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科学家 Burridge, Keith （细胞生物学）
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Keith Burridge |
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| Head of Section: Cell Biology > Cell Adhesion [ since 18 July 2001 ] |
部分名著与科研绩效：
http://scholar.google.com/scholar?q=Keith+Burridge&btnG=Search&hl=en&as_sdt=2000
K Burridge, K Fath, T Kelly, G Nuckolls, … - Annual review of cell …, 1988 - Annual Reviews
... the Extracellular Matrix and the Cytoskeleton Keith Burridge, Karl Fath, Thomas Kelly, Glen
Nuckolls, and Christopher Turner Department of Cell Biology and Anatomy, CB # 7090, 108 Swing
Building, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599 ...
Cited by 1838 - Related articles - All 4 versions
ucsd.edu [PDF]AJ Ridley, MA Schwartz, K Burridge, RA Firtel, MH … - Science, 2003 - sciencemag.org
1 Ludwig Institute for Cancer Research, Royal Free and University College School of
Medicine, London W1W 7BS, UK. 2 Departments of Microbiology and Biomedical
Engineering, Cardiovascular Research Center and Mellon Prostate Cancer Research ...
Cited by 1370 - Related articles - BL Direct - All 16 versions
1 Ludwig Institute for Cancer Research, Royal Free and University College School of
Medicine, London W1W 7BS, UK. 2 Departments of Microbiology and Biomedical
Engineering, Cardiovascular Research Center and Mellon Prostate Cancer Research ...
Cited by 1370 - Related articles - BL Direct - All 16 versions
A Horwitz, K Duggan, C Buck, MC Beckerle, K Burridge - 1986 - nature.com
Many observations suggest the presence of transmembrane linkages between the cytoskeleton
and the extracellular matrix. In fibroblasts both light and electron microscopic observations reveal
a co-alignment between actin filaments at the cell surface and extracellular fibronectin ...
Cited by 892 - Related articles - All 4 versions
Many observations suggest the presence of transmembrane linkages between the cytoskeleton
and the extracellular matrix. In fibroblasts both light and electron microscopic observations reveal
a co-alignment between actin filaments at the cell surface and extracellular fibronectin ...
Cited by 892 - Related articles - All 4 versions
rupress.org [PDF]M Chrzanowska-Wodnicka, K Burridge - The Journal of cell biology, 1996 - jcb.rupress.org
Abstract. Activated rhoA, a ras-related GTP-binding protein, stimulates the appearance of stress
fibers, focal adhesions, and tyrosine phosphorylation in quiescent cells (Ridley, AJ, and A.
Hall, 1992. Cell. 70:389-399). The pathway by which rho triggers these events has not ...
Cited by 864 - Related articles - All 7 versions
Abstract. Activated rhoA, a ras-related GTP-binding protein, stimulates the appearance of stress
fibers, focal adhesions, and tyrosine phosphorylation in quiescent cells (Ridley, AJ, and A.
Hall, 1992. Cell. 70:389-399). The pathway by which rho triggers these events has not ...
Cited by 864 - Related articles - All 7 versions
rupress.org [PDF]K Burridge, CE Turner, LH Romer - Journal of Cell Biology, 1992 - jcb.rupress.org
Abstract. Cells in culture reveal high levels of protein tyrosine phosphorylation in their focal
adhesions, the regions where cells adhere to the underlying substra- tum. We have examined
the tyrosine phosphorylation of proteins in response to plating cells on extracellular matrix ...
Cited by 784 - Related articles - BL Direct - All 5 versions
Abstract. Cells in culture reveal high levels of protein tyrosine phosphorylation in their focal
adhesions, the regions where cells adhere to the underlying substra- tum. We have examined
the tyrosine phosphorylation of proteins in response to plating cells on extracellular matrix ...
Cited by 784 - Related articles - BL Direct - All 5 versions
utoronto.ca [PDF]K Burridge, K Wennerberg - Cell, 2004 - Elsevier
Many features of cell behavior are regulated by Rho family GTPases, but the most profound effects
of these proteins are on the actin cytoskeleton and it was these that first drew attention to this
family of signaling proteins. Focusing on Rho and Rac, we will discuss how their effectors ...
Cited by 661 - Related articles - All 23 versions
Many features of cell behavior are regulated by Rho family GTPases, but the most profound effects
of these proteins are on the actin cytoskeleton and it was these that first drew attention to this
family of signaling proteins. Focusing on Rho and Rac, we will discuss how their effectors ...
Cited by 661 - Related articles - All 23 versions
SM Schoenwaelder, K Burridge - Current opinion in cell biology, 1999 - Elsevier
276 Cell regulation bind Cdc42 [31*]. This targeting does require PAK binding to PIX (PAK interacting
exchange factor), a GEF for Rac [32*]. This suggests that there is a complex formed between
Rac or Cdc42; PAK (a downstream effector) and PIX (an upstream GEF). Mutations that ...
Cited by 599 - Related articles - BL Direct - All 3 versions
276 Cell regulation bind Cdc42 [31*]. This targeting does require PAK binding to PIX (PAK interacting
exchange factor), a GEF for Rac [32*]. This suggests that there is a complex formed between
Rac or Cdc42; PAK (a downstream effector) and PIX (an upstream GEF). Mutations that ...
Cited by 599 - Related articles - BL Direct - All 3 versions
rupress.org [PDF]CA Otey, FM Pavalko, K Burridge - Journal of Cell Biology, 1990 - jcb.rupress.org
Abstract. A number of cytoskeletal-associated pro- teins that are concentrated in focal
contacts, namely ot-actinin, vinculin, talin, and integrin, have been shown to interact in vitro such
that they suggest a potential link between actin filaments and the mem- brane. Because ...
Cited by 564 - Related articles - All 4 versions
Abstract. A number of cytoskeletal-associated pro- teins that are concentrated in focal
contacts, namely ot-actinin, vinculin, talin, and integrin, have been shown to interact in vitro such
that they suggest a potential link between actin filaments and the mem- brane. Because ...
Cited by 564 - Related articles - All 4 versions
E Lazarides, K Burridge - Cell, 1975 - Elsevier
Antibodies specific for the skeletal muscle structural protein α-actinin are used to localize this
protein by indirect immunofluorescence in nonmuscle cells. In cultured nonmuscle cells, α-actinin
is localized along or between actin filament bundles producing an almost regular ...
Cited by 443 - Related articles - All 6 versions
Antibodies specific for the skeletal muscle structural protein α-actinin are used to localize this
protein by indirect immunofluorescence in nonmuscle cells. In cultured nonmuscle cells, α-actinin
is localized along or between actin filament bundles producing an almost regular ...
Cited by 443 - Related articles - All 6 versions
rupress.org [PDF]CE Turner, JR Glenney Jr, K Burridge - Journal of Cell Biology, 1990 - jcb.rupress.org
Abstract. The 68-kD protein (paxillin) is a cytoskele- tal component that localizes to the focal adhesions
at the ends of actin stress fibers in chicken embryo fibroblasts. It is also present in the focal adhesions
of Madin-Darby bovine kidney (MDBK) epithelial cells but is absent, like talin, from the ...
Cited by 407 - Related articles - All 5 versions
Abstract. The 68-kD protein (paxillin) is a cytoskele- tal component that localizes to the focal adhesions
at the ends of actin stress fibers in chicken embryo fibroblasts. It is also present in the focal adhesions
of Madin-Darby bovine kidney (MDBK) epithelial cells but is absent, like talin, from the ...
Cited by 407 - Related articles - All 5 versions
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