Recent Research Publications

For additional information, review the following recent research publications:

Lieberman R. L., B. A. Wustman, P. Huertas, A. C. Powe, Jr., C. W. Pine, R. Khanna, M. G. Schlossmacher, D. Ringe and G. A. Petsko. 2007. Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease.  Nature Chem. Biol. 3(2): 101-107.

Steet R, Chung S, Lee W, Pine C, Do H, Kornfeld S. Selective action of the iminosugar isofagomine, a pharmacological chaperone for mutant forms of acid-b-glucosidase. Biochem Pharmacol (2007), doi:10.1016/j.bcp.2006.12.015.

Parenti G, Zuppaldi A, Pittis MG, Tuzzi1 MR. Pharmacological Enhancement of Mutated a-Glucosidase Activity in Fibroblasts from Patients with Pompe Disease. Molecular Therapy. 2007 March: vol. 15 no. 3: 508-514.

Steet RA, Chung S, Wustman B, Powe A, Do H, Kornfeld SA The iminosugar isofagomine increases the activity of N370S mutant acid b-glucosidase in Gaucher fibroblasts by several mechanisms. Proc Natl Acad Sci (USA), 2006; 37: 13813-13818.

Yam GH, Bosshard N, Zuber C, Steinmann B, Roth J. Pharmacological chaperone corrects lysosomal storage in Fabry disease caused by trafficking-incompetent variants. Am J Physiol Cell Physiol 290:C1076-C1082, 2006.

Spada M, Pagliardini S, Yasuda M, Tukel T, Thiagarajan G, Sakuraba H, Ponzone A, Desnick RJ. High incidence of later-onset fabry disease revealed by newborn screening. Am J Hum Genet. 2006 Jul; 79(1):31-40. Epub 2006 Apr 28.

Ishii S, Yoshioka H, Mannen K, Kulkarni AB, Fan JQ. Transgenic mouse expressing human mutant α-galactosidase A in an endogenous enzyme deficient background: a biochemical animal model for studying active-site specific chaperone therapy for Fabry disease. Biochim Biophys Acta. 2004 Nov 5; 1690(3):250-7.

Yasuda K, Chang HH, Wu HL, Ishii S, Fan JQ. Efficient and rapid purification of recombinant human α-galactosidase A by affinity column chromatography. Protein Expr Purif. 2004 Oct; 37(2):499-506.

Romisch K. A cure for traffic jams: Small molecule chaperones in the endoplasmic reticulum. Traffic 2004; 5:815-820.

Fan JQ, Ishii S. Cell-based screening of active-site specific chaperone for the treatment of Fabry disease. Methods Enzymol. 2003; 363:412-20.

Fan JQ. A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity. Trends Pharmacol Sci. 2003 Jul; 24(7):355-60.

Ishii S, Nakao S, Minamikawa-Tachino R, Desnick RJ, Fan JQ. Alternative splicing in the α-galactosidase A gene: increased exon inclusion results in the Fabry cardiac phenotype. Am J Hum Genet. 2002 Apr; 70(4):994-1002. Epub 2002 Feb 4.

Sawkar AR, Cheng WC, Beutler E, Wong CH, Balch WE, Kelly J.  Chemical chaperones increase the cellular activity of N370S beta - glucosidase: A therapeutic strategy for Gaucher disease. Proc Natl Acad Sci.  2002 Nov; 99(24): 15428-15433.

Frustaci A, Chimenti C, Ricci R, Natale L, Russo MA, Pieroni M, Eng CM, Desnick RJ. Improvement in cardiac function in the cardiac variant of Fabry’s disease with galactose-infusion therapy. N Engl J Med, Vol. 345, No. 1. July 5, 2001.

Asano N, Ishii S, Kizu H, Ikeda K, Yasuda K, Kato A, Martin OR, Fan JQ. In vitro inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1-deoxygalactonojirimycin and its derivatives. Eur J Biochem. 2000 Jul; 267(13):4179-86.

Ishii S, Suzuki Y, Fan JQ. Role of Ser-65 in the activity of α-galactosidase A: characterization of a point mutation (S65T) detected in a patient with Fabry disease. Arch Biochem Biophys. 2000 May 15; 377(2):228-33.

Fan JQ, Ishii S, Asano N, Suzuki Y. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat Med. 1999 Jan; 5(1):112-5.