Evidence map›Paper›PMID 24848016›Full record

ArticleNucleic acids research2014

PASTA 2.0: an improved server for protein aggregation prediction.

Ian Walsh, Flavio Seno, Silvio C E Tosatto, Antonio Trovato

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 233 papers.

0numbers the graph read from it
0cells of the map it votes in
233citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

233 citing papers in PubMed, 483 citations in OpenAlex.

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  7. amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Predicting Peptide Aggregation with Protein Language Model Embeddings.Journal of chemical information and modeling · 2026
    Article
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173 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

4 authors at 2 institutions in 1 country.

Ian WalshDepartment of Biomedical Sciences, University of Padova, Padova I-35131, Italy.
Flavio SenoINFN, Padova Section, and Department of Physics and Astronomy 'G. Galilei', University of Padova, Padova I-35121, Italy.
Silvio C E TosattoDepartment of Biomedical Sciences, University of Padova, Padova I-35131, Italy silvio.tosatto@unipd.it.
Antonio TrovatoINFN, Padova Section, and Department of Physics and Astronomy 'G. Galilei', University of Padova, Padova I-35121, Italy.
Istituto Nazionale di Fisica Nucleare, Sezione di Padova · ITUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The formation of amyloid aggregates upon protein misfolding is related to several devastating degenerative diseases. The propensities of different protein sequences to aggregate into amyloids, how they are enhanced by pathogenic mutations, the presence of aggregation hot spots stabilizing pathological interactions, the establishing of cross-amyloid interactions between co-aggregating proteins, all rely at the molecular level on the stability of the amyloid cross-beta structure. Our redesigned server, PASTA 2.0, provides a versatile platform where all of these different features can be easily predicted on a genomic scale given input sequences. The server provides other pieces of information, such as intrinsic disorder and secondary structure predictions, that complement the aggregation data. The PASTA 2.0 energy function evaluates the stability of putative cross-beta pairings between different sequence stretches. It was re-derived on a larger dataset of globular protein domains. The resulting algorithm was benchmarked on comprehensive peptide and protein test sets, leading to improved, state-of-the-art results with more amyloid forming regions correctly detected at high specificity. The PASTA 2.0 server can be accessed at http://protein.bio.unipd.it/pasta2/.

Indexed as

SoftwareAlgorithmsAmyloidInternetIntrinsically Disordered ProteinsPeptidesPoint MutationProtein Structure, SecondarySequence Analysis, ProteinAmyloidIntrinsically Disordered ProteinsPeptides

Identifiers

PMID24848016
PMCPMC4086119
OpenAlexW2080831965

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.