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Results: 1-6 |
Results: 6

Authors: Waters, PJ Scriver, CR Parniak, MA
Citation: Pj. Waters et al., Homomeric and heteromeric interactions between wild-type and mutant phenylalanine hydroxylase subunits: Evaluation of two-hybrid approaches for functional analysis of mutations causing hyperphenylalaninemia, MOL GEN MET, 73(3), 2001, pp. 230-238

Authors: Waters, PJ Parniak, MA Akerman, BR Scriver, CR
Citation: Pj. Waters et al., Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype, (vol 69, pg 101, 2000), MOL GEN MET, 72(1), 2001, pp. 89-89

Authors: Waters, PJ Parniak, MA Akerman, BR Scriver, CR
Citation: Pj. Waters et al., Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype, MOL GEN MET, 69(2), 2000, pp. 101-110

Authors: Scriver, CR Waters, PJ Sarkissian, C Ryan, S Prevost, L Cote, D Novak, J Teebi, S Nowacki, PM
Citation: Cr. Scriver et al., PAHdb: A locus-specific knowledgebase, HUM MUTAT, 15(1), 2000, pp. 99-104

Authors: Scriver, CR Waters, PJ
Citation: Cr. Scriver et Pj. Waters, Monogenic traits are not simple - lessons from phenylketonuria, TRENDS GEN, 15(7), 1999, pp. 267-272

Authors: Waters, PJ Parniak, MA Akerman, BR Jones, AO Scriver, CR
Citation: Pj. Waters et al., Missense mutations in the phenylalanine hydroxylase gene (PAH) can cause accelerated proteolytic turnover of PAH enzyme: A mechanism underlying phenylketonuria, J INH MET D, 22(3), 1999, pp. 208-212
Risultati: 1-6 |