Evidence map›Paper›PMID 38691336›Full record

ArticleBiomolecular NMR assignments2024

Benjamin C Smith, Robert Silvers

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecular NMR assignments, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Biomolecular NMR assignments · 2025
    Article
  3. Conserved Functions of LARP1 Proteins in Eukaryotes.Wiley interdisciplinary reviews. RNA
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Benjamin C SmithDepartment of Chemistry & Biochemistry, Florida State University, Tallahassee, FL, 32306, USA.ORCID 0009-0000-3840-9969
Robert SilversDepartment of Chemistry & Biochemistry, Florida State University, Tallahassee, FL, 32306, USA. rsilvers@fsu.edu.ORCID 0000-0003-0197-3878

Funding

Structural Co-evolution of the LARP Superfamily and its Role in Functional PlasticityR35GM142912 · NIGMS · FLORIDA STATE UNIVERSITY · PI SILVERS, ROBERT · 2021 to 2025
$2.0M
NIGMS NIH HHS R35 GM142912NIH HHS R35GM142912
6 · The paper itself

Abstract

Human La-related protein 1 (HsLARP1) is involved in post-transcriptional regulation of certain 5' terminal oligopyrimidine (5'TOP) mRNAs as well as other mRNAs and binds to both the 5'TOP motif and the 3'-poly(A) tail of certain mRNAs. HsLARP1 is heavily involved in cell proliferation, cell cycle defects, and cancer, where HsLARP1 is significantly upregulated in malignant cells and tissues. Like all LARPs, HsLARP1 contains a folded RNA binding domain, the La motif (LaM). Our current understanding of post-transcriptional regulation that emanates from the intricate molecular framework of HsLARP1 is currently limited to small snapshots, obfuscating our understanding of the full picture on HsLARP1 functionality in post-transcriptional events. Here, we present the nearly complete resonance assignment of the LaM of HsLARP1, providing a significant platform for future NMR spectroscopic studies.

Indexed as

Amino Acid MotifsNuclear Magnetic Resonance, BiomolecularAmino Acid SequenceAutoantigensHumansNitrogen IsotopesRibonucleoproteinsRNA-Binding ProteinsRNA Recognition Motif ProteinsAutoantigensLARP1 protein, humanNitrogen-15Nitrogen IsotopesRibonucleoproteinsRNA-Binding ProteinsRNA Recognition Motif ProteinsTNRC6A protein, humanLa motifLa-related proteinLARP1RNA-binding domain

Identifiers

PMID38691336
PMCPMC11593018

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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.