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1
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M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations.
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J Mol Biol
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2010
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0.98
|
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2
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Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanK.
|
Acta Crystallogr D Biol Crystallogr
|
2006
|
0.96
|
|
3
|
Calcium/calmodulin dependent protein kinase II bound to NMDA receptor 2B subunit exhibits increased ATP affinity and attenuated dephosphorylation.
|
PLoS One
|
2011
|
0.89
|
|
4
|
Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action.
|
Acta Crystallogr D Biol Crystallogr
|
2009
|
0.83
|
|
5
|
Location and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme action.
|
Acta Crystallogr D Biol Crystallogr
|
2011
|
0.81
|
|
6
|
The role of UPF0157 in the folding of M. tuberculosis dephosphocoenzyme A kinase and the regulation of the latter by CTP.
|
PLoS One
|
2009
|
0.79
|
|
7
|
Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies.
|
J Biol Chem
|
2006
|
0.79
|
|
8
|
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis.
|
Acta Crystallogr Sect F Struct Biol Cryst Commun
|
2004
|
0.76
|
|
9
|
A double helix is the repeating unit in a luminescent calcium 5-aminoisophthalate supramolecular edifice with water-filled hexagonal channels.
|
Inorg Chem
|
2007
|
0.75
|