Evidence map›Paper›PMID 20143133›Full record

ArticleMolecular and cellular biochemistry2010

Characterization of zebrafish Esrom (Myc-binding protein 2) RCC1-like domain splice variants.

Hui Wang

Abstract read
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In one paragraph

Article in Molecular and cellular biochemistry, 2010. 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
0.1field-weighted citation impact, top 48% 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

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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, 1 citations in OpenAlex.

  1. Review
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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

1 author at 1 institution in 2 countries.

Hui WangDevelopmental Neurobiology Group, Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore 117604, Republic of Singapore. hwang@snv.jussieu.fr
Temasek Life Sciences Laboratory · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PHR protein family consists of C. elegan Rpm-1/Drosophila Highwire/Zebrafish Esrom/Mouse Phr-1/Human Pam. Esrom is required for correct neurites exiting the paused state at intermediate targets as well as pteridine synthesis. This study reports the identification and characterization of two novel Esrom splice variants, named splice variants 2 (splicing out 5' 24 bp of exon 17) and 3 (splicing out 5' 24 bp of exons 17 and 18). Polypeptides encoded by 5' 24 bp of exons 17 and 18 are part of basic amino-acid-rich region inside Esrom RCC1-like domain (RLD). These two splice variants maintain the whole protein reading frame and alternative exons usage patterns are conserved with mammal. At different developmental stages and adult zebrafish tissues, abundances of these splice variants are different. Importantly, by yeast two-hybrid screen and confocal colocalization analysis, it was found that alternative splicing of exon 18 regulates Esrom RLD interaction with kinesin family member 22 and G protein beta-subunit 1. Taken together, these results suggest that Esrom RLD functions are regulated by alternative splicing at temporal and spatial-specific manner.

Indexed as

Alternative SplicingGene Expression Regulation, DevelopmentalAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceCells, CulturedEmbryo, NonmammalianExonsHumansKidneyMixed Function OxygenasesMolecular Sequence DataSequence Homology, Amino AcidSequence Homology, Nucleic AcidSubcellular FractionsAdaptor Proteins, Signal TransducingMixed Function Oxygenasesmycbp2 protein, zebrafishZebrafish Proteins

Identifiers

PMID20143133
OpenAlexW1988372348

What OpenQuestion holds

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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.