Derek J. Francis, Ph.D. - Publications

Affiliations: 
2008 Medical College of Wisconsin, Milwaukee, WI, United States 
Area:
General Biophysics

13 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Chen Q, Zhuo Y, Sharma P, Perez I, Francis DJ, Chakravarthy S, Vishnivetskiy SA, Berndt S, Hanson SM, Zhan X, Brooks EK, Altenbach C, Hubbell WL, Klug CS, Iverson TM, et al. An eight amino acid segment controls oligomerization and preferred conformation of the two non-visual arrestins. Journal of Molecular Biology. 166790. PMID 33387531 DOI: 10.1016/j.jmb.2020.166790  0.695
2016 Chen Q, Zhuo Y, Kook S, Francis DJ, Vishnivetskiy SA, Hanson SM, Zhan X, Brooks EK, Iverson TM, Altenbach C, Hubbell WL, Klug CS, Gurevich VV. The two non-visual arrestins form distinct oligomers with different functional capabilities Neuropeptides. 55: 23. DOI: 10.1016/J.Npep.2015.11.064  0.333
2014 Chen Q, Zhuo Y, Kim M, Hanson SM, Francis DJ, Vishnivetskiy SA, Altenbach C, Klug CS, Hubbell WL, Gurevich VV. Self-association of arrestin family members. Handbook of Experimental Pharmacology. 219: 205-23. PMID 24292832 DOI: 10.1007/978-3-642-41199-1_11  0.621
2012 Francis DJ, Hubbell WL, Klug CS. Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin. Applied Magnetic Resonance. 43: 405-419. PMID 25419051 DOI: 10.1007/S00723-012-0369-Y  0.645
2011 Vishnivetskiy SA, Gimenez LE, Francis DJ, Hanson SM, Hubbell WL, Klug CS, Gurevich VV. Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. The Journal of Biological Chemistry. 286: 24288-99. PMID 21471193 DOI: 10.1074/Jbc.M110.213835  0.71
2010 Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, Klug CS, Hubbell WL, Gurevich VV. The role of arrestin alpha-helix I in receptor binding. Journal of Molecular Biology. 395: 42-54. PMID 19883657 DOI: 10.1016/J.Jmb.2009.10.058  0.695
2008 Hanson SM, Dawson ES, Francis DJ, Van Eps N, Klug CS, Hubbell WL, Meiler J, Gurevich VV. A model for the solution structure of the rod arrestin tetramer. Structure (London, England : 1993). 16: 924-34. PMID 18547524 DOI: 10.1016/J.Str.2008.03.006  0.655
2007 Hanson SM, Cleghorn WM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Nair KS, Slepak VZ, Klug CS, Gurevich VV. Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. Journal of Molecular Biology. 368: 375-87. PMID 17359998 DOI: 10.1016/J.Jmb.2007.02.053  0.705
2007 Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV. Structure and function of the visual arrestin oligomer. The Embo Journal. 26: 1726-36. PMID 17332750 DOI: 10.1038/Sj.Emboj.7601614  0.676
2007 Cleghorn WM, Hanson SM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Klug CS, Gurevich VV. Arrestin‐dependent mobilization of signaling proteins to the cytoskeleton The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A613-C  0.614
2006 Wu N, Hanson SM, Francis DJ, Vishnivetskiy SA, Thibonnier M, Klug CS, Shoham M, Gurevich VV. Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins. Journal of Molecular Biology. 364: 955-63. PMID 17054984 DOI: 10.1016/J.Jmb.2006.09.075  0.712
2006 Hanson SM, Francis DJ, Vishnivetskiy SA, Kolobova EA, Hubbell WL, Klug CS, Gurevich VV. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 103: 4900-5. PMID 16547131 DOI: 10.1073/Pnas.0600733103  0.681
2006 Hanson SM, Francis DJ, Vishnivetskiy SA, Klug CS, Gurevich VV. Visual arrestin binding to microtubules involves a distinct conformational change. The Journal of Biological Chemistry. 281: 9765-72. PMID 16461350 DOI: 10.1074/Jbc.M510738200  0.678
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