Reference for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions

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[http://www.biochemj.org/bj/339/0223/bj3390223.htm /RIDDER, I.S., DIJKSTRA., B.W. (1999). Identification of the Mg2-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY. Biochem. J., 339, 223–226.]
[http://www.biochemj.org/bj/339/0223/bj3390223.htm /RIDDER, I.S., DIJKSTRA., B.W. (1999). Identification of the Mg2-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY. Biochem. J., 339, 223–226.]
[[Crystal_structure_of_phosphoserine_phosphatase_from_Methanococcus_jannaschii,_a_hyperthermophile,_at_1.8_A_resolution.pdf | WANG, W., KIM, R., JANCARIK, J., YOKOTA, H., KIM, A. (2001). Crystal structure of the Phosphoserine Phosphatase from ''Methanococcus jannaschii'', a hyperthermophile, at 1.8 A resolution]]

Revision as of 04:40, 11 June 2007

KLESHCHINOV, V. N. (1979). Increased ATP-hydrolase activity of brain mitochondria induced by chlorpromazine (electron-cytochemical study). Morphology and Pathomorphology., 88(3), 1084-1086.

/RANGARAJAN, E.S., PROTEAU, A., WAGNER, J., HUNG, M.N., MATTE, A., CYGLER, M. (2006). Structural Snapshots of Escherichia coli Histidinol Phosphate Phosphatase along the Reaction Pathway. J. Biol. Chem., 281(49), 37930-37941.

/RIDDER, I.S., DIJKSTRA., B.W. (1999). Identification of the Mg2-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY. Biochem. J., 339, 223–226.

WANG, W., KIM, R., JANCARIK, J., YOKOTA, H., KIM, A. (2001). Crystal structure of the Phosphoserine Phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution

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