Evidence map›Paper›PMID 17146673›Full record

ReviewNaunyn-Schmiedeberg's archives of pharmacology2007

C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins.

Martin Vogelsgesang, Alexander Pautsch, Klaus Aktories

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Naunyn-Schmiedeberg's archives of pharmacology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

51 citing papers in PubMed, 108 citations in OpenAlex.

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  15. Boosting Antitumor Drug Efficacy with Chemically Engineered Multidomain Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018
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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 at 2 institutions in 2 countries.

Martin VogelsgesangInstitut für Experimentelle und Klinische Pharmakologie und Toxikologie, Albert-Ludwigs-University Freiburg, Otto-Krayer-Haus, Albertstrasse 25, Freiburg, Germany.
Alexander Pautsch
Klaus Aktories
University of Freiburg · DEBoehringer Ingelheim (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The family of C3-like exoenzymes comprises seven bacterial ADP-ribosyltransferases of different origin. The common hallmark of these exoenzymes is the selective N-ADP-ribosylation of the low molecular mass GTP-binding proteins RhoA, B, and C and inhibition of signal pathways controlled by Rho GTPases. Therefore, C3-like exoenzymes were applied as pharmacological tools for analyses of cellular functions of Rho protein in numerous studies. Recent structural and functional analyses of C3-like exoenzymes provide detailed information on the molecular mechanisms and functional consequences of ADP-ribosylation catalyzed by these toxins. More recently additional non-enzymatic actions of C3-like ADP-ribosyltransferases have been identified showing that C3 transferases from Clostridium botulinum and Clostridium limosum form a GDI-like complex with the Ras-like low molecular mass GTPase Ral without ADP-ribosylation. These results add novel information on the molecular mode of action(s) of C3-like exoenzymes and are discussed in this review.

Indexed as

ADP Ribose TransferasesAnimalsBacterial ToxinsBotulinum ToxinsHumansModels, MolecularProtein Conformationral GTP-Binding Proteinsrho GTP-Binding ProteinsSubstrate SpecificityADP Ribose TransferasesBacterial ToxinsBotulinum Toxinsexoenzyme C3, Clostridium botulinumral GTP-Binding Proteinsrho GTP-Binding Proteins

Identifiers

PMID17146673
OpenAlexW2071670333

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.