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Douglas A. Hattendorf, Ph.D. - Publications

Institution:
University of Chicago, Chicago, IL
Area:
protein folding
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6 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
2013 Colbert KN, Hattendorf DA, Weiss TM, Burkhardt P, Fasshauer D, Weis WI. Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation. Proceedings of the National Academy of Sciences of the United States of America. 110: 12637-42. PMID 23858467 DOI: 10.1073/Pnas.1303753110  0.4
2008 Burkhardt P, Hattendorf DA, Weis WI, Fasshauer D. Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. The Embo Journal. 27: 923-33. PMID 18337752 DOI: 10.1038/Emboj.2008.37  0.434
2007 Hattendorf DA, Andreeva A, Gangar A, Brennwald PJ, Weis WI. Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism. Nature. 446: 567-71. PMID 17392788 DOI: 10.1038/nature05635  0.38
2002 Cashikar AG, Schirmer EC, Hattendorf DA, Glover JR, Ramakrishnan MS, Ware DM, Lindquist SL. Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Molecular Cell. 9: 751-60. PMID 11983167 DOI: 10.1016/S1097-2765(02)00499-9  0.303
2002 Hattendorf DA, Lindquist SL. Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proceedings of the National Academy of Sciences of the United States of America. 99: 2732-7. PMID 11867765 DOI: 10.1073/Pnas.261693199  0.679
2002 Hattendorf DA, Lindquist SL. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. The Embo Journal. 21: 12-21. PMID 11782421 DOI: 10.1093/emboj/21.1.12  0.631
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