Evidence map›Paper›PMID 32696355›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

Exploring Protein Intrinsic Disorder with MobiDB.

Alexander Miguel Monzon, András Hatos, Marco Necci, Damiano Piovesan, Silvio C E Tosatto

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. 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

5 authors.

Alexander Miguel MonzonDepartment of Biomedical Sciences, University of Padua, Padua, Italy.
András HatosDepartment of Biomedical Sciences, University of Padua, Padua, Italy.
Marco NecciDepartment of Biomedical Sciences, University of Padua, Padua, Italy.
Damiano PiovesanDepartment of Biomedical Sciences, University of Padua, Padua, Italy.
Silvio C E TosattoDepartment of Biomedical Sciences, University of Padua, Padua, Italy. silvio.tosatto@unipd.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nowadays, it is well established that many proteins or regions under physiological conditions lack a fixed three-dimensional structure and are intrinsically disordered. MobiDB is the main repository of protein disorder and mobility annotations, combining different data sources to provide an exhaustive overview of intrinsic disorder. MobiDB includes curated annotations from other databases, indirect disorder evidence from structural data, and disorder predictions from protein sequences. It provides an easy-to-use web server to visualize and explore disorder information. This chapter describes the data available in MobiDB, emphasizing how to use and access the intrinsic disorder data. MobiDB is available at URL http://mobidb.bio.unipd.it .

Indexed as

Databases, Proteinbeta CateninIntrinsically Disordered ProteinsModels, MolecularMolecular Sequence Annotationbeta CateninIntrinsically Disordered ProteinsDatabaseDisorder annotationDisorder predictionIDPIDRIntrinsically disordered proteinsIntrinsically disordered regionsIntrinsic disorderMobiDBStructural flexibility

Identifiers

PMID32696355

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.