Evidence map›Paper›PMID 16407336›Full record

ArticleNucleic acids research2006

Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins.

Chad Haynes, Lilia M Iakoucheva

Abstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
–field-weighted citation impact
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

69 citing papers in PubMed.

  1. Article
  2. Exploring Disordered Regions of Human Spliceosome Proteins.The journal of physical chemistry letters · 2026
    Article
  3. Article
  4. Tumor-promoting effect and tumor immunity of SRSFs.Frontiers in cell and developmental biology · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14.International journal of molecular sciences · 2021
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

9 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

2 authors.

Chad HaynesThe Rockefeller University, Laboratory of Statistical Genetics, 1230 York Avenue, New York, NY 10021, USA.
Lilia M Iakoucheva

Funding

Protein structural disorder and ubiquitinationR21CA113711 · NCI · ROCKEFELLER UNIVERSITY · PI IAKOUCHEVA, LILIA M · 2007 to 2008
$356k
NCI NIH HHS R21 CA113711
6 · The paper itself

Abstract

Serine/arginine-rich (SR) splicing factors play an important role in constitutive and alternative splicing as well as during several steps of RNA metabolism. Despite the wealth of functional information about SR proteins accumulated to-date, structural knowledge about the members of this family is very limited. To gain a better insight into structure-function relationships of SR proteins, we performed extensive sequence analysis of SR protein family members and combined it with ordered/disordered structure predictions. We found that SR proteins have properties characteristic of intrinsically disordered (ID) proteins. The amino acid composition and sequence complexity of SR proteins were very similar to those of the disordered protein regions. More detailed analysis showed that the SR proteins, and their RS domains in particular, are enriched in the disorder-promoting residues and are depleted in the order-promoting residues as compared to the entire human proteome. Moreover, disorder predictions indicated that RS domains of SR proteins were completely unstructured. Two different classification methods, the charge-hydropathy measure and the cumulative distribution function (CDF) of the disorder scores, were in agreement with each other, and they both strongly predicted members of the SR protein family to be disordered. This study emphasizes the importance of the disordered structure for several functions of SR proteins, such as for spliceosome assembly and for interaction with multiple partners. In addition, it demonstrates the usefulness of order/disorder predictions for inferring protein structure from sequence.

Indexed as

RNA SplicingAmino AcidsArginineHumansProtein Structure, TertiaryRNA-Binding ProteinsSequence Analysis, ProteinSerineAmino AcidsArginineRNA-Binding ProteinsSerine

Identifiers

PMID16407336
PMCPMC1326245

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.