Evidence map›Paper›PMID 7756989›Full record

ArticleProtein science : a publication of the Protein Society1994

Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins.

S Pietrokovski

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing 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

66 citing papers in PubMed, 165 citations in OpenAlex.

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  14. vB_PaeM_MIJ3, a Novel Jumbo Phage InfectingFrontiers in microbiology · 2019
    Article
  15. Biotechnological Applications of Protein Splicing.Current protein & peptide science · 2019
    Review
  16. Review
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  18. Article
  19. Design of a Split Intein with Exceptional Protein Splicing Activity.Journal of the American Chemical Society · 2016
    Article
  20. Article

6 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

1 author at 1 institution in 1 country.

S PietrokovskiDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inteins (protein introns) are internal portions of protein sequences that are posttranslationally excised while the flanking regions are spliced together, making an additional protein product. Inteins have been found in a number of homologous genes in yeast, mycobacteria, and extreme thermophile archaebacteria. The inteins are probably multifunctional, autocatalyzing their own splicing, and some were also shown to be DNA endonucleases. The splice junction regions and two regions similar to homing endonucleases were thought to be the only common sequence features of inteins. This work analyzed all published intein sequences with recently developed methods for detecting weak, conserved sequence features. The methods complemented each other in the identification and assessment of several patterns characterizing the intein sequences. New intein conserved features are discovered and the known ones are quantitatively described and localized. The general sequence description of all the known inteins is derived from the motifs and their relative positions. The intein sequence description is used to search the sequence databases for intein-like proteins. A sequence region in a mycobacterial open reading frame possessing all of the intein motifs and absent from sequences homologous to both of its flanking sequences is identified as an intein. A newly discovered putative intein in red algae chloroplasts is found not to contain the endonuclease motifs present in all other inteins. The yeast HO endonuclease is found to have an overall intein-like structure and a few viral polyprotein cleavage sites are found to be significantly similar to the inteins amino-end splice junction motif. The intein features described may serve for detection of intein sequences.

Indexed as

DNA HelicasesIntronsProtein Processing, Post-TranslationalAmino Acid SequenceBacterial ProteinsDeoxyribonucleases, Type II Site-SpecificDnaB HelicasesFungal ProteinsMolecular Sequence DataMycobacterium lepraeOpen Reading FramesPlant ProteinsProteinsRhodophytaSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBacterial ProteinsDeoxyribonucleases, Type II Site-SpecificDnaB HelicasesDNA HelicasesFungal ProteinsHO protein, S cerevisiaePlant Proteinspps1 protein, Mycobacterium sp.ProteinsSaccharomyces cerevisiae ProteinsSCEI protein, S cerevisiae

Identifiers

PMID7756989
PMCPMC2142770
OpenAlexW2047944454

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.