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Year | Number of Results |
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1998 | 1 |
2001 | 1 |
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Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level.
Extremophiles. 2001 Apr;5(2):101-9. doi: 10.1007/s007920100181.
Extremophiles. 2001.
PMID: 11354453
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
Pohl E, Brunner N, Wilmanns M, Hensel R.
Pohl E, et al.
J Biol Chem. 2002 May 31;277(22):19938-45. doi: 10.1074/jbc.M112244200. Epub 2002 Feb 12.
J Biol Chem. 2002.
PMID: 11842090
Free article.
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Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax.
Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E.
Lorentzen E, et al.
J Mol Biol. 2004 Aug 13;341(3):815-28. doi: 10.1016/j.jmb.2004.05.032.
J Mol Biol. 2004.
PMID: 15288789
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NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.
Brunner NA, Brinkmann H, Siebers B, Hensel R.
Brunner NA, et al.
J Biol Chem. 1998 Mar 13;273(11):6149-56. doi: 10.1074/jbc.273.11.6149.
J Biol Chem. 1998.
PMID: 9497334
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