Annereau, Jean Philippe; Ko, Young Hee; Pedersen, Peter L (2003) Cystic fibrosis transmembrane conductance regulator: the NBF1+R (nucleotide-binding fold 1 and regulatory domain) segment acting alone catalyses a Co2+/Mn2+/Mg2+-ATPase activity markedly inhibited by both Cd2+ and the transition-state analogue orthovanada Biochem J 371:451-62
|
Pedersen, Peter L (2002) Transport ATPases in biological systems and relationship to human disease: a brief overview. J Bioenerg Biomembr 34:327-32
|
Ko, Y H; Pedersen, P L (2001) Cystic fibrosis: a brief look at some highlights of a decade of research focused on elucidating and correcting the molecular basis of the disease. J Bioenerg Biomembr 33:513-21
|
Massiah, M A; Ko, Y H; Pedersen, P L et al. (1999) Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation. Biochemistry 38:7453-61
|
Thomas, P J; Ko, Y H; Shenbagamurthi, P et al. (1995) Nucleotide domains in transport ATPases: structure-function and relationship to disease. Soc Gen Physiol Ser 50:17-28
|
Ko, Y H; Thomas, P J; Pedersen, P L (1994) The cystic fibrosis transmembrane conductance regulator. Nucleotide binding to a synthetic peptide segment from the second predicted nucleotide binding fold. J Biol Chem 269:14584-8
|
Thomas, P J; Pedersen, P L (1993) Effects of the delta F508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR. J Bioenerg Biomembr 25:11-9
|
Ko, Y H; Thomas, P J; Delannoy, M R et al. (1993) The cystic fibrosis transmembrane conductance regulator. Overexpression, purification, and characterization of wild type and delta F508 mutant forms of the first nucleotide binding fold in fusion with the maltose-binding protein. J Biol Chem 268:24330-8
|
Thomas, P J; Ko, Y H; Pedersen, P L (1992) Altered protein folding may be the molecular basis of most cases of cystic fibrosis. FEBS Lett 312:7-9
|
Thomas, P J; Shenbagamurthi, P; Sondek, J et al. (1992) The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide. J Biol Chem 267:5727-30
|