ReviewFrontiers in bioscience (Landmark edition)2009
Structural conservation of a short, functional, peptide-sequence motif.
Review in Frontiers in bioscience (Landmark edition), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- Genome-wide identification, characterization, and expression profile analysis of the caffeic acid O-methyltransferases gene family in sweet orange (Citrus sinensis L.) in response to Penicillium digitatum infection.BMC plant biology · 2026Article
- ELM: the status of the 2010 eukaryotic linear motif resource.Nucleic acids research · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Full length, eukaryotic proteins generally consist of several autonomously folding and functioning domains. Many of these domains are known to function by binding and/or modifying other partner proteins based on the recognition of a short, linear amino sequence contained within the target protein. This article reviews the many bioinformatic tools and resources which discover, define and catalogue the various, known protein domains as well as assist users by identifying domain signatures within proteins of interest. We also review the smaller subset of bioinformatic tools which catalogue and help identify the short linear motifs used for domain targeting. It has been suggested that these short, functional, peptide-sequence motifs are normally found in unstructured regions of the target. The role of protein structure in the activity of one representative of these short, functional motifs is explored through an examination of known structures deposited in the Protein Data Bank.
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What OpenQuestion holds
Registered trials
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.