B
Brett M. Collins
Researcher at University of Queensland
Publications - 153
Citations - 8750
Brett M. Collins is an academic researcher from University of Queensland. The author has contributed to research in topics: Endosome & Retromer. The author has an hindex of 46, co-authored 133 publications receiving 6875 citations. Previous affiliations of Brett M. Collins include University of Cambridge & Macquarie University.
Papers
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Journal ArticleDOI
Neuropilin-1 is a host factor for SARS-CoV-2 infection.
James L. Daly,Boris Simonetti,Katja Klein,Kai-En Chen,Maia Kavanagh Williamson,Carlos Antón-Plágaro,Deborah K. Shoemark,Lorena Simón-Gracia,Michael Bauer,Reka Hollandi,Urs F. Greber,Peter Horvath,Peter Horvath,Richard B. Sessions,Ari Helenius,Julian A. Hiscox,Julian A. Hiscox,Tambet Teesalu,David A. Matthews,Andrew D. Davidson,Brett M. Collins,Peter J. Cullen,Yohei Yamauchi,Yohei Yamauchi +23 more
TL;DR: It is shown that neuropilin-1 (NRP1), which is known to bind furin-cleaved substrates, potentiates SARS-CoV-2 infectivity and serves as a host factor for Sars-Cov-2 infection and may potentially provide a therapeutic target for COVID-19.
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Molecular Architecture and Functional Model of the Endocytic AP2 Complex
TL;DR: The structure of the 200 kDa AP2 "core" complexed with the polyphosphatidylinositol headgroup mimic inositolhexakisphosphate is described and a model for AP2 recruitment and activation is proposed.
Journal ArticleDOI
Adaptors for clathrin coats: structure and function.
TL;DR: The structure of clathrin adaptors is reviewed to establish the dynamic regulatable networks to drive vesicle genesis at the correct time and place in the cell.
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A Large-Scale Conformational Change Couples Membrane Recruitment to Cargo Binding in the AP2 Clathrin Adaptor Complex
Lauren P. Jackson,Bernard T. Kelly,Airlie J. McCoy,Thomas Gaffry,Leo C. James,Brett M. Collins,Stefan Höning,Philip R. Evans,David J. Owen +8 more
TL;DR: Using a range of biophysical techniques, it is shown that the endocytic cargo binding of AP2 is driven by its interaction with PtdIns4,5P2-containing membranes.
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Structural and thermodynamic analysis of the GFP:GFP-nanobody complex
TL;DR: The green fluorescent protein (GFP)-nanobody is a single-chain VHH antibody domain developed with specific binding activity against GFP and is emerging as a powerful tool for isolation and cellular engineering of fluorescent protein fusions in many different fields of biological research.