Evidence map›Paper›PMID 24695731›Full record

ReviewThe Journal of biological chemistry2014

Structural and dynamical features of inteins and implications on protein splicing.

Ertan Eryilmaz, Neel H Shah, Tom W Muir, David Cowburn

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

44 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. An artificially split class 3 intein.microPublication biology · 2023
    Article
  14. Review
  15. Calcimycin InhibitsACS infectious diseases · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Ertan EryilmazFrom the Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461 and.
Neel H Shahthe Department of Chemistry, Frick Laboratory, Princeton University, Princeton, New Jersey 08544.
Tom W Muirthe Department of Chemistry, Frick Laboratory, Princeton University, Princeton, New Jersey 08544.
David CowburnFrom the Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461 and david.cowburn@einstein.yu.edu.
Albert Einstein College of Medicine · US

Funding

Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Structure, Function and Applications of InteinsR01GM086868 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2008 to 2025
$4.4M
NIGMS NIH HHS GM086868NIGMS NIH HHS R01 GM086868NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Protein splicing is a posttranslational modification where intervening proteins (inteins) cleave themselves from larger precursor proteins and ligate their flanking polypeptides (exteins) through a multistep chemical reaction. First thought to be an anomaly found in only a few organisms, protein splicing by inteins has since been observed in microorganisms from all domains of life. Despite this broad phylogenetic distribution, all inteins share common structural features such as a horseshoe-like pseudo two-fold symmetric fold, several canonical sequence motifs, and similar splicing mechanisms. Intriguingly, the splicing efficiencies and substrate specificity of different inteins vary considerably, reflecting subtle changes in the chemical mechanism of splicing, linked to their local structure and dynamics. As intein chemistry has widespread use in protein chemistry, understanding the structural and dynamical aspects of inteins is crucial for intein engineering and the improvement of intein-based technologies.

Indexed as

Amino AcidsCatalytic DomainInteinsModels, MolecularMutationProtein FoldingProtein PrecursorsProteinsProtein SplicingProtein Structure, TertiaryAmino AcidsProtein PrecursorsProteinsInteinNMRProtein EngineeringProtein FoldingProtein-Protein InteractionsProtein SplicingProtein Structure

Identifiers

PMID24695731
PMCPMC4031508
OpenAlexW2009695514

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.