Evidence map›Paper›PMID 36173164›Full record

ArticleProtein science : a publication of the Protein Society2022

Structural basis for the interaction between the first SURP domain of the SF3A1 subunit in U2 snRNP and the human splicing factor SF1.

Nobukazu Nameki, Masayuki Takizawa, Takayuki Suzuki, Shoko Tani, Naohiro Kobayashi, Taiichi Sakamoto, Yutaka Muto, Kanako Kuwasako

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

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  10. [Association of ventricular septal defect with rare variations of theZhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2023
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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

8 authors at 4 institutions in 1 country.

Nobukazu NamekiDivision of Molecular Science, Graduate School of Science and Technology, Gunma University, Kiryu, Gunma, Japan.ORCID 0000-0002-6222-4451
Masayuki TakizawaFaculty of Pharmacy and Research Institute of Pharmaceutical Sciences, Musashino University, Nishitokyo, Tokyo, Japan.
Takayuki SuzukiFaculty of Pharmacy and Research Institute of Pharmaceutical Sciences, Musashino University, Nishitokyo, Tokyo, Japan.
Shoko TaniFaculty of Pharmacy and Research Institute of Pharmaceutical Sciences, Musashino University, Nishitokyo, Tokyo, Japan.
Naohiro KobayashiRIKEN Center for Biosystems Dynamics Research, Yokohama, Kanagawa, Japan.ORCID 0000-0001-5136-2077
Taiichi SakamotoDepartment of Life Science, Faculty of Advanced Engineering, Chiba Institute of Technology, Narashino, Chiba, Japan.ORCID 0000-0002-1450-9372
Yutaka MutoFaculty of Pharmacy and Research Institute of Pharmaceutical Sciences, Musashino University, Nishitokyo, Tokyo, Japan.ORCID 0000-0001-8073-7077
Kanako KuwasakoFaculty of Pharmacy and Research Institute of Pharmaceutical Sciences, Musashino University, Nishitokyo, Tokyo, Japan.ORCID 0000-0003-3758-0814
Musashino University · JPChiba Institute of Technology · JPGunma University · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SURP domains are exclusively found in splicing-related proteins in all eukaryotes. SF3A1, a component of the U2 snRNP, has two tandem SURP domains, SURP1, and SURP2. SURP2 is permanently associated with a specific short region of SF3A3 within the SF3A protein complex whereas, SURP1 binds to the splicing factor SF1 for recruitment of U2 snRNP to the early spliceosomal complex, from which SF1 is dissociated during complex conversion. Here, we determined the solution structure of the complex of SURP1 and the human SF1 fragment using nuclear magnetic resonance (NMR) methods. SURP1 adopts the canonical topology of α1-α2-3

Indexed as

Ribonucleoprotein, U2 Small NuclearRNA Splicing FactorsSpliceosomesGlycineHumansProtein BindingRNA SplicingGlycineRibonucleoprotein, U2 Small NuclearRNA Splicing FactorsSF1 protein, humanSF3A1 protein, humanbio-layer interferometrycomplex structureNMRSF1SF3A1SF3a120splicingSURPSWAPU2 snRNP

Identifiers

PMID36173164
PMCPMC9514218
OpenAlexW4297382373

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.