Evidence map›Paper›PMID 17347522›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2007

Colicin biology.

Eric Cascales, Susan K Buchanan, Denis Duché, Colin Kleanthous, Roland Lloubès, Kathleen Postle, Margaret Riley, Stephen Slatin, Danièle Cavard

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 594 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
594citing papers in PubMed, 1 pooled it
15.6field-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

594 citing papers in PubMed, 1 synthesis or guideline pooled it, 989 citations in OpenAlex.

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534 more citing papers are in PubMed but not listed here.

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

9 authors at 5 institutions in 3 countries.

Eric CascalesLaboratoire d'Ingénierie des Systèmes Macromoléculaires,Institut de Biologie Structurale et Microbiologie, Centre National de la Recherche Scientifique, UPR 9027, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. cascales@ibsm.cnrs-mrs.fr
Susan K Buchanan
Denis Duché
Colin Kleanthous
Roland Lloubès
Kathleen Postle
Margaret Riley
Stephen Slatin
Danièle Cavard
Institut de Biologie Structurale · FRAlbert Einstein College of Medicine · USNational Institute of Diabetes and Digestive and Kidney Diseases · USPennsylvania State University · USUniversity of York · GB

Funding

ENERGY TRANSDUCTION BETWEEN MEMBRANESR01GM042146 · NIGMS · WASHINGTON STATE UNIVERSITY · PI POSTLE, KATHLEEN · 1991 to 2011
$4.7M
Evolution of Stress-Induced Bacterial ToxinsR01AI064588 · NIAID · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RILEY, MARGARET A. · 2007 to 2010
$1.5M
structual characterization of protein import across bacterial outer membranesZ01DK036140 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2007 to 2007
$386k
Structural characterization of energy transduction by Tol proteinsZ01DK011010 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2008 to 2008
$340k
Biotechnology and Biological Sciences Research Council BB/C516236/1Intramural NIH HHSNIAID NIH HHS R01 AI064588NIGMS NIH HHS R01 GM042146Wellcome Trust
6 · The paper itself

Abstract

Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic determinants for colicin synthesis, immunity, and release. Insights gained into each fundamental aspect of their biology are presented: their synthesis, which is under SOS regulation; their release into the extracellular medium, which involves the colicin lysis protein; and their uptake mechanisms and modes of action. Colicins are organized into three domains, each one involved in a different step of the process of killing sensitive bacteria. The structures of some colicins are known at the atomic level and are discussed. Colicins exert their lethal action by first binding to specific receptors, which are outer membrane proteins used for the entry of specific nutrients. They are then translocated through the outer membrane and transit through the periplasm by either the Tol or the TonB system. The components of each system are known, and their implication in the functioning of the system is described. Colicins then reach their lethal target and act either by forming a voltage-dependent channel into the inner membrane or by using their endonuclease activity on DNA, rRNA, or tRNA. The mechanisms of inhibition by specific and cognate immunity proteins are presented. Finally, the use of colicins as laboratory or biotechnological tools and their mode of evolution are discussed.

Indexed as

Amino Acid SequenceColicinsEscherichia coliEscherichia coli ProteinsModels, BiologicalMolecular Sequence DataProtein BindingProtein ConformationProtein TransportSequence Homology, Amino AcidColicinsEscherichia coli Proteins

Identifiers

PMID17347522
PMCPMC1847374
OpenAlexW4210359611

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.