@Article{Guce20103625,
  author                  = {Guce, A.I. and Clark, N.E. and Salgado, E.N. and Ivanen, D.R. and Kulminskaya, A.A. and Brumer III, H. and Garman, S.C.},
  journal                 = {Journal of Biological Chemistry},
  title                   = {Catalytic mechanism of human α-galactosidase},
  year                    = {2010},
  issn                    = {00219258},
  month                   = feb,
  note                    = {cited By 82},
  number                  = {6},
  pages                   = {3625-3632},
  volume                  = {285},
  abbrev_source_title     = {J. Biol. Chem.},
  affiliation             = {Dept. of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant St., Amherst, MA, United States; Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States; Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Leningrad District, Orlova Roscha, Gatchina 188300, Russian Federation; Department of Biotechnology, Royal Insitute of Technology (KTH), 10691 Stockholm, Sweden},
  chemicals_cas           = {alpha galactosidase, 9025-35-8; glycosidase, 9032-92-2; Ligands; alpha-Galactosidase, 3.2.1.22},
  coden                   = {JBCHA},
  correspondence_address1 = {Garman, S. C.; Dept. of Biochemistry and Molecular Biology, 710 North Pleasant St., Amherst, MA, United States; email: garman@biochem.umass.edu},
  document_type           = {Article},
  doi                     = {10.1074/jbc.M109.060145},
  funding_details         = {National Institute of Diabetes and Digestive and Kidney DiseasesNational Institute of Diabetes and Digestive and Kidney Diseases, NIDDK, R01DK076877},
  keywords                = {Boat conformations; Catalytic cycles; Catalytic mechanisms; Clinical research; Clinical trial; Displacement reactions; Drug Design; Fabry disease; Galactopyranoside; Galactosidases; Glycoside hydrolases; High-resolution structures; Lysosomal storage disorder; Reaction cycles; Recombinant enzymes; Second ligand; X ray crystal structures, Binding energy; Conformations; Ligands; Substitution reactions; Sugars, Enzymes, alpha galactosidase; glycosidase; ligand, animal cell; article; catalysis; conformational transition; controlled study; enzyme active site; enzyme kinetics; enzyme structure; Fabry disease; human; ligand binding; nonhuman; priority journal; animal; binding site; catalysis; cell line; chemical structure; chemistry; enzyme specificity; enzymology; genetics; metabolism; mutation; pathology; protein binding; protein conformation; protein tertiary structure; X ray crystallography, alpha-Galactosidase; Animals; Binding Sites; Catalysis; Catalytic Domain; Cell Line; Crystallography, X-Ray; Fabry Disease; Humans; Ligands; Models, Molecular; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Substrate Specificity},
  language                = {English},
  publisher               = {Elsevier BV},
  pubmed_id               = {19940122},
  source                  = {Scopus},
  url                     = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-77950511400&doi=10.1074%2fjbc.M109.060145&partnerID=40&md5=d7be48e5b0e0006198e363b1127b3879},
}

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Biol. Chem.","affiliation":"Dept. of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant St., Amherst, MA, United States; Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States; Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Leningrad District, Orlova Roscha, Gatchina 188300, Russian Federation; Department of Biotechnology, Royal Insitute of Technology (KTH), 10691 Stockholm, Sweden","chemicals_cas":"alpha galactosidase, 9025-35-8; glycosidase, 9032-92-2; Ligands; alpha-Galactosidase, 3.2.1.22","coden":"JBCHA","correspondence_address1":"Garman, S. 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Biol. Chem.},\n affiliation = {Dept. of Biochemistry and Molecular Biology, University of Massachusetts, 710 North Pleasant St., Amherst, MA, United States; Department of Chemistry, University of Massachusetts, Amherst, MA 01003, United States; Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, Leningrad District, Orlova Roscha, Gatchina 188300, Russian Federation; Department of Biotechnology, Royal Insitute of Technology (KTH), 10691 Stockholm, Sweden},\n chemicals_cas = {alpha galactosidase, 9025-35-8; glycosidase, 9032-92-2; Ligands; alpha-Galactosidase, 3.2.1.22},\n coden = {JBCHA},\n correspondence_address1 = {Garman, S. 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