Structural basis of pharmacological chaperoning for human β-galactosidase

Journal of Biological Chemistry

Volumn 289, Issue 21, 2014, Pages 14560-14568

  Suzuki, Hironori ^a   Ohto, Umeharu ^a   Higaki, Katsumi ^b   Mena Barragán, Teresa ^c   Aguilar Moncayo, Matilde ^c   Ortiz Mellet, Carmen ^c   Nanba, Eiji ^b   Fernandez, Jose M Garcia ^d   Suzuki, Yoshiyuki ^e,g   Shimizu, Toshiyuki ^a,f  

^a UNIVERSITY OF TOKYO   (Japan)

^b TOTTORI UNIVERSITY   (Japan)

^c UNIVERSITY OF SEVILLE   (Spain)

^d CSIC   (Spain)

^e INTERNATIONAL UNIVERSITY OF HEALTH AND WELFARE   (Japan)

^f JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^g TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CELL MEMBRANES; HYDROGEN BONDS;

ACTIVE SITE RESIDUES; BICYCLIC STRUCTURE; BINDING AFFINITIES; GALACTOSIDASES; MECHANISM OF ACTION; RECOGNITION MECHANISM; SMALL MOLECULES; STRUCTURAL BASIS;

ENZYMES;

BETA GALACTOSIDASE;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME BINDING; ENZYME PURIFICATION; ENZYME STABILITY; FIBROBLAST; GENE MUTATION; GM1 GANGLIOSIDOSIS; HUMAN; HUMAN CELL; HYDROGEN BOND; ISOTHERMAL TITRATION CALORIMETRY; JAPANESE (PEOPLE); MOLECULAR CLONING; MUTANT; PHARMACOLOGICAL CHAPERONING; PHARMACOLOGICAL PROCEDURES; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; WILD TYPE;

CRYSTAL STRUCTURE; GALACTOSE; GLYCOSIDASES; LYSOSOMAL STORAGE DISEASE; X-RAY CRYSTALLOGRAPHY;

1-DEOXYNOJIRIMYCIN; BETA-GALACTOSIDASE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYCLOHEXENES; ENZYME INHIBITORS; ENZYME STABILITY; GANGLIOSIDOSIS, GM1; HEXOSAMINES; HUMANS; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; IMINO SUGARS; INOSITOL; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUCOPOLYSACCHARIDOSIS IV; MUTATION; PROTEIN STRUCTURE, TERTIARY; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84900815378     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.529529     Document Type: Article

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