Chris D. Willis, Ph.D. - Publications
Affiliations: | 2011 | Biochemistry | University of Maryland School of Medicine, Baltimore, MD, United States |
Area:
Biochemistry, Physiology BiologyYear | Citation | Score | |||
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2013 | Willis CD, Poluzzi C, Mongiat M, Iozzo RV. Endorepellin laminin-like globular 1/2 domains bind Ig3-5 of vascular endothelial growth factor (VEGF) receptor 2 and block pro-angiogenic signaling by VEGFA in endothelial cells. The Febs Journal. 280: 2271-84. PMID 23374253 DOI: 10.1111/Febs.12164 | 0.522 | |||
2012 | Willis CD, Oashi T, Busby B, Mackerell AD, Bloch RJ. Hydrophobic residues in small ankyrin 1 participate in binding to obscurin. Molecular Membrane Biology. 29: 36-51. PMID 22416964 DOI: 10.3109/09687688.2012.660709 | 0.694 | |||
2011 | Busby B, Oashi T, Willis CD, Ackermann MA, Kontrogianni-Konstantopoulos A, Mackerell AD, Bloch RJ. Electrostatic interactions mediate binding of obscurin to small ankyrin 1: biochemical and molecular modeling studies. Journal of Molecular Biology. 408: 321-34. PMID 21333652 DOI: 10.1016/J.Jmb.2011.01.053 | 0.696 | |||
2011 | Bloch RJ, Busby B, Oashi T, Willis C, Ackermann M, Kontrogianni-Konstantopoulos A, Mackerell AD. Interaction of Obscurin a with Small Ankyrin 1 Biophysical Journal. 100: 588a. DOI: 10.1016/J.Bpj.2010.12.3394 | 0.692 | |||
2010 | Busby B, Willis CD, Ackermann MA, Kontrogianni-Konstantopoulos A, Bloch RJ. Characterization and comparison of two binding sites on obscurin for small ankyrin 1. Biochemistry. 49: 9948-56. PMID 20949908 DOI: 10.1021/Bi101165P | 0.674 | |||
2010 | Willis CD, Busby B, Oashi T, MacKerell AD, Bloch R. Surface-Exposed Hydrophobic Residues on Small Ankyrin-1 Mediate Binding to Obscurin Biophysical Journal. 98: 39a. DOI: 10.1016/J.Bpj.2009.12.223 | 0.7 | |||
2007 | Fialcowitz-White EJ, Brewer BY, Ballin JD, Willis CD, Toth EA, Wilson GM. Specific protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences. The Journal of Biological Chemistry. 282: 20948-59. PMID 17517897 DOI: 10.1074/Jbc.M701751200 | 0.581 | |||
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