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Table representation of search results timeline featuring number of search results per year.
Year | Number of Results |
---|---|
2000 | 2 |
2008 | 1 |
2009 | 1 |
2010 | 1 |
2012 | 1 |
2013 | 1 |
2014 | 1 |
2024 | 0 |
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Page 1
Structure of isocitrate lyase, a persistence factor of Mycobacterium tuberculosis.
Nat Struct Biol. 2000 Aug;7(8):663-8. doi: 10.1038/77964.
Nat Struct Biol. 2000.
PMID: 10932251
Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase.
McKinney JD, Höner zu Bentrup K, Muñoz-Elías EJ, Miczak A, Chen B, Chan WT, Swenson D, Sacchettini JC, Jacobs WR Jr, Russell DG.
McKinney JD, et al.
Nature. 2000 Aug 17;406(6797):735-8. doi: 10.1038/35021074.
Nature. 2000.
PMID: 10963599
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Mycobacterium tuberculosis isocitrate lyase (MtbIcl): role of divalent cations in modulation of functional and structural properties.
Kumar R, Bhakuni V.
Kumar R, et al.
Proteins. 2008 Aug 15;72(3):892-900. doi: 10.1002/prot.21984.
Proteins. 2008.
PMID: 18275086
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Role of the transcriptional regulator RamB (Rv0465c) in the control of the glyoxylate cycle in Mycobacterium tuberculosis.
Micklinghoff JC, Breitinger KJ, Schmidt M, Geffers R, Eikmanns BJ, Bange FC.
Micklinghoff JC, et al.
J Bacteriol. 2009 Dec;191(23):7260-9. doi: 10.1128/JB.01009-09. Epub 2009 Sep 18.
J Bacteriol. 2009.
PMID: 19767422
Free PMC article.
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Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis [corrected].
Festa RA, McAllister F, Pearce MJ, Mintseris J, Burns KE, Gygi SP, Darwin KH.
Festa RA, et al.
PLoS One. 2010 Jan 6;5(1):e8589. doi: 10.1371/journal.pone.0008589.
PLoS One. 2010.
PMID: 20066036
Free PMC article.
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A novel role of the PrpR as a transcription factor involved in the regulation of methylcitrate pathway in Mycobacterium tuberculosis.
Masiewicz P, Brzostek A, Wolański M, Dziadek J, Zakrzewska-Czerwińska J.
Masiewicz P, et al.
PLoS One. 2012;7(8):e43651. doi: 10.1371/journal.pone.0043651. Epub 2012 Aug 16.
PLoS One. 2012.
PMID: 22916289
Free PMC article.
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Cysteine is the general base that serves in catalysis by isocitrate lyase and in mechanism-based inhibition by 3-nitropropionate.
Moynihan MM, Murkin AS.
Moynihan MM, et al.
Biochemistry. 2014 Jan 14;53(1):178-87. doi: 10.1021/bi401432t. Epub 2013 Dec 24.
Biochemistry. 2014.
PMID: 24354272
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