Evidence map›Paper›PMID 32500917›Full record

ArticleDatabase : the journal of biological databases and curation2020

Obtaining extremely large and accurate protein multiple sequence alignments from curated hierarchical alignments.

Andrew F Neuwald, Christopher J Lanczycki, Theresa K Hodges, Aron Marchler-Bauer

Open access · goldAbstract read
In one paragraph

Article in Database : the journal of biological databases and curation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. SPARC: Structural properties associated with residue constraints.Computational and structural biotechnology journal · 2022
    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

4 authors at 2 institutions in 1 country.

Andrew F NeuwaldInstitute for Genome Sciences.
Christopher J LanczyckiNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Building 38 A, 8600 Rockville Pike, Bethesda, MD 20894, USA.
Theresa K HodgesInstitute for Genome Sciences.
Aron Marchler-BauerNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Building 38 A, 8600 Rockville Pike, Bethesda, MD 20894, USA.
National Institutes of Health · USUniversity of Maryland, Baltimore · US

Funding

National Biomedical Information ServicesZIHLM200888 · NLM · NATIONAL LIBRARY OF MEDICINE · PI PALTOO, DINA · 2009 to 2025
$5200.7M
Advanced correlation analyses to infer sequence and structural determinants of protein functionR01GM125878 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI NEUWALD, ANDREW F · 2018 to 2021
$1.3M
NIGMS NIH HHS R01 GM125878
6 · The paper itself

Abstract

For optimal performance, machine learning methods for protein sequence/structural analysis typically require as input a large multiple sequence alignment (MSA), which is often created using query-based iterative programs, such as PSI-BLAST or JackHMMER. However, because these programs align database sequences using a query sequence as a template, they may fail to detect or may tend to misalign sequences distantly related to the query. More generally, automated MSA programs often fail to align sequences correctly due to the unpredictable nature of protein evolution. Addressing this problem typically requires manual curation in the light of structural data. However, curated MSAs tend to contain too few sequences to serve as input for statistically based methods. We address these shortcomings by making publicly available a set of 252 curated hierarchical MSAs (hiMSAs), containing a total of 26 212 066 sequences, along with programs for generating from these extremely large MSAs. Each hiMSA consists of a set of hierarchically arranged MSAs representing individual subgroups within a superfamily along with template MSAs specifying how to align each subgroup MSA against MSAs higher up the hierarchy. Central to this approach is the MAPGAPS search program, which uses a hiMSA as a query to align (potentially vast numbers of) matching database sequences with accuracy comparable to that of the curated hiMSA. We illustrate this process for the exonuclease-endonuclease-phosphatase superfamily and for pleckstrin homology domains. A set of extremely large MSAs generated from the hiMSAs in this way is available as input for deep learning, big data analyses. MAPGAPS, auxiliary programs CDD2MGS, AddPhylum, PurgeMSA and ConvertMSA and links to National Center for Biotechnology Information data files are available at https://www.igs.umaryland.edu/labs/neuwald/software/mapgaps/.

Indexed as

Databases, ProteinProteinsMachine LearningSequence AlignmentSequence Analysis, ProteinSoftwareProteins

Identifiers

PMID32500917
PMCPMC7297217
OpenAlexW3034038259

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.