusion Proteins/genetics ; Signal Transduction ; Structure-Activity Relationship ; Transfection ; ras Proteins/physiology
Chemical Substances	Fibronectins ; Reactive Oxygen Species ; Recombinant Fusion Proteins ; Luciferases (EC 1.13.12.-) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; GTP Phosphohydrolases (EC 3.6.1.-) ; Rras protein, mouse (EC 3.6.1.-) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2002-06-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/sj.onc.1205538
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