M
Merryn Strange
Researcher at University of Sydney
Publications - 3
Citations - 92
Merryn Strange is an academic researcher from University of Sydney. The author has contributed to research in topics: Necroptosis & RIPK1. The author has an hindex of 2, co-authored 3 publications receiving 55 citations.
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Journal ArticleDOI
Viral M45 and necroptosis‐associated proteins form heteromeric amyloid assemblies
Chi L.L. Pham,Nirukshan Shanmugam,Merryn Strange,Ailis O'Carroll,James W. P. Brown,Emma Sierecki,Yann Gambin,Megan Steain,Margaret Sunde +8 more
TL;DR: It is shown that the N‐terminal 90 residues of the M45 protein, which contain a RIP homotypic interaction motif (RHIM), are sufficient to confer protection against TNFR‐induced necroptosis, and mimics the interactions made by RIPK1 or ZBP1 with RIPK3, thereby forming heteromeric amyloid structures, which may explain its ability to inhibit ne croptosis.
Journal ArticleDOI
RHIM-based protein:protein interactions in microbial defence against programmed cell death by necroptosis
Max O.D.G. Baker,Nirukshan Shanmugam,Chi L.L. Pham,Merryn Strange,Megan Steain,Margaret Sunde +5 more
TL;DR: The mechanisms by which pathogens subvert RHIM:RHIM interactions in normal cellular activation of necroptosis are compared and the implications of the heteromeric nature and structure of RHIM-based amyloid complexes in the context of other functional amyloids are discussed.
Posted ContentDOI
The RHIM within the M45 protein from murine cytomegalovirus forms heteromeric amyloid fibrils with RIPK1 and RIPK3
Pham Cll,Merryn Strange,Nirukshan Shanmugam,Emma Sierecki,Yann Gambin,Megan Steain,Margaret Sunde +6 more
TL;DR: It is shown that mutation of those key tetrad residues abolishes homo- and hetero-amyloid assembly by M45 in vitro, suggesting that the amyloidogenic nature of the M45 RHIM underlies its biological activity.