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Defective protein folding as a basis of human disease.
Thomas PJ, Qu BH, Pedersen PL. Thomas PJ, et al. Among authors: pedersen pl. Trends Biochem Sci. 1995 Nov;20(11):456-9. doi: 10.1016/s0968-0004(00)89100-8. Trends Biochem Sci. 1995. PMID: 8578588 Review.
Cystic fibrosis: a brief look at some highlights of a decade of research focused on elucidating and correcting the molecular basis of the disease.
Ko YH, Pedersen PL. Ko YH, et al. Among authors: pedersen pl. J Bioenerg Biomembr. 2001 Dec;33(6):513-21. doi: 10.1023/a:1012831322753. J Bioenerg Biomembr. 2001. PMID: 11804193 Review.
Frontiers in research on cystic fibrosis: understanding its molecular and chemical basis and relationship to the pathogenesis of the disease.
Ko YH, Pedersen PL. Ko YH, et al. Among authors: pedersen pl. J Bioenerg Biomembr. 1997 Oct;29(5):417-27. doi: 10.1023/a:1022402105375. J Bioenerg Biomembr. 1997. PMID: 9511927 Review.
Altered protein folding may be the molecular basis of most cases of cystic fibrosis.
Thomas PJ, Ko YH, Pedersen PL. Thomas PJ, et al. Among authors: pedersen pl. FEBS Lett. 1992 Nov 2;312(1):7-9. doi: 10.1016/0014-5793(92)81399-7. FEBS Lett. 1992. PMID: 1385213 Review.
Effects of the delta F508 mutation on the structure, function, and folding of the first nucleotide-binding domain of CFTR.
Thomas PJ, Pedersen PL. Thomas PJ, et al. Among authors: pedersen pl. J Bioenerg Biomembr. 1993 Feb;25(1):11-9. doi: 10.1007/BF00768063. J Bioenerg Biomembr. 1993. PMID: 7680027
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 orthovanadate.
Annereau JP, Ko YH, Pedersen PL. Annereau JP, et al. Among authors: pedersen pl. Biochem J. 2003 Apr 15;371(Pt 2):451-62. doi: 10.1042/BJ20021318. Biochem J. 2003. PMID: 12523935 Free PMC article.
Cystic fibrosis transmembrane conductance regulator: the first nucleotide binding fold targets the membrane with retention of its ATP binding function.
Ko YH, Delannoy M, Pedersen PL. Ko YH, et al. Among authors: pedersen pl. Biochemistry. 1997 Apr 22;36(16):5053-64. doi: 10.1021/bi9630265. Biochemistry. 1997. PMID: 9125527
Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR).
Bianchet MA, Ko YH, Amzel LM, Pedersen PL. Bianchet MA, et al. Among authors: pedersen pl. J Bioenerg Biomembr. 1997 Oct;29(5):503-24. doi: 10.1023/a:1022443209010. J Bioenerg Biomembr. 1997. PMID: 9511935
., and Pedersen, P.L. (1995) J. Biol. Chem. 268, 24330-24338], providing support for the model. In contrast, the second nucleotide binding fold is predicted at best to be a weak ATPase as the glutamic acid residue is replaced with a glutamine. ...
., and Pedersen, P.L. (1995) J. Biol. Chem. 268, 24330-24338], providing support for the model. In contrast, the second nucleotide bi …
The first nucleotide binding fold of the cystic fibrosis transmembrane conductance regulator can function as an active ATPase.
Ko YH, Pedersen PL. Ko YH, et al. Among authors: pedersen pl. J Biol Chem. 1995 Sep 22;270(38):22093-6. doi: 10.1074/jbc.270.38.22093. J Biol Chem. 1995. PMID: 7545672
The cystic fibrosis transmembrane conductance regulator. Nucleotide binding to a synthetic peptide segment from the second predicted nucleotide binding fold.
Ko YH, Thomas PJ, Pedersen PL. Ko YH, et al. Among authors: pedersen pl. J Biol Chem. 1994 May 20;269(20):14584-8. J Biol Chem. 1994. PMID: 7514174
., and Pedersen, P.L. (1991) Science 251, 555-557). Although mutational analysis within the predicted second nucleotide binding fold indicates that this domain may be functionally important also, direct evidence for nucleotide binding is lacking. ...
., and Pedersen, P.L. (1991) Science 251, 555-557). Although mutational analysis within the predicted second nucleotide binding fold …
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