Evidence map›Paper›PMID 27043825›Full record

ArticlePloS one2016

CPAD, Curated Protein Aggregation Database: A Repository of Manually Curated Experimental Data on Protein and Peptide Aggregation.

A Mary Thangakani, R Nagarajan, Sandeep Kumar, R Sakthivel, D Velmurugan, M Michael Gromiha

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Prediction and Evaluation of Protein Aggregation with Computational Methods.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
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  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. AntiTbPdb: a knowledgebase of anti-tubercular peptides.Database : the journal of biological databases and curation · 2018
    Article
  17. Article
  18. Article
  19. Challenges in structural approaches to cell modeling.Journal of molecular biology · 2016
    Review
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

6 authors at 3 institutions in 2 countries.

A Mary ThangakaniCenter for Advanced Studies in Crystallography and Biophysics and Bioinformatics Infrastructure Facility, University of Madras, Chennai, 600025, India.
R NagarajanDepartment of Biotechnology, Bhupat and Jyoti Metha School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.
Sandeep KumarBiotherapeutics Pharmaceutical Sciences, Pfizer Inc., 700 Chesterfield Parkway West, Chesterfield, Missouri, 63017, United States of America.
R SakthivelDepartment of Biotechnology, Bhupat and Jyoti Metha School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.
D VelmuruganCenter for Advanced Studies in Crystallography and Biophysics and Bioinformatics Infrastructure Facility, University of Madras, Chennai, 600025, India.
M Michael GromihaDepartment of Biotechnology, Bhupat and Jyoti Metha School of Biosciences, Indian Institute of Technology Madras, Chennai, 600036, India.
Indian Institute of Technology Madras · INUniversity of Madras · INPfizer (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Accurate distinction between peptide sequences that can form amyloid-fibrils or amorphous β-aggregates, identification of potential aggregation prone regions in proteins, and prediction of change in aggregation rate of a protein upon mutation(s) are critical to research on protein misfolding diseases, such as Alzheimer's and Parkinson's, as well as biotechnological production of protein based therapeutics. We have developed a Curated Protein Aggregation Database (CPAD), which has collected results from experimental studies performed by scientific community aimed at understanding protein/peptide aggregation. CPAD contains more than 2300 experimentally observed aggregation rates upon mutations in known amyloidogenic proteins. Each entry includes numerical values for the following parameters: change in rate of aggregation as measured by fluorescence intensity or turbidity, name and source of the protein, Uniprot and Protein Data Bank codes, single point as well as multiple mutations, and literature citation. The data in CPAD has been supplemented with five different types of additional information: (i) Amyloid fibril forming hexa-peptides, (ii) Amorphous β-aggregating hexa-peptides, (iii) Amyloid fibril forming peptides of different lengths, (iv) Amyloid fibril forming hexa-peptides whose crystal structures are available in the Protein Data Bank (PDB) and (v) Experimentally validated aggregation prone regions found in amyloidogenic proteins. Furthermore, CPAD is linked to other related databases and resources, such as Uniprot, Protein Data Bank, PUBMED, GAP, TANGO, WALTZ etc. We have set up a web interface with different search and display options so that users have the ability to get the data in multiple ways. CPAD is freely available at http://www.iitm.ac.in/bioinfo/CPAD/. The potential applications of CPAD have also been discussed.

Indexed as

Databases, ProteinPeptidesProtein Aggregation, PathologicalProteinsAmyloidogenic ProteinsAnimalsDatabases, GeneticHumansMutationStructure-Activity RelationshipWeb BrowserAmyloidogenic ProteinsPeptidesProteins

Identifiers

PMID27043825
PMCPMC4820268
OpenAlexW2339837954

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.