Evidence map›Paper›PMID 9539722›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

A novel glutamine-RNA interaction identified by screening libraries in mammalian cells.

R Tan, A D Frankel

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed, 59 citations in OpenAlex.

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  6. RNA-Binding Macrocyclic Peptides.Frontiers in molecular biosciences · 2022
    Review
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  9. The new (dis)order in RNA regulation.Cell communication and signaling : CCS · 2016
    Review
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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

2 authors at 1 institution in 1 country.

R TanDepartment of Biochemistry and Biophysics, University of California, 513 Parnassus Avenue, San Francisco, CA 94143-0448, USA.
A D Frankel
University of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The arginine-rich motif provides a versatile framework for RNA recognition in which few amino acids other than arginine are needed to mediate specific binding. Using a mammalian screening system based on transcriptional activation by HIV Tat, we identified novel arginine-rich peptides from combinatorial libraries that bind tightly to the Rev response element of HIV. Remarkably, a single glutamine, but not asparagine, within a stretch of polyarginine can mediate high-affinity binding. These results, together with the structure of a Rev peptide-Rev response element complex, suggest that the carboxamide groups of glutamine or asparagine are well-suited to hydrogen bond to G-A base pairs and begin to establish an RNA recognition code for the arginine-rich motif. The screening approach may provide a relatively general method for screening expression libraries in mammalian cells.

Indexed as

ArginineHIV Long Terminal RepeatPeptide LibraryAmino Acid SequenceAnimalsBinding SitesCell LineChloramphenicol O-AcetyltransferaseGene Products, revGene Products, tatGenes, ReporterGreen Fluorescent ProteinsHeLa CellsHIVHumansLuminescent ProteinsArginineChloramphenicol O-AcetyltransferaseGene Products, revGene Products, tatGreen Fluorescent ProteinsLuminescent ProteinsPeptide LibraryRecombinant Fusion Proteinsrev Gene Products, Human Immunodeficiency VirusRNAtat Gene Products, Human Immunodeficiency Virus

Identifiers

PMID9539722
PMCPMC22474
OpenAlexW2092618307

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.