Proline residues link the active site to transmembrane domain movements in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Cellular and Molecular Neuroscience,Molecular Biology
Link
http://link.springer.com/content/pdf/10.1007/s11302-010-9180-0.pdf
Reference45 articles.
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2. Ivanenkov VV, Meller J, Kirley TL (2005) Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling. Biochemistry 44:8998–9012
3. Murphy-Piedmonte DM, Crawford PA, Kirley TL (2005) Bacterial expression, folding, purification and characterization of soluble NTPDase5 (CD39L4) ecto-nucleotidase. Biochim Biophys Acta 1747:251–259
4. Ivanenkov VV, Murphy-Piedmonte DM, Kirley TL (2003) Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function. Biochemistry 42:11726–11735
5. Stout JG, Strobel RS, Kirley TL (1995) Identification and immunolocalization of ecto-ATPDase in chicken stomach. Biochem Mol Biol Int 36:529–535
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