@article {2456,
	title = {Nanomechanical Properties of Tenascin-X Revealed by Single-Molecule Force Spectroscopy},
	journal = {Journal of Molecular Biology},
	volume = {385},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 403HJTimes Cited: 4Cited Reference Count: 35Jollymore, Ashlee Lethias, Claire Peng, Qing Cao, Yi Li, Hongbin},
	month = {Jan},
	pages = {1277-1286},
	type = {Article},
	abstract = {Tenascin-X is an extracellular matrix protein and binds a variety of molecules in extracellular matrix and on cell membrane. Tenascin-X plays important roles in regulating the structure and mechanical properties of connective tissues. Using single-molecule atomic force microscopy, we have investigated the mechanical properties of bovine tenascin-X in detail. Our results indicated that tenascin-X is an elastic protein and the fibronectin type III (FnIII) domains can unfold under a stretching force and refold to regain their mechanical stability upon the removal of the stretching force. All the 30 FnIII domains of tenascin-X show similar mechanical stability, mechanical unfolding kinetics, and contour length increment upon domain unfolding, despite their large sequence diversity. In contrast to the homogeneity in their mechanical unfolding behaviors, FnIII domains fold at different rates. Using the 10th FnIII domain of tenascin-X (TNXfn10) as a model system, we constructed a polyprotein chimera composed of alternating TNXfn10 and GB1 domains and used. atomic force microscopy to confirm that the mechanical properties of TNXfn10 are consistent with those of the FnIII domains of tenascin-X These results lay the foundation to further study the mechanical properties of individual FnIII domains and establish the relationship between point mutations and mechanical phenotypic effect on tenascin-X Moreover, our results provided the opportunity to compare the mechanical properties and design of different forms of tenascins. The comparison between tenascin-X and tenascin-C revealed interesting common as well as distinguishing features for mechanical unfolding and folding of tenascin-C and tenascin-X and will open up new avenues to investigate the mechanical. functions and architectural design of different forms of tenascins. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {AFM, BINDING, DEFICIENCY, DOMAINS, FAMILY, FnIII domains, IDENTIFICATION, III MODULES, MECHANICAL STABILITY, mechanical unfolding, microscopy, PROTEIN, single molecule force spectroscopy, tenascin},
	isbn = {0022-2836},
	url = {<Go to ISI>://000263073400022},
	author = {Jollymore, A. and Lethias, C. and Peng, Q. and Cao, Y. and Li, H. B.}
}
@article {1198,
	title = {Strongylophorine-26, a Rho-dependent inhibitor of tumor cell invasion that reduces actin stress fibers and induces nonpolarized lamellipodial extensions},
	journal = {Molecular Cancer Therapeutics},
	volume = {4},
	number = {5},
	year = {2005},
	note = {ISI Document Delivery No.: 926DETimes Cited: 6Cited Reference Count: 37},
	month = {May},
	pages = {772-778},
	type = {Article},
	abstract = {Strongylophorine-26, a new meroditerpenoid, was recently identified as an inhibitor of cancer cell invasion. This study was undertaken to characterize its mechanism of action. We find that strongylophorine-26 inhibits the motility of MDA-MB-231 breast carcinoma cells on a plastic surface. Upon addition of strongylophorine-26, rapid cell contraction and depolarization occurred, followed by spreading and flattening of the entire cell. Treated cells exhibited increased membrane ruffling throughout and extended lamellipodia in all directions. Strongylophorine-26 induced a decrease in actin stress fibers, a dramatic increase in the size and number of focal adhesions, and the appearance of a dense meshwork of actin filaments around the cell periphery. Strongylophorine-26 caused a transient activation of the small GTPase Rho and treatment with the Rho inhibitor C3 exoenzyme abrogated the anti-invasive activity of strongylophorine-26. These effects are distinct from those of many motility and angiogenesis inhibitors that seem to act by a common mechanism involving the induction of actin stress fibers. This difference in mechanism of action sets strongylophorine-26 apart as an experimental anticancer agent and indicates that pharmacologic inhibition of cell migration may be achieved by mechanisms not involving the stabilization of actin stress fibers.},
	keywords = {ACTIVATION, ANGIOGENESIS, CYTOSKELETON, FAMILY, FOCAL ADHESIONS, KINASE, MIGRATION, MOTILITY, PROTEIN, SMALL GTPASE},
	isbn = {1535-7163},
	url = {<Go to ISI>://000229102300009},
	author = {McHardy, L. M. and Warabi, K. and Andersen, R. J. and Roskelley, C. D. and Roberge, M.}
}
@article {3478,
	title = {MODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX},
	journal = {Science},
	volume = {269},
	number = {5232},
	year = {1995},
	note = {ISI Document Delivery No.: RX194Times Cited: 143Cited Reference Count: 49},
	month = {Sep},
	pages = {1866-1869},
	type = {Article},
	abstract = {Conformational changes, including local protein folding, play important roles in protein-DNA interactions. Here, studies of the transcription factor Ets-1 provided evidence that local protein unfolding also can accompany DNA binding. Circular dichroism and partial proteolysis showed that the secondary structure of the Ets-1 DNA-binding domain is unchanged in the presence of DNA. In contrast, DNA allosterically induced the unfolding of an cr helix that lies within a flanking region involved in the negative regulation of DNA binding. These findings suggest a structural basis for the intramolecular inhibition of DNA binding and a mechanism for the cooperative partnerships that are common features of many eukaryotic transcription factors.},
	keywords = {BASIC REGION, CRYSTAL-STRUCTURE, DOMAIN, FAMILY, GCN4, INDUCED CONFORMATIONAL CHANGE, PROTEIN-KINASES, REPRESSOR, SEQUENCE, SUBUNITS},
	isbn = {0036-8075},
	url = {<Go to ISI>://A1995RX19400036},
	author = {Petersen, J. M. and Skalicky, J. J. and Donaldson, L. W. and McIntosh, L. P. and Alber, T. and Graves, B. J.}
}
