Evidence map›Paper›PMID 25800680›Full record

ArticleBiophysical chemistry

Modulation of conformational changes in helix 69 mutants by pseudouridine modifications.

Jun Jiang, Daya Nidhi Kharel, Christine S Chow

Abstract read
In one paragraph

Article in Biophysical chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Advancements in pseudouridine modifying enzyme and cancer.Frontiers in cell and developmental biology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Article
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

3 authors at 1 institution in 1 country.

Jun JiangDepartment of Chemistry, Wayne State University, Detroit, MI 48202, United States.
Daya Nidhi KharelDepartment of Chemistry, Wayne State University, Detroit, MI 48202, United States.
Christine S ChowDepartment of Chemistry, Wayne State University, Detroit, MI 48202, United States. Electronic address: cchow@wayne.edu.
Wayne State University · US

Funding

The Role of Ribosomal RNA ModificationsR01GM087596 · NIGMS · WAYNE STATE UNIVERSITY · PI CHOW, CHRISTINE S · 2009 to 2012
$1.1M
NIGMS NIH HHS GM087596NIGMS NIH HHS R01 GM087596
6 · The paper itself

Abstract

Centrally located at the ribosomal subunit interface and mRNA tunnel, helix 69 (H69) from 23S rRNA participates in key steps of translation. Ribosome activity is influenced by three pseudouridine modifications, which modulate the structure and conformational behavior of H69. To understand how H69 is affected by the presence of pseudouridine in combination with sequence changes, the biophysical properties of wild-type H69 and representative mutants (A1912G, U1917C, and A1919G) were examined. Results from NMR and circular dichroism spectroscopy indicate that pH-dependent structural changes of wild-type H69 and the chosen mutants are modulated by pseudouridine and loop sequence. The effects of the mutations on global stability of H69 are negligible; however, pseudouridine stabilizes H69 at low pH conditions. Alterations to induced conformational changes of H69 likely result in compromised function, as indicated by previous biological studies.

Indexed as

Models, MolecularEscherichia coliEscherichia coli ProteinsMutationNucleic Acid ConformationPseudouridineRNAEscherichia coli ProteinsPseudouridineRNACDNMRRibosomeRNAThermodynamics

Identifiers

PMID25800680
PMCPMC4414897
OpenAlexW1993734925

What OpenQuestion holds

Textmetadata
LicenceTDM
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.