Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registry
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Yicheng WangChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.
Kuntal ChatterjeeMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Anthony TumberChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.
Stephen A MarshallChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7678-4989
Philipp S SimonMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-2859-4475
Hiroki MakitaMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-4968-914X
Daniel W PaleyMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0003-1161-5142
Vandana TiwariMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.
Alexander T SteadChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-9784-8216
Asmit BhowmickMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-6154-6635
Vittal K YachandraMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.ORCID http://orcid.org/0000-0002-3983-7858
Lennart BrewitzChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK. lennart.brewitz@ichf.edu.pl.ORCID http://orcid.org/0000-0002-9465-777X
Jan F KernMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA. jfkern@lbl.gov.ORCID http://orcid.org/0000-0002-7272-1603
Christopher J SchofieldChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK. christopher.schofield@chem.ox.ac.uk.ORCID http://orcid.org/0000-0002-0290-6565
Patrick RabeChemistry Research Laboratory and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK. patrick.rabe@chem.ox.ac.uk.ORCID http://orcid.org/0000-0002-3448-9559
Funding
Structural Dynamics at LCLSP41GM139687 · NIGMS · STANFORD UNIVERSITY · PI HUNTER, MARK · 2021 to 2025
$7.5M
Biological Spectroscopy and Crystallography Using an X-ray Free Electron Laser - Supplemental EquipmentR01GM110501 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Junko Yano · 2014 to 2026
$4.8M
High throughput sample delivery method for time resolved studies of enzyme reactions with X-ray and complementary techniquesR01GM126289 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KERN, JAN F · 2017 to 2025
$4.6M
DIALS: supporting structural biology through open source diffraction processing softwareR24GM154040 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Aaron Samuel Brewster · 2024 to 2026
$3.7M
Diamond Light Source MX-31353NIGMS NIH HHS R01 GM110501NIGMS NIH HHS R01 GM126289NIGMS NIH HHS R24 GM154040ODCDC CDC HHS S10 OD023453RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/M011224/1RCUK | Engineering and Physical Sciences Research Council (EPSRC) EPW524311/1U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM110501U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM117126U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM126289U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM149528U.S. Department of Health & Human Services | National Institutes of Health (NIH) GM151988U.S. Department of Health & Human Services | National Institutes of Health (NIH) P41GM139687Wellcome Trust (Wellcome) 106244/Z/14/ZWellcome Trust (Wellcome) 210734/Z/18/ZWellcome Trust (Wellcome) 227298/Z/23/Z
6 · The paper itself
Abstract
Protein-hydroxylation catalysed by Fe(II) and 2-oxoglutarate (2OG) dependent oxygenases is an important regulatory mechanism in human biology. Such oxygenases typically coordinate their Fe(II) cofactor via a conserved triad of an aspartate- or glutamate- and two histidine-residues. By contrast, aspartate/asparagine β-hydroxylase (AspH), which catalyses asparagine/aspartate-residue oxidation in epidermal growth factor-like domains (EGFDs), has only two histidine-residues (H679, H725), with a water occupying the site normally occupied by an aspartate- or glutamate-residue. We describe mechanistic studies with catalytically active AspH crystals. Turnover studies with single crystals under cryogenic conditions give (3 R)-hydroxylated EGFDs with the product alcohol coordinating Fe(II) trans to H725. Time-resolved serial crystallography of microcrystals using an acoustic droplet ejection system, coupled to X-ray emission analyses, demonstrate turnover within 1.5 s, giving a product complex in which Fe(II) is regenerated. Solution and crystallographic studies with the O
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.
Structural basis of the promiscuity of the unusual Fe(II) and 2-oxoglutarate dependent human aspartate/asparagine-β-hydroxylase. · full record | Socratic