Evidence map›Paper›PMID 11967365›Full record

ArticleProtein science : a publication of the Protein Society2002

Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information.

Andrey V Kajava, Bostjan Kobe

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2002. 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
3.7field-weighted citation impact, top 6% 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, 117 citations in OpenAlex.

  1. Article
  2. Conserved leucine-rich repeat proteins in the adhesive projectile slime of velvet worms.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Identifying Natural Bioactive Peptides from the Common Octopus (International journal of molecular sciences · 2023
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  9. Article
  10. Designed leucine-rich repeat proteins bind two muramyl dipeptide ligands.Protein science : a publication of the Protein Society · 2021
    Article
  11. Article
  12. Article
  13. Pediatric Dilated Cardiomyopathy-AssociatedJournal of the American Heart Association · 2018
    Article
  14. Article
  15. LRRC3B is downregulated in non-small-cell lung cancer and inhibits cancer cell proliferation and invasion.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  16. Article
  17. Article
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  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

2 authors at 2 institutions in 2 countries.

Andrey V KajavaCenter for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, MD 20892, USA. kajava@helix.nih.gov
Bostjan Kobe
National Institutes of Health · USUniversity of Queensland · AU

Funding

MODELING THE STRUCTURES OF PROTEINS AND PROTEIN COMPLEXESZ01CT000259 · CIT · COMPUTER RESEARCH AND TECHNOLOGY · PI KAJAVA, ANDREY V · 1996 to 2002
–
Wellcome Trust
6 · The paper itself

Abstract

The three-dimensional structures of leucine-rich repeat (LRR)-containing proteins from five different families were previously predicted based on the crystal structure of the ribonuclease inhibitor, using an approach that combined homology-based modeling, structure-based sequence alignment of LRRs, and several rational assumptions. The structural models have been produced based on very limited sequence similarity, which, in general, cannot yield trustworthy predictions. Recently, the protein structures from three of these five families have been determined. In this report we estimate the quality of the modeling approach by comparing the models with the experimentally determined structures. The comparison suggests that the general architecture, curvature, "interior/exterior" orientations of side chains, and backbone conformation of the LRR structures can be predicted correctly. On the other hand, the analysis revealed that, in some cases, it is difficult to predict correctly the twist of the overall super-helical structure. Taking into consideration the conclusions from these comparisons, we identified a new family of bacterial LRR proteins and present its structural model. The reliability of the LRR protein modeling suggests that it would be informative to apply similar modeling approaches to other classes of solenoid proteins.

Indexed as

Models, MolecularNuclear ProteinsSchizosaccharomyces pombe ProteinsAmino Acid SequenceCell Cycle ProteinsFungal ProteinsGTPase-Activating ProteinsLeucineMolecular Sequence DataProtein ConformationRepetitive Sequences, Amino AcidSequence AlignmentCell Cycle ProteinsFungal ProteinsGTPase-Activating ProteinsLeucineNuclear ProteinsSchizosaccharomyces pombe Proteinssds22 protein, S pombe

Identifiers

PMID11967365
PMCPMC2373561
OpenAlexW1968723998

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.