Evidence map›Paper›PMID 7527560›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

cDNA cloning of the Sm proteins D2 and D3 from human small nuclear ribonucleoproteins: evidence for a direct D1-D2 interaction.

T Lehmeier, V Raker, H Hermann, R Lührmann

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 65 citations in OpenAlex.

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  6. Evolutionarily conserved protein ERH controls CENP-E mRNA splicing and is required for the survival of KRAS mutant cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2012
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  12. The spliceosomal snRNP core complex of Trypanosoma brucei: cloning and functional analysis reveals seven Sm protein constituents.Proceedings of the National Academy of Sciences of the United States of America · 2000
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  19. Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 1997
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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

4 authors at 1 institution in 1 country.

T LehmeierInstitut für Molekularbiologie und Tumorforschung, Philipps-Universität Marburg, Germany.
V Raker
H Hermann
R Lührmann
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/U6, and U5 share a set of common proteins denoted B/B', D1, D2, D3, E, F, and G which play an important part in the biogenesis of the snRNPs. In addition, there is a link between the common proteins and autoimmunity; the three D proteins, together with B/B', are the major autoantigens for the so-called anti-Sm antibodies often produced by patients suffering from systemic lupus erythematosus. Here we describe the characterization of the human proteins D2 and D3 by cDNA cloning and immunological methods. D2 and D3 are encoded by distinct genes and are 118 and 126 amino acids in length, respectively. Both proteins prepared by in vitro translation exhibit Sm epitopes and can be precipitated by anti-Sm autoantibodies. They react differently with various patient sera, in a manner consistent with the reaction pattern on immunoblots of the D proteins isolated from HeLa cells. D1 and D2 synthesized in vitro form specific complexes, a result that is significant for the assembly pathway of the various core proteins into an snRNP's core ribonucleoprotein structure. The D3 protein is homologous to the human D1 protein, showing an overall amino acid sequence identity of 29%, including two regions with over 60% identity. D2 has less than 15% sequence identity with D1 and D3. A data bank search revealed a striking similarity (with more than 40% sequence identity) between human D3 and a Saccharomyces cerevisiae gene, previously published as the 5' flanking gene of yeast pep3 [Preston, R.A., Manolson, M., Becherer, K., Weidenhammer, E., Kirkpatrick, D., Wright, R. & Jones, E. (1991) Mol. Cell. Biol. 11, 5801-5812], suggesting that this gene encodes the yeast homologue of the human D3 protein.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceAntibodies, MonoclonalAutoantibodiesAutoantigensBase SequenceCloning, MolecularDNA, ComplementaryEpitopesFungal ProteinsHeLa CellsHumansLupus Erythematosus, SystemicMolecular Sequence DataRibonucleoproteins, Small NuclearSaccharomyces cerevisiaeAntibodies, MonoclonalAutoantibodiesAutoantigensDNA, ComplementaryEpitopesFungal ProteinsRibonucleoproteins, Small NuclearSaccharomyces cerevisiae ProteinsSMD1 protein, S cerevisiaeSm protein D2Sm protein D3snRNP Core Proteins

Identifiers

PMID7527560
PMCPMC45428
OpenAlexW2093307415

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.