Evidence map›Paper›PMID 15520810›Full record

ReviewNature reviews. Molecular cell biology2004

Strategies for RNA folding and assembly.

Renée Schroeder, Andrea Barta, Katharina Semrad

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing 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.

3 · Its place in the literature

Who cites it

157 citing papers in PubMed.

  1. Key Points to Consider When Studying RNA Remodeling by Proteins.Methods in molecular biology (Clifton, N.J.) · 2027
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  14. Intrinsically Disordered Proteins: An Overview.International journal of molecular sciences · 2022
    Review
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  20. Article

97 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

3 authors.

Renée SchroederMax F. Perutz Laboratories, Department of Microbiology and Genetics, University of Vienna, Austria. renee.schroeder@univie.ac.at
Andrea Barta
Katharina Semrad

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA is structurally very flexible, which provides the basis for its functional diversity. An RNA molecule can often adopt different conformations, which enables the regulation of its function through folding. Proteins help RNAs reach their functionally active conformation by increasing their structural stability or by chaperoning the folding process. Large, dynamic RNA-protein complexes, such as the ribosome or the spliceosome, require numerous proteins that coordinate conformational switches of the RNA components during assembly and during their respective activities.

Indexed as

Nucleic Acid ConformationAdenosine TriphosphateAmino Acid SequenceBase SequenceCatalysisMolecular ChaperonesMolecular Sequence DataProtein ConformationProteinsProtein Structure, TertiaryRNARNA, CatalyticSpliceosomesAdenosine TriphosphateMolecular ChaperonesProteinsRNARNA, Catalytic

Identifiers

PMID15520810

What OpenQuestion holds

Textmetadata
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.