ArticleRedox biology2020
Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16
Open access · goldAbstract read
In one paragraph
Article in Redox biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
What it found
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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.
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.
Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- The impact of physiological oxidants on triggering amyloid formation of the cell cycle regulator protein p16Protein science : a publication of the Protein Society · 2026Article
- Article
- Characterizing the amyloid core region of the tumor suppressor protein p16The Journal of biological chemistry · 2024Article
- Amyloid formation and depolymerization of tumor suppressor p16Nature communications · 2024Article
- Redox proteomics of PANC-1 cells reveals the significance of HIF-1 signaling protein oxidation in pancreatic ductal adenocarcinoma pathogenesis.Journal of translational medicine · 2024Article
- Oxidation Promotes Distinct Huntingtin Aggregates in the Presence and Absence of Membranes.Biochemistry · 2022Article
- Reaction ofInternational journal of molecular sciences · 2022Article
- Bioinformatic identification of previously unrecognized amyloidogenic proteins.The Journal of biological chemistry · 2022Article
- Cancer metabolism and tumor microenvironment: fostering each other?Science China. Life sciences · 2022Review
- Mitochondria inter-organelle relationships in cancer protein aggregation.Frontiers in cell and developmental biology · 2022Review
- Endogenous SORedox biology · 2021Article
- Review
- Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
- Cross-talk between redox signalling and protein aggregation.Biochemical Society transactions · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 5 institutions in 3 countries.
Christoph GöblCenter for Integrated Protein Science Munich (CIPSM) at the Department of Chemistry Technische Universität München, Lichtenbergstr. 4, 85747, Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Vanessa K MorrisCenter for Integrated Protein Science Munich (CIPSM) at the Department of Chemistry Technische Universität München, Lichtenbergstr. 4, 85747, Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Loes van DamCenter for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands.
Marieke VisscherCenter for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands.
Paulien E PoldermanCenter for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands.
Christoph HartlmüllerCenter for Integrated Protein Science Munich (CIPSM) at the Department of Chemistry Technische Universität München, Lichtenbergstr. 4, 85747, Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Hesther de RuiterCenter for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands.
Manuel HoraCenter for Integrated Protein Science Munich (CIPSM) at the Department of Chemistry Technische Universität München, Lichtenbergstr. 4, 85747, Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Laura LiesingerOmics Center Graz, BioTechMed-Graz, Graz, Austria; Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, 8010, Graz, Austria.
Ruth Birner-GruenbergerOmics Center Graz, BioTechMed-Graz, Graz, Austria; Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, 8010, Graz, Austria.
Harmjan R VosCenter for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands.
Bernd ReifCenter for Integrated Protein Science Munich (CIPSM) at the Department of Chemistry Technische Universität München, Lichtenbergstr. 4, 85747, Garching, Germany; Institute of Structural Biology, Helmholtz Zentrum München, 85764, Neuherberg, Germany.
Tobias MadlGottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, 8010, Graz, Austria; BioTechMed-Graz, Austria. Electronic address: tobias.madl@medunigraz.at.
Tobias B DansenCenter for Molecular Medicine, Molecular Cancer Research, University Medical Center Utrecht, Universiteitsweg 100, 3584CG, Utrecht, The Netherlands. Electronic address: T.B.Dansen@umcutrecht.nl.
University Medical Center Utrecht · NLMedical University of Graz · ATCenter for Integrated Protein Science Munich · DETechnical University of Munich · DEHelmholtz Zentrum München · DE
Funding
Austrian Science Fund FWF I 3792Austrian Science Fund FWF KLI 425Austrian Science Fund FWF KLI 645Austrian Science Fund FWF P 28854Austrian Science Fund FWF W 1226
Abstract
The tumor suppressor p16
Indexed as
AmyloidCell CycleCellular SenescenceCyclin-Dependent Kinase Inhibitor p16CysteineHEK293 CellsHumansModels, MolecularOxidation-ReductionProtein MultimerizationProtein Structure, SecondaryAmyloidCDKN2A protein, humanCyclin-Dependent Kinase Inhibitor p16CysteineAmyloidsCysteine oxidationProtein aggregationRedox signalingStructural biology
Identifiers
What OpenQuestion holds
Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390
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.