Evidence map›Paper›PMID 10493576›Full record

ArticleProtein science : a publication of the Protein Society1999

Predicting conformational switches in proteins.

M Young, K Kirshenbaum, K A Dill, S Highsmith

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 73 citations in OpenAlex.

  1. Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024
    Article
  2. Article
  3. Inaccurate secondary structure predictions often indicate protein fold switching.Protein science : a publication of the Protein Society · 2019
    Article
  4. Comprehensive analysis of sequences of a protein switch.Protein science : a publication of the Protein Society · 2016
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Prion protein misfolding.Current molecular medicine · 2009
    Review
  12. Article
  13. Article
  14. Article
  15. The effect of long-range interactions on the secondary structure formation of proteins.Protein science : a publication of the Protein Society · 2005
    Article
  16. Article
  17. The PredictProtein server.Nucleic acids research · 2004
    Article
  18. On the properties and sequence context of structurally ambivalent fragments in proteins.Protein science : a publication of the Protein Society · 2003
    Article
  19. The PredictProtein server.Nucleic acids research · 2003
    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 2 institutions in 1 country.

M YoungDepartment of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
K Kirshenbaum
K A Dill
S Highsmith
University of California, San Francisco · USUniversity of the Pacific · US

Funding

STRUCTURE/FUNCTION OF MOLECULAR MOTORSP01AR042895 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COOKE, ROGER A · 1994 to 2008
$9.8M
BIOTECHNOLOGYT32GM008388 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI HUNT, C ANTHONY · 1990 to 1999
–
NIAMS NIH HHS AR42895NIGMS NIH HHS GM07175NIGMS NIH HHS GM08388
6 · The paper itself

Abstract

We describe a new computational technique to predict conformationally switching elements in proteins from their amino acid sequences. The method, called ASP (Ambivalent Structure Predictor), analyzes results from a secondary structure prediction algorithm to identify regions of conformational ambivalence. ASP identifies ambivalent regions in 16 test protein sequences for which function involves substantial backbone rearrangements. In the test set, all sites previously described as conformational switches are correctly predicted to be structurally ambivalent regions. No such regions are predicted in three negative control protein sequences. ASP may be useful as a guide for experimental studies on protein function and motion in the absence of detailed three-dimensional structural data.

Indexed as

Protein ConformationAdenylyl CyclasesAldehyde ReductaseBase SequenceComputational BiologyDNA-Binding ProteinsDNA Topoisomerases, Type IEnzyme ActivatorsGTP-Binding Protein alpha Subunits, GsHemagglutinin Glycoproteins, Influenza VirusModels, MolecularMyosinsNF-kappa BNF-kappa B p50 SubunitPeptide Elongation Factor TuPrionsAdenylyl CyclasesAldehyde ReductaseDNA-Binding ProteinsDNA Topoisomerases, Type IEnzyme ActivatorsGTP-Binding Protein alpha Subunits, GsHemagglutinin Glycoproteins, Influenza VirusMyosinsNF-kappa BNF-kappa B p50 SubunitPeptide Elongation Factor TuPrionsRecombinasesSerpinsTATA-Box Binding ProteinTranscription FactorsTransducinTransposases

Identifiers

PMID10493576
PMCPMC2144394
OpenAlexW2131782103

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.