Evidence map›Paper›PMID 18535149›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2008

Structure, function, and evolution of bacterial ATP-binding cassette systems.

Amy L Davidson, Elie Dassa, Cedric Orelle, Jue Chen

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 660 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
660citing papers in PubMed, 1 pooled it
32.6field-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

660 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,417 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. A copper uptake ABC transport system is essential forEmerging microbes & infections · 2026
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600 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

4 authors at 2 institutions in 2 countries.

Amy L DavidsonDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA. adavidso@purdue.edu
Elie Dassa
Cedric Orelle
Jue Chen
Purdue University West Lafayette · USCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

summaryATP-binding cassette (ABC) systems are universally distributed among living organisms and function in many different aspects of bacterial physiology. ABC transporters are best known for their role in the import of essential nutrients and the export of toxic molecules, but they can also mediate the transport of many other physiological substrates. In a classical transport reaction, two highly conserved ATP-binding domains or subunits couple the binding/hydrolysis of ATP to the translocation of particular substrates across the membrane, through interactions with membrane-spanning domains of the transporter. Variations on this basic theme involve soluble ABC ATP-binding proteins that couple ATP hydrolysis to nontransport processes, such as DNA repair and gene expression regulation. Insights into the structure, function, and mechanism of action of bacterial ABC proteins are reported, based on phylogenetic comparisons as well as classic biochemical and genetic approaches. The availability of an increasing number of high-resolution structures has provided a valuable framework for interpretation of recent studies, and realistic models have been proposed to explain how these fascinating molecular machines use complex dynamic processes to fulfill their numerous biological functions. These advances are also important for elucidating the mechanism of action of eukaryotic ABC proteins, because functional defects in many of them are responsible for severe human inherited diseases.

Indexed as

Adenosine TriphosphateAmino Acid MotifsAmino Acid SequenceATP-Binding Cassette TransportersBiological TransportEvolution, MolecularGram-Negative BacteriaModels, MolecularPhylogenyProtein Structure, SecondarySequence AlignmentAdenosine TriphosphateATP-Binding Cassette Transporters

Identifiers

PMID18535149
PMCPMC2415747
OpenAlexW2133691154

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.