S
Sean A. McKenna
Researcher at University of Manitoba
Publications - 69
Citations - 3509
Sean A. McKenna is an academic researcher from University of Manitoba. The author has contributed to research in topics: RNA & Protein kinase R. The author has an hindex of 29, co-authored 68 publications receiving 2806 citations. Previous affiliations of Sean A. McKenna include Stanford University & Queen's University.
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Journal ArticleDOI
Dynamic light scattering: a practical guide and applications in biomedical sciences.
TL;DR: Evidence of the usefulness of DLS to study the homogeneity of proteins, nucleic acids, and complexes of protein–protein or protein–nucleic acid preparations, as well as to study protein–small molecule interactions is provided.
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Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A.
Parker L. Andersen,Honglin Zhou,Landon Pastushok,Trevor F. Moraes,Sean A. McKenna,Barry Ziola,Michael J. Ellison,Vishva M. Dixit,Wei Xiao +8 more
TL;DR: It is demonstrated that divergent activities of mammalian Ubc13 rely on its pairing with either of two Uevs, Uev1A or Mms2, and this finding suggests a novel regulatory mechanism in which differentUevs direct Ubcs to diverse cellular processes through physical interaction and alternative polyubiquitination.
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Structure of a Conjugating Enzyme-Ubiquitin Thiolester Intermediate Reveals a Novel Role for the Ubiquitin Tail
Katherine S. Hamilton,Michael J. Ellison,Kathryn R. Barber,R. Scott Williams,John Torin Huzil,Sean A. McKenna,Christopher Ptak,Mark Glover,Gary S. Shaw +8 more
TL;DR: The first three-dimensional model of a E2-Ub thiolester intermediate has been determined for the catalytic domain of the E2 protein Ubc1 (Ubc1(Delta450)) and ubiquitin from S. cerevisiae and provides insights into the arrangement of Ub, E2, and E3 within a ternary targeting complex.
Journal ArticleDOI
Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13.
Trevor F. Moraes,R.A. Edwards,Sean A. McKenna,Landon Pastushok,Wei Xiao,J. N. Glover,Michael J. Ellison +6 more
TL;DR: The structure of the hMms2–hUbc13 complex provides the conceptual foundation for understanding the mechanism of Lys 63 multiubiquitin chain assembly and for its interactions with the RING finger proteins Rad5 and Traf6.
Journal ArticleDOI
Noncovalent Interaction between Ubiquitin and the Human DNA Repair Protein Mms2 Is Required for Ubc13-mediated Polyubiquitination
Sean A. McKenna,Leo Spyracopoulos,Trevor F. Moraes,Landon Pastushok,Christopher Ptak,Wei Xiao,Michael J. Ellison +6 more
TL;DR: The results suggest that the role of Mms2 is to correctly orient either a target-bound or untethered ubiquitin molecule such that its Lys-63 is placed proximally to the C terminus of the ubiquit in molecule that is linked to the active site of Ubc13.