Evidence map›Paper›PMID 11350927›Full record

ArticleThe EMBO journal2001

Autoproteolysis and feedback in a protease cascade directing Drosophila dorsal-ventral cell fate.

M Dissing, H Giordano, R DeLotto

Abstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

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  11. Endocytosis is required for Toll signaling and shaping of the Dorsal/NF-kappaB morphogen gradient during Drosophila embryogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2010
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  12. Article
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  15. A single modular serine protease integrates signals from pattern-recognition receptors upstream of the Drosophila Toll pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009
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  16. Article
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  20. Genome-wide identification of mRNAs associated with the translational regulator PUMILIO in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 2006
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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

3 authors.

M DissingDepartment of Genetics, Institute of Molecular Biology, University of Copenhagen, Oster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark.
H Giordano
R DeLotto

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three serine protease zymogens, Gastrulation defective (GD), Snake (Snk) and Easter (Ea), and a nerve growth factor-like growth factor ligand precursor, Spaetzle, are required for specification of dorsal- ventral cell fate during Drosophila embryogenesis. The proteases have been proposed to function in a sequential activation cascade within the extracellular compartment called the perivitelline space. We examined biochemical interactions between these four proteins using a heterologous co-expression system. The results indicate that the three proteases do function in a sequential activation cascade, that GD becomes active and initiates the cascade and that interaction between GD and Snk is sufficient for GD to cleave itself autoproteolytically. The proteolytically active form of Ea cleaves GD at a different position, revealing biochemical feedback in the pathway. Both GD and Snk bind to heparin-Sepharose, providing a link between the pipe-defined ventral prepattern and the protease cascade. Our results suggest a model of the cascade in which initiation is by relief from inhibition, and spatial regulation of activity is due to interaction with sulfated proteoglycans.

Indexed as

Drosophila ProteinsProtein Processing, Post-TranslationalAnimalsCell DifferentiationCell LineageDrosophila melanogasterEnzyme ActivationEnzyme PrecursorsFeedbackHeparinInsect ProteinsSerine EndopeptidasesDrosophila Proteinsea protein, DrosophilaEnzyme PrecursorsHeparinInsect ProteinsSerine Endopeptidasessnk protein, Drosophilaspz protein, Drosophila

Identifiers

PMID11350927
PMCPMC125460

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.