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Dive into the research topics where Gerben C. M. Zondag is active.

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Featured researches published by Gerben C. M. Zondag.


Current Opinion in Cell Biology | 1997

Lysophosphatidic acid: G-protein signalling and cellular responses

Wouter H. Moolenaar; Onno Kranenburg; Friso R. Postma; Gerben C. M. Zondag

Lysophosphatidic acid (LPA) is a serum-borne phospholipid that activates a specific G protein coupled receptor to evoke multiple cellular responses. Recent work has identified two cDNAs encoding putative LPA receptors, various LPA-like agonists that act on distinct receptors, and new pathways that link the receptor(s) to such diverse events as Ras signalling, cytoskeletal remodelling and membrane depolarization.


European Journal of Cancer | 2000

Rho family proteins in cell adhesion and cell migration

Eva E. Evers; Gerben C. M. Zondag; Angeliki Malliri; L.S Price; J.-P ten Klooster; R.A. van der Kammen; John G. Collard

Cell migration and the regulation of cadherin-mediated homotypic cell-cell interactions are critical events during development, morphogenesis and wound healing. Aberrations in signalling pathways involved in the regulation of cell migration and cadherin-mediated cell-cell adhesion contribute to tumour invasion and metastasis. The rho family proteins, including cdc42, rac1 and rhoA, regulate signalling pathways that mediate the distinct actin cytoskeleton changes required for both cellular motility and cell-cell adhesion. Recent studies indicate that rac directly influences rho activity at the GTPase level and that the reciprocal balance between rac and rho activity can determine epithelial or mesenchymal cell morphology and migratory behaviour of epithelial (tumour) cells.


Journal of Cell Biology | 2000

Oncogenic Ras Downregulates Rac Activity, Which Leads to Increased Rho Activity and Epithelial–Mesenchymal Transition

Gerben C. M. Zondag; Eva E. Evers; Jean Paul ten Klooster; Lennert Janssen; Rob A. van der Kammen; John G. Collard


Journal of Biological Chemistry | 1993

Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase.

Martijn F. B. G. Gebbink; Gerben C. M. Zondag; Richard Wubbolts; Roderick L. Beijersbergen; I. Van Etten; Wouter H. Moolenaar


Journal of Biological Chemistry | 1995

Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain.

Gerben C. M. Zondag; Gregory M. Koningstein; Ying-Ping Jiang; Jan Sap; Wouter H. Moolenaar; Martijn F. B. G. Gebbink


Journal of Biological Chemistry | 2000

Receptor Protein-tyrosine Phosphatase RPTPμ Binds to and Dephosphorylates the Catenin p120 ctn

Gerben C. M. Zondag; Albert B. Reynolds; Wouter H. Moolenaar


Journal of Cell Biology | 1995

Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact.

Martijn F. B. G. Gebbink; Gerben C. M. Zondag; G. M. Koningstein; E. Feiken; Richard Wubbolts; Wouter H. Moolenaar


Journal of Cell Biology | 1998

Acute loss of Cell–Cell Communication Caused by G Protein–coupled Receptors: A Critical Role for c-Src

Friso R. Postma; Trudi Hengeveld; Jacqueline Alblas; Ben N. G. Giepmans; Gerben C. M. Zondag; Kees Jalink; Wouter H. Moolenaar


Biochemistry | 1993

Purification and characterization of the cytoplasmic domain of human receptor-like protein tyrosine phosphatase RPTP mu.

Martijn F. B. G. Gebbink; Mark H. G. Verheijen; Gerben C. M. Zondag; Ingrid van Etten; Wouter H. Moolenaar


Journal of Cell Biology | 1996

Lack of association between receptor protein tyrosine phosphatase RPTP mu and cadherins.

Gerben C. M. Zondag; Wouter H. Moolenaar; Martijn F. B. G. Gebbink

Collaboration


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Wouter H. Moolenaar

Netherlands Cancer Institute

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Friso R. Postma

Netherlands Cancer Institute

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Ben N. G. Giepmans

University Medical Center Groningen

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Eva E. Evers

Netherlands Cancer Institute

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Ingrid van Etten

Netherlands Cancer Institute

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Jacqueline Alblas

Netherlands Cancer Institute

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Kees Jalink

Netherlands Cancer Institute

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Trudi Hengeveld

Netherlands Cancer Institute

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