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Year | Number of Results |
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1993 | 1 |
1995 | 2 |
2000 | 2 |
2003 | 1 |
2024 | 0 |
PubMed for id: 79047
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Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium.
Science. 1995 Mar 3;267(5202):1344-6. doi: 10.1126/science.267.5202.1344.
Science. 1995.
PMID: 17812611
The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies.
Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccaï G, Vellieux FM.
Irimia A, et al.
J Mol Biol. 2003 Feb 21;326(3):859-73. doi: 10.1016/s0022-2836(02)01450-x.
J Mol Biol. 2003.
PMID: 12581646
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Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui.
Madern D, Ebel C, Mevarech M, Richard SB, Pfister C, Zaccai G.
Madern D, et al.
Biochemistry. 2000 Feb 8;39(5):1001-10. doi: 10.1021/bi9910023.
Biochemistry. 2000.
PMID: 10653644
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Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui.
Richard SB, Madern D, Garcin E, Zaccai G.
Richard SB, et al.
Biochemistry. 2000 Feb 8;39(5):992-1000. doi: 10.1021/bi991001a.
Biochemistry. 2000.
PMID: 10653643
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Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui.
Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M.
Cendrin F, et al.
Biochemistry. 1993 Apr 27;32(16):4308-13. doi: 10.1021/bi00067a020.
Biochemistry. 1993.
PMID: 8476859
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Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts.
Madern D, Pfister C, Zaccai G.
Madern D, et al.
Eur J Biochem. 1995 Jun 15;230(3):1088-95. doi: 10.1111/j.1432-1033.1995.tb20659.x.
Eur J Biochem. 1995.
PMID: 7601139
Free article.
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