Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease.

[1]  S. Chung,et al.  The iminosugar isofagomine increases the activity of N370S mutant acid β-glucosidase in Gaucher fibroblasts by several mechanisms , 2006, Proceedings of the National Academy of Sciences.

[2]  J. Trojanowski,et al.  Glucocerebrosidase mutations are an important risk factor for Lewy body disorders , 2006, Neurology.

[3]  Min Zhang,et al.  Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations. , 2006, The Journal of biological chemistry.

[4]  J. Kelly,et al.  Therapeutic strategies to ameliorate lysosomal storage disorders – a focus on Gaucher disease , 2006, Cellular and Molecular Life Sciences CMLS.

[5]  J. Sancho,et al.  Miglustat (NB-DNJ) works as a chaperone for mutated acid beta-glucosidase in cells transfected with several Gaucher disease mutations. , 2005, Blood cells, molecules & diseases.

[6]  R. Dwek,et al.  Imino sugar inhibitors for treating the lysosomal glycosphingolipidoses. , 2005, Glycobiology.

[7]  F. Felicetti,et al.  The N370S (Asn370-->Ser) mutation affects the capacity of glucosylceramidase to interact with anionic phospholipid-containing membranes and saposin C. , 2005, The Biochemical journal.

[8]  G. Pastores,et al.  An open-label, noncomparative study of miglustat in type I Gaucher disease: efficacy and tolerability over 24 months of treatment. , 2005, Clinical therapeutics.

[9]  J. Sussman,et al.  X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide. Implications for Gaucher disease. , 2005, The Journal of biological chemistry.

[10]  J. Sussman,et al.  X-ray structure of human acid-beta-glucosidase covalently bound to conduritol B epoxide , 2005 .

[11]  V S Lamzin,et al.  Modelling bound ligands in protein crystal structures. , 2004, Acta crystallographica. Section D, Biological crystallography.

[12]  K Henrick,et al.  Electronic Reprint Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions Biological Crystallography Secondary-structure Matching (ssm), a New Tool for Fast Protein Structure Alignment in Three Dimensions , 2022 .

[13]  Kevin Cowtan,et al.  research papers Acta Crystallographica Section D Biological , 2005 .

[14]  R. Dwek,et al.  Sustained therapeutic effects of oral miglustat (Zavesca, N-butyldeoxynojirimycin, OGT 918) in type I Gaucher disease , 2004, Journal of Inherited Metabolic Disease.

[15]  S. Brothers,et al.  Pharmacologic Rescue of Conformationally‐Defective Proteins: Implications for the Treatment of Human Disease , 2004, Traffic.

[16]  Seiichiro Ogawa,et al.  N-Octyl-β-valienamine up-regulates activity of F213I mutant β-glucosidase in cultured cells: a potential chemical chaperone therapy for Gaucher disease , 2004 .

[17]  A. W. Schüttelkopf,et al.  PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. , 2004, Acta crystallographica. Section D, Biological crystallography.

[18]  J. Allman,et al.  Neuropathology provides clues to the pathophysiology of Gaucher disease. , 2004, Molecular genetics and metabolism.

[19]  R. Dwek,et al.  Membrane disruption and cytotoxicity of hydrophobic N-alkylated imino sugars is independent of the inhibition of protein and lipid glycosylation. , 2003, The Biochemical journal.

[20]  Jian‐Qiang Fan.  A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity. , 2003, Trends in pharmacological sciences.

[21]  J. Sussman,et al.  X‐ray structure of human acid‐β‐glucosidase, the defective enzyme in Gaucher disease , 2003, EMBO reports.

[22]  M. Wendeler,et al.  Chemical Chaperones—A New Concept in Drug Research , 2003, Chembiochem : a European journal of chemical biology.

[23]  H. Naim,et al.  Intracellular transport of acid β‐glucosidase and lysosome‐associated membrane proteins is affected in Gaucher's disease (G202R mutation) , 1999, The Journal of pathology.

[24]  X. Qi,et al.  Acid β-Glucosidase: Intrinsic Fluorescence and Conformational Changes Induced by Phospholipids and Saposin C† , 1998 .

[25]  Z. Otwinowski,et al.  [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.

[26]  E. Beutler,et al.  Glucocerebrosidase (Gaucher disease) , 1996, Human mutation.

[27]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[28]  S. Withers,et al.  Identification of Glu340 as the active-site nucleophile in human glucocerebrosidase by use of electrospray tandem mass spectrometry. , 1994, The Journal of biological chemistry.

[29]  V. Scheinker,et al.  Analysis of human acid beta-glucosidase by site-directed mutagenesis and heterologous expression. , 1994, The Journal of biological chemistry.

[30]  R. Desnick,et al.  Human acid beta-glucosidase: use of inhibitors, alternative substrates and amphiphiles to investigate the properties of the normal and Gaucher disease active sites. , 1987, Biochimica et biophysica acta.

[31]  N. Radin,et al.  Mechanism of activation of glucocerebrosidase by co-beta-glucosidase (glucosidase activator protein). , 1981, Biochimica et biophysica acta.