Evidence map›Paper›PMID 35606511›Full record

ArticleCommunications biology2022

Opening opportunities for K

Janine-Denise Kopicki, Ankur Saikia, Stephan Niebling, Christian Günther, Raghavendra Anjanappa, Maria Garcia-Alai, Sebastian Springer, Charlotte Uetrecht

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Janine-Denise KopickiCentre for Structural Systems Biology (CSSB), Leibniz Institute of Virology (LIV), Notkestraße 85, 22607, Hamburg, Germany.ORCID 0000-0001-9806-5352
Ankur SaikiaLife Sciences and Chemistry School of Science, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.ORCID 0000-0002-7169-5765
Stephan NieblingCentre for Structural Systems Biology (CSSB), European Molecular Biology Laboratory - Hamburg Outstation, Notkestraße 85, Hamburg, 22607, Germany.
Christian GüntherCentre for Structural Systems Biology (CSSB), European Molecular Biology Laboratory - Hamburg Outstation, Notkestraße 85, Hamburg, 22607, Germany.
Raghavendra AnjanappaLife Sciences and Chemistry School of Science, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.
Maria Garcia-AlaiCentre for Structural Systems Biology (CSSB), European Molecular Biology Laboratory - Hamburg Outstation, Notkestraße 85, Hamburg, 22607, Germany.
Sebastian SpringerLife Sciences and Chemistry School of Science, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany. s.springer@jacobs-university.de.ORCID 0000-0002-5527-6149
Charlotte UetrechtCentre for Structural Systems Biology (CSSB), Leibniz Institute of Virology (LIV), Notkestraße 85, 22607, Hamburg, Germany. charlotte.uetrecht@cssb-hamburg.de.ORCID 0000-0002-1991-7922
Constructor University · DEEuropean Molecular Biology Laboratory · DEUniversity of Siegen · DE

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COHEN, BRUCE E · 1985 to 2011
$17.6M
NCRR NIH HHS P41 RR001081
6 · The paper itself

Abstract

An essential element of adaptive immunity is selective binding of peptide antigens by major histocompatibility complex (MHC) class I proteins and their presentation to cytotoxic T lymphocytes. Using native mass spectrometry, we analyze the binding of peptides to an empty disulfide-stabilized HLA-A*02:01 molecule and, due to its unique stability, we determine binding affinities of complexes loaded with truncated or charge-reduced peptides. We find that the two anchor positions can be stabilized independently, and we further analyze the contribution of additional amino acid positions to the binding strength. As a complement to computational prediction tools, our method estimates binding strength of even low-affinity peptides to MHC class I complexes quickly and efficiently. It has huge potential to eliminate binding affinity biases and thus accelerate drug discovery in infectious diseases, autoimmunity, vaccine design, and cancer immunotherapy.

Indexed as

Histocompatibility Antigens Class IPeptidesHLA AntigensT-Lymphocytes, CytotoxicHistocompatibility Antigens Class IHLA AntigensPeptides

Identifiers

PMID35606511
PMCPMC9127112
OpenAlexW4281288685

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.