Evidence map›Paper›PMID 28160322›Full record

ArticleProteins2017

ATLAS: A database linking binding affinities with structures for wild-type and mutant TCR-pMHC complexes.

Tyler Borrman, Jennifer Cimons, Michael Cosiano, Michael Purcaro, Brian G Pierce, Brian M Baker, Zhiping Weng

Abstract read
In one paragraph

Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

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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

7 authors.

Tyler BorrmanProgram in Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, Massachusetts, 01605.
Jennifer CimonsDepartment of Chemistry and Biochemistry and the Harper Cancer Research Institute, University of Notre Dame, Notre Dame, Indiana, 46556.
Michael CosianoDepartment of Chemistry and Biochemistry and the Harper Cancer Research Institute, University of Notre Dame, Notre Dame, Indiana, 46556.
Michael PurcaroProgram in Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, Massachusetts, 01605.
Brian G PierceUniversity of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, 20850.
Brian M BakerDepartment of Chemistry and Biochemistry and the Harper Cancer Research Institute, University of Notre Dame, Notre Dame, Indiana, 46556.
Zhiping WengProgram in Bioinformatics and Integrative Biology, University of Massachusetts Medical School, Worcester, Massachusetts, 01605.ORCID 0000-0002-3032-7966

Funding

Structural biophysics and molecular design in cellular immunityR35GM118166 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BAKER, BRIAN M · 2016 to 2025
$4.4M
Development of a Computational Framework for TCR EngineeringR01GM103773 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BAKER, BRIAN M, WENG, ZHIPING · 2013 to 2016
$1.2M
NIGMS NIH HHS R01 GM103773NIGMS NIH HHS R35 GM118166
6 · The paper itself

Abstract

The ATLAS (Altered TCR Ligand Affinities and Structures) database (https://zlab.umassmed.edu/atlas/web/) is a manually curated repository containing the binding affinities for wild-type and mutant T cell receptors (TCRs) and their antigens, peptides presented by the major histocompatibility complex (pMHC). The database links experimentally measured binding affinities with the corresponding three dimensional (3D) structures for TCR-pMHC complexes. The user can browse and search affinities, structures, and experimental details for TCRs, peptides, and MHCs of interest. We expect this database to facilitate the development of next-generation protein design algorithms targeting TCR-pMHC interactions. ATLAS can be easily parsed using modeling software that builds protein structures for training and testing. As an example, we provide structural models for all mutant TCRs in ATLAS, built using the Rosetta program. Utilizing these structures, we report a correlation of 0.63 between experimentally measured changes in binding energies and our predicted changes. Proteins 2017; 85:908-916. © 2016 Wiley Periodicals, Inc.

Indexed as

Databases, FactualMutationSoftwareBinding SitesHistocompatibility Antigens Class IHumansInternetLigandsModels, MolecularPeptidesProtein BindingProtein ConformationReceptors, Antigen, T-CellThermodynamicsHistocompatibility Antigens Class ILigandsPeptidesReceptors, Antigen, T-Cell3D vieweradaptive immunitybinding energyprotein modelingRosettascoring functions

Identifiers

PMID28160322
PMCPMC5860664

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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.