Evidence map›Paper›PMID 31331936›Full record

ArticleThe Journal of biological chemistry2019

Autophosphorylation activates c-Src kinase through global structural rearrangements.

Edgar E Boczek, Qi Luo, Marco Dehling, Michael Röpke, Sophie L Mader, Andreas Seidl, Ville R I Kaila, Johannes Buchner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  17. Nuclear Functions of the Tyrosine Kinase Src.International journal of molecular sciences · 2020
    Review
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 2 institutions in 2 countries.

Edgar E BoczekCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany; Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Qi LuoCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany; Soft Matter Research Center and Department of Chemistry, Zhejiang University, Zhejiang Sheng 310027, China.
Marco DehlingCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany; Novartis Biologics Technical Development and Manufacturing, Sandoz Biopharmaceuticals, Hexal AG, 82041 Oberhaching, Germany.
Michael RöpkeCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany.
Sophie L MaderCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany.
Andreas SeidlNovartis Biologics Technical Development and Manufacturing, Sandoz Biopharmaceuticals, Hexal AG, 82041 Oberhaching, Germany.
Ville R I KailaCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany. Electronic address: ville.kaila@ch.tum.de.
Johannes BuchnerCenter for Integrated Protein Science, Department Chemie, Technische Universität München, 85748 Garching, Germany. Electronic address: johannes.buchner@tum.de.
Center for Integrated Protein Science Munich · DENovartis (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The prototypical kinase c-Src plays an important role in numerous signal transduction pathways, where its activity is tightly regulated by two phosphorylation events. Phosphorylation at a specific tyrosine by C-terminal Src kinase inactivates c-Src, whereas autophosphorylation is essential for the c-Src activation process. However, the structural consequences of the autophosphorylation process still remain elusive. Here we investigate how the structural landscape of c-Src is shaped by nucleotide binding and phosphorylation of Tyr

Indexed as

Deuterium Exchange MeasurementHumansMass SpectrometryMolecular Dynamics SimulationPhosphorylationProtein AggregatesProtein ConformationProto-Oncogene Proteins pp60(c-src)Protein AggregatesProto-Oncogene Proteins pp60(c-src)activationATPbiophysicsconformational changeenzyme mechanismhydrogen/deuterium exchangemolecular dynamicsoncogenephosphorylationprotein kinaseSrc

Identifiers

PMID31331936
PMCPMC6721954
OpenAlexW2962907733

What OpenQuestion holds

Textmetadata
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.