Evidence map›Paper›PMID 29946118›Full record

ArticleNature communications2018

Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1.

Hamed Kooshapur, Nila Roy Choudhury, Bernd Simon, Max Mühlbauer, Alexander Jussupow, Noemi Fernandez, Alisha N Jones, Andre Dallmann, Frank Gabel, Carlo Camilloni and 3 more

Open access · goldAbstract readValidation Study
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 112 citations in OpenAlex.

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  7. hnRNP A1 induces aberrantLife science alliance · 2025
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3 more citing papers are in PubMed but not listed here.

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

13 authors at 5 institutions in 4 countries.

Hamed KooshapurInstitute of Structural Biology, Helmholtz Zentrum München, Neuherberg, 85764, Germany.ORCID http://orcid.org/0000-0001-5878-1872
Nila Roy ChoudhuryWellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Edinburgh, EH9 3BF, UK.
Bernd SimonStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, 69117, Germany.
Max MühlbauerCenter for Integrated Protein Science Munich at Department Chemie, Technical University of Munich, Garching, 85747, Germany.ORCID http://orcid.org/0000-0002-2056-6795
Alexander JussupowCenter for Integrated Protein Science Munich at Department Chemie, Technical University of Munich, Garching, 85747, Germany.
Noemi FernandezMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh, EH4 2XU, UK.
Alisha N JonesInstitute of Structural Biology, Helmholtz Zentrum München, Neuherberg, 85764, Germany.
Andre DallmannInstitute of Structural Biology, Helmholtz Zentrum München, Neuherberg, 85764, Germany.
Frank GabelInstitut Laue-Langevin, Grenoble, 38044, France.
Carlo CamilloniCenter for Integrated Protein Science Munich at Department Chemie, Technical University of Munich, Garching, 85747, Germany.
Gracjan MichlewskiWellcome Trust Centre for Cell Biology, University of Edinburgh, Michael Swann Building, Edinburgh, EH9 3BF, UK. Gracjan.Michlewski@ed.ac.uk.ORCID http://orcid.org/0000-0002-7409-9619
Javier F CaceresMRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh, EH4 2XU, UK. Javier.Caceres@igmm.ed.ac.uk.ORCID http://orcid.org/0000-0001-8025-6169
Michael SattlerInstitute of Structural Biology, Helmholtz Zentrum München, Neuherberg, 85764, Germany. sattler@helmholtz-muenchen.de.ORCID http://orcid.org/0000-0002-1594-0527
Center for Integrated Protein Science Munich · DEWestern General Hospital · GBCentre National de la Recherche Scientifique · FREuropean Molecular Biology Laboratory · DEWellcome Centre for Cell Biology · GB

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) GRK1721EC | Seventh Framework Programme (European Union Seventh Framework Programme) 291763Medical Research Council G1000564Medical Research Council MC_PC_U127584479Medical Research Council MC_UU_00007/7Medical Research Council (MRC) G10000564Wellcome Trust 092076Wellcome Trust 095518/Z/11/Z
6 · The paper itself

Abstract

Post-transcriptional mechanisms play a predominant role in the control of microRNA (miRNA) production. Recognition of the terminal loop of precursor miRNAs by RNA-binding proteins (RBPs) influences their processing; however, the mechanistic basis for how levels of individual or subsets of miRNAs are regulated is mostly unexplored. We previously showed that hnRNP A1, an RBP implicated in many aspects of RNA processing, acts as an auxiliary factor that promotes the Microprocessor-mediated processing of pri-mir-18a. Here, by using an integrative structural biology approach, we show that hnRNP A1 forms a 1:1 complex with pri-mir-18a where both RNA recognition motifs (RRMs) bind to cognate RNA sequence motifs in the terminal loop of pri-mir-18a. Terminal loop binding induces an allosteric destabilization of base-pairing in the pri-mir-18a stem that promotes its downstream processing. Our results highlight terminal loop RNA recognition by RBPs as a potential general principle of miRNA biogenesis and regulation.

Indexed as

Base SequenceBinding SitesBiophysical PhenomenaCrystallography, X-RayHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1HumansMicroRNAsModels, MolecularMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularNucleic Acid ConformationProtein BindingProtein DomainsRNA Processing, Post-TranscriptionalRNA StabilityHeterogeneous Nuclear Ribonucleoprotein A1hnRNPA1 protein, humanMicroRNAsMIRN18A microRNA, human

Identifiers

PMID29946118
PMCPMC6018666
OpenAlexW2809229380

What OpenQuestion holds

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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.