Evidence map›Paper›PMID 21297639›Full record

ArticleNature structural & molecular biology2011

Structural and biochemical studies of the 5'→3' exoribonuclease Xrn1.

Jeong Ho Chang, Song Xiang, Kehui Xiang, James L Manley, Liang Tong

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

81 citing papers in PubMed, 119 citations in OpenAlex.

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  9. 5'-terminal glycosylation of protein-coding transcripts: An epitranscriptomic modification that prolongs mRNA lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2025
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21 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

5 authors at 2 institutions in 2 countries.

Jeong Ho ChangDepartment of Biological Sciences, Columbia University, New York, NY, USA.
Song Xiang
Kehui Xiang
James L Manley
Liang Tong
Columbia University · USChinese Academy of Sciences · CN

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
MRNA SYTHESIS IN ANIMAL CELLS--3END FORMATIONR01GM028983 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 1985 to 2014
$6.4M
Structural biology of pre-mRNA 3'-end processingR01GM077175 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2007 to 2015
$2.8M
Structure and function of 5' to 3' exoribonucleasesR01GM090059 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2011 to 2015
$1.9M
NIBIB NIH HHS P30 EB009998NIGMS NIH HHS GM028983NIGMS NIH HHS GM077175NIGMS NIH HHS GM090059NIGMS NIH HHS R01 GM028983NIGMS NIH HHS R01 GM077175NIGMS NIH HHS R01 GM090059
6 · The paper itself

Abstract

The 5'→3' exoribonucleases (XRNs) have important functions in transcription, RNA metabolism and RNA interference. The structure of Rat1 (also known as Xrn2) showed that the two highly conserved regions of XRNs form a single, large domain that defines the active site of the enzyme. Xrn1 has a 510-residue segment after the conserved regions that is required for activity but is absent from Rat1/Xrn2. Here we report the crystal structures of Kluyveromyces lactis Xrn1 (residues 1-1,245, E178Q mutant), alone and in complex with a Mn(2+) ion in the active site. The 510-residue segment contains four domains (D1-D4), located far from the active site. Our mutagenesis and biochemical studies show that their functional importance results from their ability to stabilize the conformation of the N-terminal segment of Xrn1. These domains might also constitute a platform that interacts with protein partners of Xrn1.

Indexed as

Catalytic DomainExoribonucleasesKluyveromycesManganeseModels, MolecularMutationProtein Structure, TertiaryExoribonucleasesManganese

Identifiers

PMID21297639
PMCPMC3075561
OpenAlexW2023771912

What OpenQuestion holds

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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.