Evidence map›Paper›PMID 9512547›Full record

ArticleNucleic acids research1998

Non-canonical inteins.

A E Gorbalenya

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Protein Splicing of Inteins: A Powerful Tool in Synthetic Biology.Frontiers in bioengineering and biotechnology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Posttranslational protein modification in Archaea.Microbiology and molecular biology reviews : MMBR · 2005
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. InBase, the Intein Database.Nucleic acids research · 2000
    Article
  17. Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocystis sp. PCC6803.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
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.

A E GorbalenyaM. P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782 Moscow Region, Russia. gorbalen@ncifcrf.gov
Chumakov Institute of Poliomyelitis and Viral Encephalitides · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous analyses have shown that inteins (protein splicing elements) employ two structural organizations: the 'canonical' Nintein-Dod-inteinC found in dozens of inteins and a 'non-canonical' Nintein-inteinC described in two inteins, where Nintein at the N-terminus and inteinC at the C-terminus are conserved domains involved in self-splicing and Dod is the Dod DNA endonuclease (DNase). In this study, four non-canonical inteins, each with unique structural features, have been identified using alignment-based Hidden Markov Models. A Nintein-inteinC intein, carrying an unprecedented replacement of the N-terminal catalytic Cys(Ser) by Ala, is described in a putative ATPase encoded by Methanococcus jannaschii . Three replicative proteins of Synechocystis spp. contain inteins with the organizations: (i) Nintein minus X minus inteinC over Dod, where X is an uncharacterized domain and Dod DNase is located in an alternative open reading frame (ORF) being embedded between two novel CG and YK domains; (ii) Nintein-HN-inteinC, where HN stands for phage-like DNase from the EX1H-HX3H family; (iii) Nintein>|<inteinC, where >|< indicates that the intein domains are associated with a disrupted host protein encoded by two spatially separated ORFs. The expression of some of these newly identified inteins may affect the intein hosts. The variety of structural forms of inteins could have evolved through invasion of self-splicing proteases by different mobile DNases or the departure of mobile DNases from canonical inteins.

Indexed as

Databases as TopicProtein SplicingSequence Homology, Amino AcidAdenosine TriphosphatasesAlanineAmino Acid SequenceBase SequenceBinding SitesConsensus SequenceConserved SequenceCyanobacteriaCysteineMethanococcusMolecular Sequence DataOpen Reading FramesPeptide LibraryAdenosine TriphosphatasesAlanineCysteinePeptide LibrarySerine

Identifiers

PMID9512547
PMCPMC147447
OpenAlexW1968337797

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.