Evidence map›Paper›PMID 28753936›Full record

ArticleMolecules (Basel, Switzerland)2017

Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA.

Ryo Iwaoka, Takashi Nagata, Kengo Tsuda, Takao Imai, Hideyuki Okano, Naohiro Kobayashi, Masato Katahira

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mechanism of RNA recognition by a Musashi RNA-binding protein.Current research in structural biology · 2022
    Review
  13. Review
  14. RNA-Targeted Therapies and High-Throughput Screening Methods.International journal of molecular sciences · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Ryo IwaokaInstitute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan. iwaoka.ryo.g78@kyoto-u.jp.
Takashi NagataInstitute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan. nagata.takashi.6w@kyoto-u.ac.jp.
Kengo TsudaRIKEN Center for Life Science Technologies, 1-7-22 Suehirocho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan. kengo.tsuda@riken.jp.
Takao ImaiDepartment of Physiology, Keio University School of Medicine, Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan. imait@a8.keio.jp.
Hideyuki OkanoDepartment of Physiology, Keio University School of Medicine, Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan. hidokano@a2.keio.jp.
Naohiro KobayashiInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan. naohiro@protein.osaka-u.ac.jp.
Masato KatahiraInstitute of Advanced Energy, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan. katahira.masato.6u@kyoto-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Musashi-1 (Msi1) controls the maintenance of stem cells and tumorigenesis through binding to its target mRNAs and subsequent translational regulation. Msi1 has two RNA-binding domains (RBDs), RBD1 and RBD2, which recognize r(GUAG) and r(UAG), respectively. These minimal recognition sequences are connected by variable linkers in the Msi1 target mRNAs, however, the molecular mechanism by which Msi1 recognizes its targets is not yet understood. We previously determined the solution structure of the Msi1 RBD1:r(GUAGU) complex. Here, we determined the first structure of the RBD2:r(GUAGU) complex. The structure revealed that the central trinucleotide, r(UAG), is specifically recognized by the intermolecular hydrogen-bonding and aromatic stacking interactions. Importantly, the C-terminal region, which is disordered in the free form, took a certain conformation, resembling a helix. The observation of chemical shift perturbation and intermolecular NOEs, together with increases in the heteronuclear steady-state {¹H}-

Indexed as

AnimalsBase SequenceBinding SitesHydrogen BondingMiceNerve Tissue ProteinsProtein BindingProtein Structure, TertiaryRNARNA-Binding ProteinsRNA, MessengerMsi1h protein, mouseNerve Tissue ProteinsRNARNA-Binding ProteinsRNA, MessengerMsi1protein-RNA complexRNA-binding proteinsolution structure determination

Identifiers

PMID28753936
PMCPMC6152312

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Registered trials

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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.