Alexander Fish
University of Massachusetts Medical School
3 Papers
Alexander Fish is an academic researcher from University of Massachusetts Medical School. The author has contributed to research in topics: MutS-1 & HMG-box. The author has an hindex of 2, co-authored 3 publications. Previous affiliations of Alexander Fish include Erasmus University Rotterdam.
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Papers
AChBP-targeted a-conotoxin correlates distinct binding orientations with nAChR subtype selectivity This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation or the creation of derivative works without specific permission.
C. Ulens,Alexander Fish,Yvonne Kendel,Gene Hopping,Christina I. Schroeder,A.B. Smit,Titia K. Sixma,Richard J. Lewis +7 more
- 01 Jan 2007
Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS
Maria Chiara Monti,Serge X. Cohen,Alexander Fish,Herrie H. K. Winterwerp,Arjan Barendregt,Peter Friedhoff,Anastassis Perrakis,Albert J. R. Heck,Titia K. Sixma,Robert H. H. van den Heuvel,Joyce H.G. Lebbink +10 more
TL;DR: In this article, the authors used native mass spectrometry to detect simultaneous DNA mismatch binding and asymmetric nucleotide binding to Escherichia coli MutS, which is the first direct evidence for such a postulated mismatch repair intermediate.
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation
Flora S. Groothuizen,Alexander Fish,Maxim V. Petoukhov,Annet Reumer,Laura Manelyte,Herrie H. K. Winterwerp,Martin G. Marinus,Joyce H.G. Lebbink,Dmitri I. Svergun,Peter Friedhoff,Titia K. Sixma +10 more
TL;DR: Structural data reveal that the tetramerization domains are flexible with respect to the body of the protein, resulting in mostly extended structures, and this inability to undergo a conformational change rather than mismatch affinity is correlated with mismatch repair.