Evidence map›Paper›PMID 29604149›Full record

ArticleProtein science : a publication of the Protein Society2018

Functional classification of protein structures by local structure matching in graph representation.

Caitlyn L Mills, Rohan Garg, Joslynn S Lee, Liang Tian, Alexandru Suciu, Gene D Cooperman, Penny J Beuning, Mary Jo Ondrechen

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. 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
0.6field-weighted citation impact, top 35% 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

2 citing papers in PubMed, 11 citations in OpenAlex.

  1. CHARMM-GUIJournal of chemical information and modeling · 2021
    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

8 authors at 1 institution in 1 country.

Caitlyn L MillsDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.
Rohan GargCollege of Computer and Information Science, Northeastern University, Boston, Massachusetts.
Joslynn S LeeDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.
Liang TianDepartment of Mathematics, Northeastern University, Boston, Massachusetts.
Alexandru SuciuDepartment of Mathematics, Northeastern University, Boston, Massachusetts.
Gene D CoopermanCollege of Computer and Information Science, Northeastern University, Boston, Massachusetts.
Penny J BeuningDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.ORCID 0000-0002-7770-022X
Mary Jo OndrechenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts.
Northeastern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As a result of high-throughput protein structure initiatives, over 14,400 protein structures have been solved by Structural Genomics (SG) centers and participating research groups. While the totality of SG data represents a tremendous contribution to genomics and structural biology, reliable functional information for these proteins is generally lacking. Better functional predictions for SG proteins will add substantial value to the structural information already obtained. Our method described herein, Graph Representation of Active Sites for Prediction of Function (GRASP-Func), predicts quickly and accurately the biochemical function of proteins by representing residues at the predicted local active site as graphs rather than in Cartesian coordinates. We compare the GRASP-Func method to our previously reported method, Structurally Aligned Local Sites of Activity (SALSA), using the Ribulose Phosphate Binding Barrel (RPBB), 6-Hairpin Glycosidase (6-HG), and Concanavalin A-like Lectins/Glucanase (CAL/G) superfamilies as test cases. In each of the superfamilies, SALSA and the much faster method GRASP-Func yield similar correct classification of previously characterized proteins, providing a validated benchmark for the new method. In addition, we analyzed SG proteins using our SALSA and GRASP-Func methods to predict function. Forty-one SG proteins in the RPBB superfamily, nine SG proteins in the 6-HG superfamily, and one SG protein in the CAL/G superfamily were successfully classified into one of the functional families in their respective superfamily by both methods. This improved, faster, validated computational method can yield more reliable predictions of function that can be used for a wide variety of applications by the community.

Indexed as

Computational BiologyCatalytic DomainGlycoside HydrolasesLectinsPentosesProtein ConformationProteinsGlycoside HydrolasesLectinsPentosesProteinsribulose6-Hairpin Glycosidase (6-HG) superfamilyConcanavalin A-like Lectins/Glucanase (CAL/G) superfamilyGraph Representation of Active Sites for Prediction of Function (GRASP-Func)protein function annotationRibulose Phosphate Binding Barrel (RPBB) superfamilyStructurally Aligned Local Sites of Activity (SALSA)

Identifiers

PMID29604149
PMCPMC5980557
OpenAlexW2795174361

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.