Evidence map›Paper›PMID 30558886›Full record

ArticleBiophysical journal2019

FBP21's C-Terminal Domain Remains Dynamic When Wrapped around the c-Sec63 Unit of Brr2 Helicase.

Jana Sticht, Miriam Bertazzon, Lisa M Henning, Jan R Licha, Esam T Abualrous, Christian Freund

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. NMR illuminates intrinsic disorder.Current opinion in structural biology · 2021
    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

6 authors at 1 institution in 1 country.

Jana StichtLaboratory of Protein Biochemistry, Freie Universität Berlin, Berlin, Germany; Core Facility BioSupraMol, Freie Universität Berlin, Berlin, Germany. Electronic address: sticht@zedat.fu-berlin.de.
Miriam BertazzonLaboratory of Protein Biochemistry, Freie Universität Berlin, Berlin, Germany.
Lisa M HenningLaboratory of Protein Biochemistry, Freie Universität Berlin, Berlin, Germany.
Jan R LichaLaboratory of Protein Biochemistry, Freie Universität Berlin, Berlin, Germany.
Esam T AbualrousLaboratory of Protein Biochemistry, Freie Universität Berlin, Berlin, Germany; Computational Molecular Biology Group, Freie Universität Berlin, Berlin, Germany.
Christian FreundLaboratory of Protein Biochemistry, Freie Universität Berlin, Berlin, Germany. Electronic address: chfreund@zedat.fu-berlin.de.
Freie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Based on our recent finding that FBP21 regulates human Brr2 helicase activity involved in the activation of the spliceosomal B-complex, we investigated the structural and dynamic contribution of FBP21 to the interaction. By using NMR spectroscopy, we could show that the 50 C-terminal residues of FBP21 (FBP21

Indexed as

HumansMolecular Docking SimulationNuclear ProteinsProtein DomainsRibonucleoproteins, Small NuclearRNA-Binding ProteinsThermodynamicsNuclear ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsSNRNP200 protein, humanWBP4 protein, human

Identifiers

PMID30558886
PMCPMC6372199
OpenAlexW2902457095

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.