ArticleCommunicative & integrative biology2009
The NBDs that wouldn't die: A cautionary tale of the use of isolated nucleotide binding domains of ABC transporters.
Article in Communicative & integrative biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
The trial behind it
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- How to move an amphipathic molecule across a lipid bilayer: different mechanisms for different ABC transporters?Biochemical Society transactions · 2016Review
- Barley has two peroxisomal ABC transporters with multiple functions in β-oxidation.Journal of experimental botany · 2014Article
- The α/β hydrolase CGI-58 and peroxisomal transport protein PXA1 coregulate lipid homeostasis and signaling in Arabidopsis.The Plant cell · 2013Article
- Identification of small-molecule inhibitors of Yersinia pestis Type III secretion system YscN ATPase.PloS one · 2011Article
- The Arabidopsis peroxisomal ABC transporter, comatose, complements the Saccharomyces cerevisiae pxa1 pxa2Delta mutant for metabolism of long-chain fatty acids and exhibits fatty acyl-CoA-stimulated ATPase activity.The Journal of biological chemistry · 2010Article
- The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids.The FEBS journal · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
COMATOSE (CTS), the plant homologue of Adrenoleukodystrophy protein, is a full length ABC transporter localized in peroxisomes. In a recent article, we reported that the two-nucleotide binding domains of CTS are not functionally equivalent in vivo. Mutations in conserved residues in the Walker A (K487A) and B (D606N) motifs of NBD1 resulted in a null phenotype, whereas identical mutations in the equivalent residues in NBD2 (K1136A and D1276N) had no detectable effect.1 In order to study the effect of these mutations on the ATPase activity of the nucleotide binding domains, we cloned and expressed the isolated NBDs as maltose binding protein (MBP) fusion proteins. We show that ATPase activity is associated with the isolated MBP-NBDs. However, mutations of amino acids located in conserved motifs did not result in striking reduction in activity despite well characterized roles in ATP binding and hydrolysis.2 We urge caution in the interpretation of results obtained from the study of isolated NBD fusions and their extrapolation to the mechanism of ATP hydrolysis in ABC transporter proteins.
Indexed as
Identifiers
19704900PMC2686355W1974735191What OpenQuestion holds
Registered trials
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.