Evidence map›Paper›PMID 28325844›Full record

ArticleRNA (New York, N.Y.)2017

The sole LSm complex in

Kirsten A Reimer, Martha R Stark, Lisbeth-Carolina Aguilar, Sierra R Stark, Robert D Burke, Jack Moore, Richard P Fahlman, Calvin K Yip, Haruko Kuroiwa, Marlene Oeffinger and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2017. 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
0.4field-weighted citation impact, top 37% 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, 18 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

11 authors at 6 institutions in 2 countries.

Kirsten A ReimerDepartment of Chemistry, University of Northern British Columbia, Prince George, BC V2N 4Z9, Canada.ORCID 0000-0002-5183-6110
Martha R StarkDepartment of Chemistry, University of Northern British Columbia, Prince George, BC V2N 4Z9, Canada.
Lisbeth-Carolina AguilarLaboratory of RNP Biochemistry, Institut de Recherches Cliniques de Montréal (IRCM), Faculty of Medicine, McGill University, Montreal, QC H3A 0G4, Canada.ORCID 0000-0002-7296-3733
Sierra R StarkDepartment of Chemistry, University of Northern British Columbia, Prince George, BC V2N 4Z9, Canada.
Robert D BurkeDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, V8W 3P6, Canada.ORCID 0000-0001-5527-4410
Jack MooreDepartment of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Richard P FahlmanDepartment of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Calvin K YipDepartment of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC V6T 1Z3, Canada.ORCID 0000-0003-1779-9501
Haruko KuroiwaKuroiwa Initiative Research Unit, College of Science, Rikkyo University, Toshima, Tokyo 171-8501, Japan.
Marlene OeffingerLaboratory of RNP Biochemistry, Institut de Recherches Cliniques de Montréal (IRCM), Faculty of Medicine, McGill University, Montreal, QC H3A 0G4, Canada.ORCID 0000-0001-6427-1393
Stephen D RaderDepartment of Chemistry, University of Northern British Columbia, Prince George, BC V2N 4Z9, Canada.ORCID 0000-0001-7242-1785
University of Northern British Columbia · CAMontreal Clinical Research Institute · CAUniversity of Alberta · CARikkyo University · JPUniversity of British Columbia · CAUniversity of Victoria · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins of the Sm and Sm-like (LSm) families, referred to collectively as (L)Sm proteins, are found in all three domains of life and are known to promote a variety of RNA processes such as base-pair formation, unwinding, RNA degradation, and RNA stabilization. In eukaryotes, (L)Sm proteins have been studied, inter alia, for their role in pre-mRNA splicing. In many organisms, the LSm proteins form two distinct complexes, one consisting of LSm1-7 that is involved in mRNA degradation in the cytoplasm, and the other consisting of LSm2-8 that binds spliceosomal U6 snRNA in the nucleus. We recently characterized the splicing proteins from the red alga

Indexed as

RNA SplicingAmino Acid SequenceBase SequenceComputational BiologyImmunoprecipitationModels, MolecularNucleic Acid ConformationPhylogenyProtein BindingProtein ConformationProtein TransportRhodophytaRNA-Binding ProteinsRNA, MessengerRNA PrecursorsRNA, Small NuclearRNA-Binding ProteinsRNA, MessengerRNA PrecursorsRNA, Small NuclearU6 small nuclear RNACyanidioschyzon merolaeLSm complexmRNA degradationPat1pre-mRNA splicingU6 snRNA

Identifiers

PMID28325844
PMCPMC5435867
OpenAlexW2603791616

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.