Evidence map›Paper›PMID 10373506›Full record

ArticleMolecular and cellular biology1999

Assembly of the alpha-globin mRNA stability complex reflects binary interaction between the pyrimidine-rich 3' untranslated region determinant and poly(C) binding protein alphaCP.

A N Chkheidze, D L Lyakhov, A V Makeyev, J Morales, J Kong, S A Liebhaber

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 126 citations in OpenAlex.

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  15. Structural determinants of human ζ-globin mRNA stability.Journal of hematology & oncology · 2014
    Article
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5 more citing papers are in PubMed but not listed here.

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.

A N ChkheidzeHoward Hughes Medical Institute and Departments of Genetics and Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, USA.
D L Lyakhov
A V Makeyev
J Morales
J Kong
S A Liebhaber
Howard Hughes Medical Institute · US

Funding

VAV ANTISENSE ODN--A NOVEL THERAPEUTIC FOR HUMAN LEUKEMIASP01CA072765 · NCI · UNIVERSITY OF PENNSYLVANIA · PI GEWIRTZ, ALAN M · 1997 to 2007
$8.5M
UTILIZATION OF TRANSGENIC MICE FOR STUDIES IN SICKLE CELL DISEASEP60HL038632 · NHLBI · CHILDREN'S HOSPITAL OF PHILADELPHIA · PI OHENE-FREMPONG, KWAKU · 1988 to 2002
$6.4M
NCI NIH HHS CA72765-01NCI NIH HHS P01 CA072765NHLBI NIH HHS HL38632-6NHLBI NIH HHS P60 HL038632
6 · The paper itself

Abstract

Globin mRNAs accumulate to 95% of total cellular mRNA during terminal erythroid differentiation, reflecting their extraordinary stability. The stability of human alpha-globin mRNA is paralleled by formation of a sequence-specific RNA-protein (RNP) complex at a pyrimidine-rich site within its 3' untranslated region (3'UTR), the alpha-complex. The proteins of the alpha-complex are widely expressed. The alpha-complex or a closely related complex also assembles at pyrimidine-rich 3'UTR segments of other stable mRNAs. These data suggest that the alpha-complex may constitute a general determinant of mRNA stability. One or more alphaCPs, members of a family of hnRNP K-homology domain poly(C) binding proteins, are essential constituents of the alpha-complex. The ability of alphaCPs to homodimerize and their reported association with additional RNA binding proteins such as AU-rich binding factor 1 (AUF1) and hnRNP K have suggested that the alpha-complex is a multisubunit structure. In the present study, we have addressed the composition of the alpha-complex. An RNA titration recruitment assay revealed that alphaCPs were quantitatively incorporated into the alpha-complex in the absence of associated AUF1 and hnRNP K. A high-affinity direct interaction between each of the three major alphaCP isoforms and the alpha-globin 3'UTR was detected, suggesting that each of these proteins might be sufficient for alpha-complex assembly. This sufficiency was further supported by the sequence-specific binding of recombinant alphaCPs to a spectrum of RNA targets. Finally, density sedimentation analysis demonstrated that the alpha-complex could accommodate only a single alphaCP. These data established that a single alphaCP molecule binds directly to the alpha-globin 3'UTR, resulting in a simple binary structure for the alpha-complex.

Indexed as

DNA-Binding ProteinsHeterogeneous-Nuclear Ribonucleoprotein DTranscription Factors3' Untranslated RegionsCytosolGlobinsHeterogeneous Nuclear Ribonucleoprotein D0Heterogeneous-Nuclear Ribonucleoprotein KHeterogeneous-Nuclear RibonucleoproteinsHumansK562 CellsPyrimidinesRibonucleoproteinsRNA-Binding ProteinsRNA, Messenger3' Untranslated RegionsDNA-Binding ProteinsGlobinsHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0Heterogeneous-Nuclear Ribonucleoprotein KHeterogeneous-Nuclear RibonucleoproteinsHNRNPD protein, humanPCBP1 protein, humanPyrimidinesRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerTranscription Factors

Identifiers

PMID10373506
PMCPMC84255
OpenAlexW2115018128

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.