Evidence map›Paper›PMID 3362858›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1988

Do exons code for structural or functional units in proteins?

T W Traut

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 146 citations in OpenAlex.

  1. TDP-43: [GU]-ardian of the transcriptome.Molecular neurodegeneration · 2026
    Review
  2. Monomeric and Oligomeric Decorsins of the Asian Medicinal LeechInternational journal of molecular sciences · 2025
    Article
  3. Review
  4. Genetic Profiling of the Full-LengthMicrobiology spectrum · 2023
    Article
  5. Genome-Wide Identification of Mango (Frontiers in plant science · 2019
    Article
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  15. How are close residues of protein structures distributed in primary sequence?Proceedings of the National Academy of Sciences of the United States of America · 1995
    Article
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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

1 author at 1 institution in 1 country.

T W TrautDepartment of Biochemistry, University of North Carolina School of Medicine, Chapel Hill 27599-7260.
University of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In considering the origin and evolution of proteins, the possibility that proteins evolved from exons coding for specific structure-function modules is attractive for its economy and simplicity but is not systematically supported by the available data. However, the number of correspondences between exons and units of protein structure-function that have so far been identified appears to be greater than expected by chance alone. The available data also show (i) that exons are fairly limited in size but are large enough to specify structure-function modules in proteins; (ii) that the position of introns for homologous domains in the same gene is reasonably stable, but there is also evidence for mechanisms that alter the position or existence of introns; and (iii) that it is possible that the observed relationship of exons to protein structure represents a degenerate state of an ancestral correspondence between exons and structure-function modules in proteins.

Indexed as

ExonsIntronsNucleic Acid ConformationProteinsStructure-Activity RelationshipProteins

Identifiers

PMID3362858
PMCPMC280119
OpenAlexW2131067627

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.