Department of Chemical and Biomolecular Engineering,
Johns Hopkins Physical Sciences - Oncology Center
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Pathogenic activation of receptor tyrosine kinases in mammalian membranes.
Journal of molecular biology Dec, 2008 | Pubmed ID: 18976668
Increased expression of the integral membrane protein ErbB2 in Chinese hamster ovary cells expressing the anti-apoptotic gene Bcl-xL.
Protein expression and purification Sep, 2009 | Pubmed ID: 19376231
Physical basis behind achondroplasia, the most common form of human dwarfism.
The Journal of biological chemistry Sep, 2010 | Pubmed ID: 20624921
Specific inhibition of a pathogenic receptor tyrosine kinase by its transmembrane domain.
Biochimica et biophysica acta Jan, 2011 | Pubmed ID: 20713021
FGFR3 heterodimerization in achondroplasia, the most common form of human dwarfism.
The Journal of biological chemistry Apr, 2011 | Pubmed ID: 21324899
High-throughput selection of transmembrane sequences that enhance receptor tyrosine kinase activation.
Journal of molecular biology Sep, 2011 | Pubmed ID: 21767549
Physical-chemical principles underlying RTK activation, and their implications for human disease.
Biochimica et biophysica acta Apr, 2012 | Pubmed ID: 21840295
Effect of the G375C and G346E achondroplasia mutations on FGFR3 activation.
PloS one , 2012 | Pubmed ID: 22529939
Production of plasma membrane vesicles with chloride salts and their utility as a cell membrane mimetic for biophysical characterization of membrane protein interactions.
Analytical chemistry Oct, 2012 | Pubmed ID: 22985263
Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence.
Scientific reports , 2012 | Pubmed ID: 23152945
Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes.
Biochimica et biophysica acta Sep, 2014 | Pubmed ID: 24631664
Quantification of the effects of mutations on receptor tyrosine kinase (RTK) activation in mammalian cells.
Methods in molecular biology (Clifton, N.J.) , 2015 | Pubmed ID: 25319891
Switching from protease-independent to protease-dependent cancer cell invasion.
Biophysical journal Dec, 2014 | Pubmed ID: 25468324
Three-dimensional matrix fiber alignment modulates cell migration and MT1-MMP utility by spatially and temporally directing protrusions.
Scientific reports Oct, 2015 | Pubmed ID: 26423227
Local 3D matrix confinement determines division axis through cell shape.
Oncotarget Feb, 2016 | Pubmed ID: 26515603
Collective cancer cell invasion induced by coordinated contractile stresses.
Oncotarget Dec, 2015 | Pubmed ID: 26528856
Lijuan He*,1,2,
Alexandra Sneider*,1,
Weitong Chen1,
Michelle Karl1,
Vishnu Prasath3,
Pei-Hsun Wu1,2,
Gunnar Mattson3,
Denis Wirtz1,2,4
1Department of Chemical and Biomolecular Engineering, Johns Hopkins University,
2Johns Hopkins Physical Sciences - Oncology Center, Johns Hopkins University,
3Department of Biomedical Engineering, Johns Hopkins University,
4Departments of Oncology and Pathology and Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School of Medicine
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