Evidence map›Paper›PMID 38349818›Full record

ArticleeLife2024

Structural and biophysical analysis of a

Michael J Currie, James S Davies, Mariafrancesca Scalise, Ashutosh Gulati, Joshua D Wright, Michael C Newton-Vesty, Gayan S Abeysekera, Ramaswamy Subramanian, Weixiao Y Wahlgren, Rosmarie Friemann and 9 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
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.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 11 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors at 13 institutions in 7 countries.

Michael J Currie *Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology, and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.ORCID https://orcid.org/0000-0003-1509-7581
James S Davies *Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology, and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.ORCID https://orcid.org/0000-0003-4029-1650
Mariafrancesca ScaliseDepartment DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Arcavacata di Rende, Italy.
Ashutosh GulatiDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Joshua D WrightBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology, and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.ORCID https://orcid.org/0000-0003-3870-9800
Michael C Newton-VestyBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology, and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.
Gayan S AbeysekeraBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology, and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.
Ramaswamy SubramanianBiological Sciences and Biomedical Engineering, Bindley Bioscience Center, Purdue University West Lafayette, West Lafayette, United States.
Weixiao Y WahlgrenDepartment of Chemistry and Molecular Biology, Biochemistry and Structural Biology, University of Gothenburg, Gothenburg, Sweden.ORCID https://orcid.org/0000-0003-0413-165X
Rosmarie FriemannCentre for Antibiotic Resistance Research (CARe) at University of Gothenburg, Gothenburg, Sweden.
Jane R AllisonBiomolecular Interaction Centre, Digital Life Institute, Maurice Wilkins Centre for Molecular Biodiscovery, and School of Biological Sciences, University of Auckland, Auckland, New Zealand.
Peter D MaceBiochemistry Department, School of Biomedical Sciences, University of Otago, Dunedin, New Zealand.ORCID https://orcid.org/0000-0003-2175-9537
Michael D W GriffinARC Centre for Cryo-electron Microscopy of Membrane Proteins, Bio Molecular Science and Biotechnology Institute, Department of Biochemistry and Pharmacology, University of Melbourne, Melbourne, Australia.
Borries DemelerDepartment of Chemistry and Biochemistry, University of Montana, Missoula, United States.
Soichi WakatsukiBiological Sciences Division, SLAC National Accelerator Laboratory, Menlo Park, United States.
David DrewDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.ORCID https://orcid.org/0000-0001-8866-6349
Cesare IndiveriDepartment DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Arcavacata di Rende, Italy.
Renwick C J DobsonBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology, and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.ORCID https://orcid.org/0000-0002-5506-4939
Rachel A NorthDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
University of Canterbury · NZStockholm University · SEBiotechnology Institute · USAntibiotic (Bulgaria) · BGInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · ITMaurice Wilkins Centre · NZPurdue University West Lafayette · USSLAC National Accelerator Laboratory · USThe University of Sydney · AUUniversity of Calabria · ITUniversity of Gothenburg · SEUniversity of Lethbridge · CAUniversity of Otago · NZ

Funding

Development of an UltraScan Meta-Scheduler for HPC Job SubmissionR01GM120600 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Emre H. Brookes, BORRIES DEMELER · 2016 to 2026
$3.6M
6 · The paper itself

Abstract

Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active transporters that receive their substrates via a soluble-binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-electron microscopy (cryo-EM) structures of TRAP transporters provide a broad framework to understand how they work, but the mechanistic details of transport are not yet defined. Here we report the cryo-EM structure of the

Indexed as

Haemophilus influenzaeN-Acetylneuraminic AcidAdenosine TriphosphateBacterial ProteinsCryoelectron MicroscopyMembrane Transport ProteinsAdenosine TriphosphateBacterial ProteinsMembrane Transport ProteinsN-Acetylneuraminic Acidmembrane transport proteinsmolecular biophysicsNeu5Acprotein–protein interactionsialic acidstructural biologytransport mechanism

Identifiers

PMID38349818
PMCPMC10942642
OpenAlexW4388099794

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 OpenQuestion graph.