M
Martin J. Scanlon
Researcher at Monash University
Publications - 144
Citations - 5082
Martin J. Scanlon is an academic researcher from Monash University. The author has contributed to research in topics: DsbA & Fatty acid-binding protein. The author has an hindex of 37, co-authored 140 publications receiving 4504 citations. Previous affiliations of Martin J. Scanlon include University of Queensland & University of Nottingham.
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Journal ArticleDOI
Activation of the pseudokinase MLKL unleashes the four-helix bundle domain to induce membrane localization and necroptotic cell death
Joanne M Hildebrand,Maria C. Tanzer,Isabelle S Lucet,Isabelle S Lucet,Samuel N. Young,Sukhdeep Kaur. Spall,Pooja Sharma,Catia L Pierotti,Jean-Marc Garnier,Renwick C. J. Dobson,Renwick C. J. Dobson,Andrew I. Webb,Anne Tripaydonis,Jeffrey J. Babon,Mark D. Mulcair,Martin J. Scanlon,Warren S. Alexander,Andrew F. Wilks,Peter E. Czabotar,Guillaume Lessene,Guillaume Lessene,James M. Murphy,John Silke +22 more
TL;DR: It is shown that the MLKL pseudokinase domain acts as a latch to restrain the N-terminal four-helix bundle (4HB) domain and that unleashing this domain results in formation of a high-molecular-weight, membrane-localized complex and cell death.
Journal ArticleDOI
DSB proteins and bacterial pathogenicity
Begoña Heras,Stephen R. Shouldice,Makrina Totsika,Martin J. Scanlon,Mark A. Schembri,Jennifer L. Martin +5 more
TL;DR: A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding as discussed by the authors, which is a process that is essential for cell integrity and to produce virulence factors.
DSB proteins and bacterial pathogenicity
Begoña Heras,Stephen R. Shouldice,Makrina Totsika,Martin J. Scanlon,Mark A. Schembri,Jennifer L. Martin +5 more
TL;DR: This view of protein-folding machinery must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.
Journal ArticleDOI
Isolation, solution structure, and insecticidal activity of kalata B2, a circular protein with a twist: do Möbius strips exist in nature?
Cameron Victor Jennings,K. Johan Rosengren,Norelle L. Daly,Manuel R. Plan,Jackie Stevens,Martin J. Scanlon,Clement Waine,David Norman,Marilyn A. Anderson,David J. Craik +9 more
TL;DR: Kalata B2 is the second putative member of the Mobius cyclotide family to be structurally characterized and has a cis-peptidyl-proline bond, thus validating the suggested name for this subfamily of cyclotides.
Journal ArticleDOI
Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor
TL;DR: The three-dimensional structure of the human LDL receptor has been determined by two-dimensional NMR spectroscopy and shown to consist of a beta-hairpin structure, followed by a series of beta turns, which may represent a structural paradigm both for the other modules in the LDL receptor and for the homologous domains of several other proteins.