ArticleF1000 biology reports2009
Diversity of protein structures and difficulties in fold recognition: the curious case of protein G.
Article in F1000 biology reports, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Exploring Polypharmacology in Drug Discovery and Repurposing Using the CANDO Platform.Current pharmaceutical design · 2016Review
- Amelogenin in Enamel Tissue Engineering.Advances in experimental medicine and biology · 2015Article
- The Promise and Challenge of Digital Biology.Journal of bioengineering & biomedical science · 2013Article
- Disease risk of missense mutations using structural inference from predicted function.Current protein & peptide science · 2010Article
- Prospects and Pits on the Path of Biomimetics: The case of tooth enamel.Journal of biomimetics, biomaterials, and tissue engineering · 2010Article
- A protein sequence meta-functional signature for calcium binding residue prediction.Pattern recognition letters · 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
2 authors.
Funding
Abstract
We examine the ability of current state-of-the-art methods in protein structure prediction to discriminate topologically distant folds encoded by highly similar (>90% sequence identity) designed proteins in blind protein structure prediction experiments. We detail the corresponding prognosis for the protein fold recognition field and highlight the features of the methodologies that successfully deciphered this folding riddle.
Identifiers
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.