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Showing 1–16 of 16 results
Advanced filters: Author: Leighton Coates Clear advanced filters

  • The SARS-CoV-2 3CL main protease (3CL Mpro) is a chymotrypsin-like protease that facilitates the production of non-structural proteins, which are essential for viral replication and is therefore of great interest as a drug target. Here, the authors present the 2.30 Å room temperature crystal structure of ligand-free 3CL Mpro and compare it with the earlier determined low-temperature ligand-free and inhibitor-bound crystal structures.

    • Daniel W. Kneller
    • Gwyndalyn Phillips
    • Andrey Kovalevsky
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-6

  • The number of K+ occupied binding sites in the selectivity filter of potassium ion channels is still under debate. Here, the authors collect diffraction data on the K+ selective NaK channel NaK2K at a wavelength of 3.35 Å, close to the K absorption edge, revealing that all four binding sites in the selectivity filter are fully occupied by K+ ions.

    • Patricia S. Langan
    • Venu Gopal Vandavasi
    • Leighton Coates
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-5

  • Efforts to convert aptamers into molecular switches using rational design are often unsuccessful. Here the authors describe a massively parallel screening-based strategy whereby millions of potential aptamer switches are synthesised, sequenced and screened directly on a flow-cell.

    • Alex M. Yoshikawa
    • Alexandra E. Rangel
    • H. Tom Soh
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • An analysis of 24,202 critical cases of COVID-19 identifies potentially druggable targets in inflammatory signalling (JAK1), monocyte–macrophage activation and endothelial permeability (PDE4A), immunometabolism (SLC2A5 and AK5), and host factors required for viral entry and replication (TMPRSS2 and RAB2A).

    • Erola Pairo-Castineira
    • Konrad Rawlik
    • J. Kenneth Baillie
    ResearchOpen Access
    Nature
    Volume: 617, P: 764-768

  • The activity of human manganese superoxide dismutase (MnSOD) is determined by the state of a key catalytic residue, Tyr34, which was reported to undergo cyclic deprotonation and protonation events to promote the electron transfers of MnSOD. Here, the authors performed neutron diffraction, X-ray spectroscopy, and quantum chemistry calculations of Tyr34Phe MnSOD in oxidized, reduced and product inhibited enzymatic states, to elucidate the role of Tyr34 in MnSOD catalysis.

    • Jahaun Azadmanesh
    • Katelyn Slobodnik
    • Gloria E. O. Borgstahl
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-17

  • Human manganese superoxide dismutase is an oxidoreductase that converts superoxide to molecular oxygen and hydrogen peroxide with proton-coupled electron transfers (PCETs), and has evolved to be highly product inhibited to limit the formation of hydrogen peroxide. Here, the authors use neutron diffraction and X-ray absorption spectroscopy of the product-bound, trivalent, and divalent states of the enzyme to identify the product-inhibited complex and propose a PCET mechanism.

    • Jahaun Azadmanesh
    • Katelyn Slobodnik
    • Gloria E. O. Borgstahl
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18

  • A global network of researchers was formed to investigate the role of human genetics in SARS-CoV-2 infection and COVID-19 severity; this paper reports 13 genome-wide significant loci and potentially actionable mechanisms in response to infection.

    • Mari E. K. Niemi
    • Juha Karjalainen
    • Chloe Donohue
    ResearchOpen Access
    Nature
    Volume: 600, P: 472-477

  • Human manganese superoxide dismutase (MnSOD) is an oxidoreductase that uses concerted proton and electron transfers to reduce the levels of superoxide radicals in mitochondria, but mechanistic insights into this process are limited. Here, the authors report neutron crystal structures of Mn3+SOD and Mn2+SOD, revealing changes in the protonation states of key residues in the enzyme active site during the redox cycle.

    • Jahaun Azadmanesh
    • William E. Lutz
    • Gloria E. O. Borgstahl
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Analysis of changes in functional groups of species and potential drivers of environmental change for protected areas across the world’s major tropical regions reveals large variation between reserves that have been effective and those experiencing an erosion of biodiversity, and shows that environmental changes immediately outside reserves are nearly as important as those inside in determining their ecological fate.

    • William F. Laurance
    • D. Carolina Useche
    • Franky Zamzani
    Research
    Nature
    Volume: 489, P: 290-294