Evidence map›Paper›PMID 22291027›Full record

ArticleThe Journal of biological chemistry2012

Proteome of Hydra nematocyst.

Prakash G Balasubramanian, Anna Beckmann, Uwe Warnken, Martina Schnölzer, Andreas Schüler, Erich Bornberg-Bauer, Thomas W Holstein, Suat Özbek

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 111 citations in OpenAlex.

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  9. Bioactive Peptides and Proteins from Centipede Venoms.Molecules (Basel, Switzerland) · 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

8 authors at 2 institutions in 1 country.

Prakash G BalasubramanianDepartment of Molecular Evolution and Genomics, Centre for Organismal Studies, University of Heidelberg, D48149 Münster, Germany.
Anna BeckmannDepartment of Molecular Evolution and Genomics, Centre for Organismal Studies, University of Heidelberg, D48149 Münster, Germany.
Uwe WarnkenFunctional Proteome Analysis, German Cancer Research Center (DKFZ), 69120 Heidelberg, D48149 Münster, Germany.
Martina SchnölzerFunctional Proteome Analysis, German Cancer Research Center (DKFZ), 69120 Heidelberg, D48149 Münster, Germany.
Andreas SchülerInstitute for Evolution and Biodiversity, University of Münster, D48149 Münster, Germany.
Erich Bornberg-BauerInstitute for Evolution and Biodiversity, University of Münster, D48149 Münster, Germany.
Thomas W HolsteinDepartment of Molecular Evolution and Genomics, Centre for Organismal Studies, University of Heidelberg, D48149 Münster, Germany. Electronic address: holstein@uni-hd.de.
Suat ÖzbekDepartment of Molecular Evolution and Genomics, Centre for Organismal Studies, University of Heidelberg, D48149 Münster, Germany. Electronic address: suat.oezbek@cos.uni-heidelberg.de.
Heidelberg University · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Stinging cells or nematocytes of jellyfish and other cnidarians represent one of the most poisonous and sophisticated cellular inventions in animal evolution. This ancient cell type is unique in containing a giant secretory vesicle derived from the Golgi apparatus. The organelle structure within the vesicle comprises an elastically stretched capsule (nematocyst) to which a long tubule is attached. During exocytosis, the barbed part of the tubule is accelerated with >5 million g in <700 ns, enabling a harpoon-like discharge (Nüchter, T., Benoit, M., Engel, U., Ozbek, S., and Holstein, T. W. (2006) Curr. Biol. 16, R316-R318). Hitherto, the molecular components responsible for the organelle's biomechanical properties were largely unknown. Here, we describe the proteome of nematocysts from the freshwater polyp Hydra magnipapillata. Our analysis revealed an unexpectedly complex secretome of 410 proteins with venomous and lytic but also adhesive or fibrous properties. In particular, the insoluble fraction of the nematocyst represents a functional extracellular matrix structure of collagenous and elastic nature. This finding suggests an evolutionary scenario in which exocytic vesicles harboring a venomous secretome assembled a sophisticated predatory structure from extracellular matrix motif proteins.

Indexed as

Evolution, MolecularAnimalsExocytosisExtracellular Matrix ProteinsHydraNematocystProteomeSecretory VesiclesExtracellular Matrix ProteinsProteome

Identifiers

PMID22291027
PMCPMC3323026
OpenAlexW2007134949

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.