The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli

scientific article published on 15 January 2014

The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2014PLoSO...985529W
P356DOI10.1371/JOURNAL.PONE.0085529
P932PMC publication ID3893208
P698PubMed publication ID24454883
P5875ResearchGate publication ID259879534

P50authorJack GreenblattQ6112804
Andrew EmiliQ64126987
P2093author name stringWalid A Houry
Mohan Babu
Chris Graham
Keith S Wong
Jamie D Snider
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P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue1
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)e85529
P577publication date2014-01-15
P1433published inPLOS OneQ564954
P1476titleThe MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coli
P478volume9

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cites work (P2860)
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Q93013129Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex
Q27321084Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA
Q38761978The 'liaisons dangereuses' between iron and antibiotics.
Q42357638Transcriptomes of the Extremely Thermoacidophilic Archaeon Metallosphaera sedula Exposed to Metal "Shock" Reveal Generic and Specific Metal Responses
Q50082699Use of genetic and chemical synthetic lethality as probes of complexity in bacterial cell systems

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