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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Trends in Pharmacolo...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Trends in Pharmacological Sciences
Article . 2006 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations

Authors: Hiroshi, Omote; Miki, Hiasa; Takuya, Matsumoto; Masato, Otsuka; Yoshinori, Moriyama;

The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations

Abstract

Multidrug and toxic compound extrusion (MATE) proteins, comprising the most recently designated family of multidrug transporter proteins, are widely distributed in all kingdoms of living organisms, although their function is far from understood. The bacterial MATE-type transporters that have been characterized function as exporters of cationic drugs, such as norfloxacin and ethidium, through H(+) or Na(+) exchange. Plant MATE-type transporters are involved in the detoxification of secondary metabolites, including alkaloids. Mammalian MATE-type transporters are responsible for the final step in the excretion of metabolic waste and xenobiotic organic cations in the kidney and liver through electroneutral exchange of H(+). Thus, we propose that members of the MATE family are organic cation exporters that excrete metabolic or xenobiotic organic cations from the body.

Related Organizations
Keywords

ATP Binding Cassette Transporter, Subfamily B, Saccharomyces cerevisiae Proteins, Organic Cation Transport Proteins, Arabidopsis Proteins, Molecular Sequence Data, Antiporters, Protein Structure, Tertiary, Xenobiotics, Bacterial Proteins, Pharmaceutical Preparations, Animals, Humans, Steroids, Amino Acid Sequence, Carrier Proteins, Biotransformation, Phylogeny, Transcription Factors

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Powered by OpenAIRE graph
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
377
Top 1%
Top 1%
Top 1%
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