Xiaolan Qian
National Institutes of Health
37 Papers
250 Citations
Xiaolan Qian is an academic researcher from National Institutes of Health. The author has contributed to research in topics: DLC1 & Tumor suppressor gene. The author has an hindex of 22, co-authored 32 publications.
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Papers
Oncogenic inhibition by a deleted in liver cancer gene requires cooperation between tensin binding and Rho-specific GTPase-activating protein activities
Xiaolan Qian,Guorong Li,Holly K. Asmussen,Laura Asnaghi,William C. Vass,Richard Braverman,Kenneth M. Yamada,Nicholas C. Popescu,Alex G. Papageorge,Douglas R. Lowy +9 more
TL;DR: The results suggest that DLC1 is a multifunctional protein whose biological activity depends on cooperation between its tensin binding and RhoGAP activities, although neither activity depends upon the other.
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Sipa1 is a candidate for underlying the metastasis efficiency modifier locus Mtes1.
Yeong-Gwan Park,Xiaohong Zhao,Fabienne Lesueur,Fabienne Lesueur,Douglas R. Lowy,Mindy Lancaster,Paul D.P. Pharoah,Xiaolan Qian,Kent W. Hunter +8 more
TL;DR: Examination of human expression data and analysis of candidate genes suggest that the Sipa1 polymorphism is one of the genetic polymorphisms underlying the Mtes1 locus, which is the first demonstration, to the authors' knowledge, of a constitutional genetic polymorphism affecting tumor metastasis.
Isolation of Mouse Embryo Fibroblasts
Marian E. Durkin,Xiaolan Qian,Nicholas C. Popescu,Douglas R. Lowy +3 more
- 20 Sep 2013
TL;DR: A protocol for the isolation of MEFs from day 13.5-day 14.5 mouse embryos is described, and the MEFs obtained are suitable for use in biochemical assays and for further genetic manipulations.
Full activity of the deleted in liver cancer 1 (DLC1) tumor suppressor depends on an LD-like motif that binds talin and focal adhesion kinase (FAK)
TL;DR: It is concluded that the LD-like motif, which binds talin and FAK, is required for the full tumor suppressor activity of DLC1 and contributes to the association of DLC 1 with focal adhesions.
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Ras-Specific Exchange Factor GRF: Oligomerization through Its Dbl Homology Domain and Calcium-Dependent Activation of Raf
Pieter H. Anborgh,Xiaolan Qian,Alex G. Papageorge,William C. Vass,Jeffrey E. DeClue,Douglas R. Lowy +5 more
TL;DR: It is concluded that GRF 1 and GRF2 can form homo- and hetero-oligomers via their DH domains, that mutational inactivation of oligomer formation by GRF1 is associated with impaired biological and signaling activities, and that in 293T cellsGRF1 mediates at least two pathways for Raf activation.
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