Evidence map›Paper›PMID 33637753›Full record

ArticleNature communications2021

System-wide identification and prioritization of enzyme substrates by thermal analysis.

Amir Ata Saei, Christian M Beusch, Pierre Sabatier, Juan Astorga Wells, Hassan Gharibi, Zhaowei Meng, Alexey Chernobrovkin, Sergey Rodin, Katja Näreoja, Ann-Gerd Thorsell and 8 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

32 citing papers in PubMed, 73 citations in OpenAlex.

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  20. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022
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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

18 authors at 5 institutions in 3 countries.

Amir Ata Saei *Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. Amirata.Saei.Dibavar@ki.se.ORCID http://orcid.org/0000-0002-2639-6328
Christian M Beusch *Division of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-9100-8283
Pierre SabatierDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-2734-1791
Juan Astorga WellsDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0003-1017-8841
Hassan GharibiDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-3072-4929
Zhaowei MengDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Alexey ChernobrovkinDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-7709-0161
Sergey RodinDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Katja NäreojaDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Ann-Gerd ThorsellDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Tobias KarlbergDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Qing ChengDivision of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Susanna L LundströmDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Massimiliano GaetaniDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0001-5610-0797
Ákos VégváriDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-1287-0906
Elias S J ArnérDivision of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.ORCID http://orcid.org/0000-0002-4807-6114
Herwig SchülerDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.ORCID http://orcid.org/0000-0003-4059-3501
Roman A ZubarevDivision of Physiological Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden. Roman.Zubarev@ki.se.ORCID http://orcid.org/0000-0001-9839-2089
Karolinska Institutet · SEHarvard University · USScience for Life Laboratory · SESechenov University · RUUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the immense importance of enzyme-substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change their thermal stability. In our proof-of-concept studies, SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, opening opportunities to investigate the effect of post-translational modifications on signal transduction and facilitate drug discovery.

Indexed as

Protein Processing, Post-TranslationalCarcinomaDrug DiscoveryEnzymesHCT116 CellsHumansMass SpectrometryPoly(ADP-ribose) PolymerasesProteinsProteomicsProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSubstrate SpecificityThioredoxin Reductase 1EnzymesPARP10 protein, humanPoly(ADP-ribose) PolymerasesProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-aktThioredoxin Reductase 1TXNRD1 protein, human

Identifiers

PMID33637753
PMCPMC7910609
OpenAlexW3131784305

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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.