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Biological Chemistry|November 20, 2002
Triple-helical peptide analysis of collagenolytic protease activityJanelle L Lauer-Fields, Gregg B Fields
Biopolymers|September 14, 2002
Matrix metalloproteinases and collagen catabolismJanelle L Lauer-Fields, Darius Juska, Gregg B Fields
Journal of Biomolecular Techniques : JBT|December 9, 2004
Development of a solid-phase assay for analysis of matrix metalloproteinase activityJanelle L Lauer-Fields, Hideaki Nagase, Gregg B Fields
The Journal of Biological Chemistry|October 29, 2003
Induction of endothelial cell activation by a triple helical alpha2beta integrin ligand, derived from type I collagen alpha1(I)496-507Diane Baronas-Lowell, Janelle L Lauer-Fields, Gregg B Fields
Biochemistry|September 8, 2004
Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stabilityDmitriy Minond, Janelle L Lauer-Fields, Hideaki Nagase, et al.
Methods in Molecular Biology (Clifton, N.J.)|July 9, 2008
Application of topologically constrained mini-proteins as ligands, substrates, and inhibitorsJanelle L Lauer-Fields, Dmitriy Minond, Keith Brew, et al.
Biomacromolecules|May 14, 2003
Characterization of peptide-amphiphiles possessing cellular activation sequencesNavdeep B Malkar, Janelle L Lauer-Fields, Darius Juska, et al.
Matrix Biology : Journal of the International Society for Matrix Biology|August 7, 2004
Contributions of the MMP-2 collagen binding domain to gelatin cleavage. Substrate binding via the collagen binding domain is required for hydrolysis of gelatin but not short peptidesXiaoping Xu, Yao Wang, Janelle L Lauer-Fields, et al.
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