Evidence map›Paper›PMID 33577684›Full record

ArticleNucleic acids research2021

Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45.

Xiaolei Chen, Zhongmei Yang, Wenfeng Wang, Kaiyue Qian, Mingjie Liu, Junchao Wang, Mingzhu Wang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. RBM45 Preferential Binding to mThe journal of physical chemistry. B · 2026
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  3. Review
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  11. RBM45 is an mCell reports · 2022
    Article
  12. Review
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

7 authors at 1 institution in 1 country.

Xiaolei ChenInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Zhongmei YangInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Wenfeng WangInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Kaiyue QianInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Mingjie LiuInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Junchao WangInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Mingzhu WangInstitutes of Physical Science and Information Technology, Anhui University, 111 Jiulong Road, Hefei 230601, Anhui, China.
Anhui University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RBM45 is an RNA-binding protein involved in neural development, whose aggregation is associated with neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar dementia (FTLD). However, the mechanisms of RNA-binding and aggregation of RBM45 remain unelucidated. Here, we report the crystal structure of the N-terminal tandem RRM domains of human RBM45 in complex with single-stranded DNA (ssDNA). Our structural and biochemical results revealed that both the RRM1 and RRM2 of RBM45 recognized the GAC sequence of RNA/ssDNA. Two aromatic residues and an arginine residue in each RRM were critical for RNA-binding, and the interdomain linker was also involved in RNA-binding. Two RRMs formed a pair of antiparallel RNA-binding sites, indicating that the N-terminal tandem RRM domains of RBM45 bound separate GAC motifs in one RNA strand or GAC motifs in different RNA strands. Our findings will be helpful in the identification of physiologic targets of RBM45 and provide evidence for understanding the physiologic and pathologic functions of RBM45.

Indexed as

Crystallography, X-RayDNA, Single-StrandedHumansModels, MolecularNerve Tissue ProteinsNucleotide MotifsProtein BindingRNARNA-Binding ProteinsRNA Recognition MotifDNA, Single-StrandedNerve Tissue ProteinsRBM45 protein, humanRNARNA-Binding Proteins

Identifiers

PMID33577684
PMCPMC7968997
OpenAlexW3126491875

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.