Evidence map›Paper›PMID 31301363›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2019

Decoding the PTM-switchboard of Notch.

Daniel Antfolk, Christian Antila, Kati Kemppainen, Sebastian K-J Landor, Cecilia Sahlgren

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
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  5. Modes of Notch signalling in development and disease.Nature reviews. Molecular cell biology · 2025
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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

5 authors.

Daniel AntfolkFaculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
Christian AntilaFaculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
Kati KemppainenFaculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
Sebastian K-J LandorFaculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland. Electronic address: sebastian.landor@abo.fi.
Cecilia SahlgrenFaculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland; Department of Biomedical Engineering, Institute for Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, the Netherlands. Electronic address: cecilia.sahlgren@abo.fi.

Funding

European Research Council 771168
6 · The paper itself

Abstract

The developmentally indispensable Notch pathway exhibits a high grade of pleiotropism in its biological output. Emerging evidence supports the notion of post-translational modifications (PTMs) as a modus operandi controlling dynamic fine-tuning of Notch activity. Although, the intricacy of Notch post-translational regulation, as well as how these modifications lead to multiples of divergent Notch phenotypes is still largely unknown, numerous studies show a correlation between the site of modification and the output. These include glycosylation of the extracellular domain of Notch modulating ligand binding, and phosphorylation of the PEST domain controlling half-life of the intracellular domain of Notch. Furthermore, several reports show that multiple PTMs can act in concert, or compete for the same sites to drive opposite outputs. However, further investigation of the complex PTM crosstalk is required for a complete understanding of the PTM-mediated Notch switchboard. In this review, we aim to provide a consistent and up-to-date summary of the currently known PTMs acting on the Notch signaling pathway, their functions in different contexts, as well as explore their implications in physiology and disease. Furthermore, we give an overview of the present state of PTM research methodology, and allude to a future with PTM-targeted Notch therapeutics.

Indexed as

AnimalsHumansProtein Processing, Post-TranslationalReceptors, NotchSignal TransductionReceptors, NotchGlycosylationNotchPhosphorylationPost-translational modificationsPTM

Identifiers

PMID31301363
PMCPMC7116576

What OpenQuestion holds

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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.