J
Jonathan N. Wells
Researcher at University of Edinburgh
Publications - 18
Citations - 983
Jonathan N. Wells is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Protein complex assembly & Genome. The author has an hindex of 9, co-authored 16 publications receiving 600 citations. Previous affiliations of Jonathan N. Wells include Cornell University & Western General Hospital.
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Journal ArticleDOI
Kinetic Analysis of Protein Stability Reveals Age-Dependent Degradation
Erik McShane,Celine Sin,Henrick Zauber,Jonathan N. Wells,Neysan Donnelly,Xi Wang,Jingyi Hou,Wei Chen,Zuzana Storchova,Joseph A. Marsh,Angelo Valleriani,Matthias Selbach,Matthias Selbach +12 more
TL;DR: Together, the data show that non-exponentially degradation is common, conserved, and has important consequences for complex formation and regulation of protein abundance.
Journal ArticleDOI
A Field Guide to Eukaryotic Transposable Elements.
TL;DR: It is argued that cataloging TE diversity and dissecting the idiosyncratic behavior of individual elements are crucial to expanding the authors' comprehension of their impact on the biology of genomes and the evolution of species.
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Interrogation of Mammalian Protein Complex Structure, Function, and Membership Using Genome-Scale Fitness Screens
Joshua Pan,Robin M. Meyers,Brittany C. Michel,Brittany C. Michel,Nazar Mashtalir,Ann E. Sizemore,Jonathan N. Wells,Seth H. Cassel,Francisca Vazquez,Barbara A. Weir,William C. Hahn,Joseph A. Marsh,Aviad Tsherniak,Cigall Kadoch,Cigall Kadoch +14 more
TL;DR: The utility of genetic perturbation screens alone, and in combination with large-scale biophysical data, is demonstrated to enhance the understanding of mammalian protein complexes in normal and disease states.
Journal ArticleDOI
Evolution of condensin and cohesin complexes driven by replacement of Kite by Hawk proteins.
TL;DR: Using a combination of profile Hidden Markov Model (HMM)-based homology searches, network analysis and structural alignments, a common origin is identified for these regulators, for which the name Hawks is proposed, i.e. HEAT proteins associated with kleisins.
Journal ArticleDOI
Operon Gene Order Is Optimized for Ordered Protein Complex Assembly.
TL;DR: Using structure-based assembly predictions, it is shown that operon gene order has been optimized to match the order in which protein subunits assemble, showing that ordered protein complex assembly pathways are of significant biological importance and represent a major evolutionary constraint on operon Gene organization.