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Mark E. Zweifel, Ph.D. - Publications

Affiliations: 
2007 Johns Hopkins University, Baltimore, MD 
Area:
General Biophysics
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7 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 Zweifel ME, Courtemanche N. Competition for delivery of profilin-actin to barbed ends limits the rate of formin-mediated actin filament elongation. The Journal of Biological Chemistry. PMID 32075907 DOI: 10.1074/jbc.RA119.012000  0.315
2005 Zweifel ME, Leahy DJ, Barrick D. Structure and Notch receptor binding of the tandem WWE domain of Deltex. Structure (London, England : 1993). 13: 1599-611. PMID 16271883 DOI: 10.1016/J.Str.2005.07.015  0.599
2003 Zweifel ME, Leahy DJ, Hughson FM, Barrick D. Structure and stability of the ankyrin domain of the Drosophila Notch receptor. Protein Science : a Publication of the Protein Society. 12: 2622-32. PMID 14573873 DOI: 10.1110/Ps.03279003  0.609
2002 Zweifel ME, Barrick D. Relationships between the temperature dependence of solvent denaturation and the denaturant dependence of protein stability curves. Biophysical Chemistry. 101: 221-37. PMID 12488003 DOI: 10.1016/S0301-4622(02)00181-3  0.479
2001 Zweifel ME, Barrick D. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding. Biochemistry. 40: 14357-67. PMID 11724547 DOI: 10.1021/Bi011436+  0.618
2001 Zweifel ME, Barrick D. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 1. Solution conformational and hydrodynamic properties. Biochemistry. 40: 14344-56. PMID 11724546 DOI: 10.1021/Bi011435H  0.569
1999 Gough NR, Zweifel ME, Martinez-Augustin O, Aguilar RC, Bonifacino JS, Fambrough DM. Utilization of the indirect lysosome targeting pathway by lysosome-associated membrane proteins (LAMPs) is influenced largely by the C-terminal residue of their GYXXphi targeting signals. Journal of Cell Science. 112: 4257-69. PMID 10564644  0.305
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