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Archives of Biochemistry and Biophysics

Volumn 530, Issue 2, 2013, Pages 73-82

A new model for allosteric regulation of phenylalanine hydroxylase: Implications for disease and therapeutics

(5) Jaffe, Eileen K a Stith, Linda a Lawrence, Sarah H a Andrake, Mark a Dunbrack Jr , Roland L a

a FOX CHASE CANCER CENTER (United States)

Author keywords

ACT domain dimerization; Morpheein; Pharmacological chaperone; Protein homology modeling; Protein multimerization

Indexed keywords

PHENYLALANINE 4 MONOOXYGENASE; TETRAMER;

ALLOSTERISM; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; IN VITRO STUDY; MUTATION; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

ALLOSTERIC REGULATION; ANIMALS; HUMANS; MODELS, CHEMICAL; MOLECULAR CHAPERONES; PHENYLALANINE HYDROXYLASE; PHENYLKETONURIAS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RATS;

RATTUS;

EID: 84873052980 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2012.12.017 Document Type: Article

Times cited : (49)

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