메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Identification of Small Molecule Compounds for Pharmacological Chaperone Therapy of Aspartylglucosaminuria

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; MUTANT PROTEIN; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE;

EID: 84996548960     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep37583     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 84891768251 scopus 로고    scopus 로고
    • Aspartylglucosaminuria: Unusual neonatal presentation in Qatari twins with a novel aspartylglucosaminidase gene mutation and 3 new cases in a Turkish family
    • Opladen, T. et al. Aspartylglucosaminuria: unusual neonatal presentation in Qatari twins with a novel aspartylglucosaminidase gene mutation and 3 new cases in a Turkish family. J Child Neurol 29, 36-42 (2014).
    • (2014) J Child Neurol , vol.29 , pp. 36-42
    • Opladen, T.1
  • 2
    • 0035871210 scopus 로고    scopus 로고
    • Molecular pathogenesis of a disease: Structural consequences of aspartylglucosaminuria mutations
    • Saarela, J. et al. Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations. Hum Mol Genet 10, 983-995 (2001).
    • (2001) Hum Mol Genet , vol.10 , pp. 983-995
    • Saarela, J.1
  • 3
    • 0026327411 scopus 로고
    • Spectrum of mutations in aspartylglucosaminuria
    • Ikonen, E. et al. Spectrum of mutations in aspartylglucosaminuria. Proc Natl Acad Sci USA 88, 11222-11226 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11222-11226
    • Ikonen, E.1
  • 4
    • 0028964044 scopus 로고
    • Intracellular sorting of aspartylglucosaminidase: The role of N-linked oligosaccharides and evidence of Man-6-P-independent lysosomal targeting
    • Tikkanen, R., Enomaa, N., Riikonen, A., Ikonen, E. & Peltonen, L. Intracellular sorting of aspartylglucosaminidase: the role of N-linked oligosaccharides and evidence of Man-6-P-independent lysosomal targeting. DNA Cell Biol 14, 305-312 (1995).
    • (1995) DNA Cell Biol , vol.14 , pp. 305-312
    • Tikkanen, R.1    Enomaa, N.2    Riikonen, A.3    Ikonen, E.4    Peltonen, L.5
  • 5
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen, C., Tikkanen, R., Rouvinen, J. & Peltonen, L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol 2, 1102-1108 (1995).
    • (1995) Nat Struct Biol , vol.2 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 6
    • 0029936212 scopus 로고    scopus 로고
    • Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation
    • Tikkanen, R., Riikonen, A., Oinonen, C., Rouvinen, R. & Peltonen, L. Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation. EMBO J 15, 2954-2960 (1996).
    • (1996) EMBO J , vol.15 , pp. 2954-2960
    • Tikkanen, R.1    Riikonen, A.2    Oinonen, C.3    Rouvinen, R.4    Peltonen, L.5
  • 7
    • 0032566667 scopus 로고    scopus 로고
    • Activation and oligomerization of aspartylglucosaminidase
    • Saarela, J. et al. Activation and oligomerization of aspartylglucosaminidase. J Biol Chem 273, 25320-25328 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 25320-25328
    • Saarela, J.1
  • 8
    • 0026089364 scopus 로고
    • Aspartylglucosaminuria: CDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
    • Ikonen, E. et al. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J 10, 51-58 (1991).
    • (1991) EMBO J , vol.10 , pp. 51-58
    • Ikonen, E.1
  • 9
    • 0025790959 scopus 로고
    • Aspartylglycosaminuria in the Finnish population: Identification of two point mutations in the heavy chain of glycoasparaginase
    • Mononen, I. et al. Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase. Proc Natl Acad Sci USA 88, 2941-2945 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2941-2945
    • Mononen, I.1
  • 10
    • 77957586806 scopus 로고    scopus 로고
    • Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice
    • Dunder, U., Valtonen, P., Kelo, E. & Mononen, I. Early initiation of enzyme replacement therapy improves metabolic correction in the brain tissue of aspartylglycosaminuria mice. J Inherit Metab Dis 33, 611-617 (2010).
    • (2010) J Inherit Metab Dis , vol.33 , pp. 611-617
    • Dunder, U.1    Valtonen, P.2    Kelo, E.3    Mononen, I.4
  • 11
    • 13444256574 scopus 로고    scopus 로고
    • Massive accumulation of Man2GlcNAc2-Asn in nonneuronal tissues of glycosylasparaginase-deficient mice and its removal by enzyme replacement therapy
    • Kelo, E., Dunder, U. & Mononen, I. Massive accumulation of Man2GlcNAc2-Asn in nonneuronal tissues of glycosylasparaginase-deficient mice and its removal by enzyme replacement therapy. Glycobiology 15, 79-85 (2005).
    • (2005) Glycobiology , vol.15 , pp. 79-85
    • Kelo, E.1    Dunder, U.2    Mononen, I.3
  • 12
    • 0031788218 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse
    • Peltola, M. et al. Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse. Gene Ther 5, 1314-1321 (1998).
    • (1998) Gene Ther , vol.5 , pp. 1314-1321
    • Peltola, M.1
  • 13
    • 33745281681 scopus 로고    scopus 로고
    • Use of nonviral promoters in adenovirus-mediated gene therapy: Reduction of lysosomal storage in the aspartylglucosaminuria mouse
    • Virta, S., Rapola, J., Jalanko, A. & Laine, M. Use of nonviral promoters in adenovirus-mediated gene therapy: reduction of lysosomal storage in the aspartylglucosaminuria mouse. J Gene Med 8, 699-706 (2006).
    • (2006) J Gene Med , vol.8 , pp. 699-706
    • Virta, S.1    Rapola, J.2    Jalanko, A.3    Laine, M.4
  • 14
    • 84876225140 scopus 로고    scopus 로고
    • Pharmacological chaperones as therapeutics for lysosomal storage diseases
    • Boyd, R. E. et al. Pharmacological chaperones as therapeutics for lysosomal storage diseases. J Med Chem 56, 2705-2725 (2013).
    • (2013) J Med Chem , vol.56 , pp. 2705-2725
    • Boyd, R.E.1
  • 15
    • 77449098166 scopus 로고    scopus 로고
    • Treating lysosomal storage diseases with pharmacological chaperones: From concept to clinics
    • Parenti, G. Treating lysosomal storage diseases with pharmacological chaperones: from concept to clinics. EMBO Mol Med 1, 268-279 (2009).
    • (2009) EMBO Mol Med , vol.1 , pp. 268-279
    • Parenti, G.1
  • 16
    • 84921324921 scopus 로고    scopus 로고
    • Lysosomal storage diseases: From pathophysiology to therapy
    • Parenti, G., Andria, G. & Ballabio, A. Lysosomal storage diseases: from pathophysiology to therapy. Annu Rev Med 66, 471-486 (2015).
    • (2015) Annu Rev Med , vol.66 , pp. 471-486
    • Parenti, G.1    Andria, G.2    Ballabio, A.3
  • 17
    • 33846020543 scopus 로고    scopus 로고
    • Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs
    • Arakawa, T., Ejima, D., Kita, Y. & Tsumoto, K. Small molecule pharmacological chaperones: From thermodynamic stabilization to pharmaceutical drugs. Biochim Biophys Acta 1764, 1677-1687 (2006).
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1677-1687
    • Arakawa, T.1    Ejima, D.2    Kita, Y.3    Tsumoto, K.4
  • 18
    • 34748866532 scopus 로고    scopus 로고
    • Active-site-specific chaperone therapy for Fabry disease. Yin and Yang of enzyme inhibitors
    • Fan, J. Q. & Ishii, S. Active-site-specific chaperone therapy for Fabry disease. Yin and Yang of enzyme inhibitors. FEBS J 274, 4962-4971 (2007).
    • (2007) FEBS J , vol.274 , pp. 4962-4971
    • Fan, J.Q.1    Ishii, S.2
  • 19
    • 0025988646 scopus 로고
    • In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation
    • Ikonen, E., Enomaa, N., Ulmanen, I. & Peltonen, L. In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation. Genomics 11, 206-211 (1991).
    • (1991) Genomics , vol.11 , pp. 206-211
    • Ikonen, E.1    Enomaa, N.2    Ulmanen, I.3    Peltonen, L.4
  • 20
    • 0029835573 scopus 로고    scopus 로고
    • Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization
    • Riikonen, A. et al. Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization. J Biol Chem 271, 21340-21344 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 21340-21344
    • Riikonen, A.1
  • 21
    • 0030780140 scopus 로고    scopus 로고
    • Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase
    • Tikkanen, R., Peltola, M., Oinonen, C., Rouvinen, J. & Peltonen, L. Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase. EMBO J 16, 6684-6693 (1997).
    • (1997) EMBO J , vol.16 , pp. 6684-6693
    • Tikkanen, R.1    Peltola, M.2    Oinonen, C.3    Rouvinen, J.4    Peltonen, L.5
  • 22
    • 84905164552 scopus 로고    scopus 로고
    • Pharmacological chaperone therapy for lysosomal storage diseases
    • Parenti, G., Moracci, M., Fecarotta, S. & Andria, G. Pharmacological chaperone therapy for lysosomal storage diseases. Future Med Chem 6, 1031-1045 (2014).
    • (2014) Future Med Chem , vol.6 , pp. 1031-1045
    • Parenti, G.1    Moracci, M.2    Fecarotta, S.3    Andria, G.4
  • 23
    • 17044443537 scopus 로고    scopus 로고
    • Bone marrow transplantation in aspartylglucosaminuria-histopathological and MRI study
    • Autti, T. et al. Bone marrow transplantation in aspartylglucosaminuria-histopathological and MRI study. Neuropediatrics 30, 283-288 (1999).
    • (1999) Neuropediatrics , vol.30 , pp. 283-288
    • Autti, T.1
  • 24
    • 0030887772 scopus 로고    scopus 로고
    • Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation
    • Laitinen, A. et al. Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation. Clin Genet 51, 174-178 (1997).
    • (1997) Clin Genet , vol.51 , pp. 174-178
    • Laitinen, A.1
  • 25
    • 6844252256 scopus 로고    scopus 로고
    • Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients
    • Jalanko, A. et al. Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients. Hum Mol Genet 7, 265-272 (1998).
    • (1998) Hum Mol Genet , vol.7 , pp. 265-272
    • Jalanko, A.1
  • 26
    • 0029850423 scopus 로고    scopus 로고
    • A mouse model for the human lysosomal disease aspartylglycosaminuria
    • Kaartinen, V. et al. A mouse model for the human lysosomal disease aspartylglycosaminuria. Nat Med 2, 1375-1378 (1996).
    • (1996) Nat Med , vol.2 , pp. 1375-1378
    • Kaartinen, V.1
  • 27
    • 84875217250 scopus 로고    scopus 로고
    • Gene therapy and neurodevelopmental disorders
    • Gray, S. J. Gene therapy and neurodevelopmental disorders. Neuropharmacology 68, 136-142 (2013).
    • (2013) Neuropharmacology , vol.68 , pp. 136-142
    • Gray, S.J.1
  • 28
    • 0028086586 scopus 로고
    • Dissection of the molecular consequences of a double mutation causing a human lysosomal disease
    • Riikonen, A. et al. Dissection of the molecular consequences of a double mutation causing a human lysosomal disease. DNA Cell Biol 13, 257-264 (1994).
    • (1994) DNA Cell Biol , vol.13 , pp. 257-264
    • Riikonen, A.1
  • 29
    • 84914154673 scopus 로고    scopus 로고
    • Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria
    • Sui, L., Lakshminarasimhan, D., Pande, S. & Guo, H. C. Structural basis of a point mutation that causes the genetic disease aspartylglucosaminuria. Structure 22, 1855-1861 (2014).
    • (2014) Structure , vol.22 , pp. 1855-1861
    • Sui, L.1    Lakshminarasimhan, D.2    Pande, S.3    Guo, H.C.4
  • 30
    • 0037474204 scopus 로고    scopus 로고
    • Two-step dimerization for autoproteolysis to activate glycosylasparaginase
    • Wang, Y. & Guo, H. C. Two-step dimerization for autoproteolysis to activate glycosylasparaginase. J Biol Chem 278, 3210-3219 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 3210-3219
    • Wang, Y.1    Guo, H.C.2
  • 31
    • 0030051163 scopus 로고    scopus 로고
    • Activation of glycosylasparaginase. Formation of active N-terminal threonine by intramolecular autoproteolysis
    • Guan, C. et al. Activation of glycosylasparaginase. Formation of active N-terminal threonine by intramolecular autoproteolysis. J Biol Chem 271, 1732-1737 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 1732-1737
    • Guan, C.1
  • 32
    • 0034844352 scopus 로고    scopus 로고
    • Glycosylasparaginase inhibition studies: Competitive inhibitors, transition state mimics, noncompetitive inhibitors
    • Risley, J. M., Huang, D. H., Kaylor, J. J., Malik, J. J. & Xia, Y. Q. Glycosylasparaginase inhibition studies: competitive inhibitors, transition state mimics, noncompetitive inhibitors. J Enzyme Inhib 16, 269-274 (2001).
    • (2001) J Enzyme Inhib , vol.16 , pp. 269-274
    • Risley, J.M.1    Huang, D.H.2    Kaylor, J.J.3    Malik, J.J.4    Xia, Y.Q.5
  • 33
    • 0033520327 scopus 로고    scopus 로고
    • Structural insights into the mechanism of intramolecular proteolysis
    • Xu, Q., Buckley, D., Guan, C. & Guo, H. C. Structural insights into the mechanism of intramolecular proteolysis. Cell 98, 651-661 (1999).
    • (1999) Cell , vol.98 , pp. 651-661
    • Xu, Q.1    Buckley, D.2    Guan, C.3    Guo, H.C.4
  • 34
    • 84876489098 scopus 로고    scopus 로고
    • Free glycine accelerates the autoproteolytic activation of human asparaginase
    • Su, Y. et al. Free glycine accelerates the autoproteolytic activation of human asparaginase. Chem Biol 20, 533-540 (2013).
    • (2013) Chem Biol , vol.20 , pp. 533-540
    • Su, Y.1
  • 35
    • 4544358286 scopus 로고    scopus 로고
    • Betaine in human nutrition
    • Craig, S. A. Betaine in human nutrition. Am J Clin Nutr 80, 539-549 (2004).
    • (2004) Am J Clin Nutr , vol.80 , pp. 539-549
    • Craig, S.A.1
  • 36
    • 77950409779 scopus 로고    scopus 로고
    • Recovery of PEX1-Gly843Asp peroxisome dysfunction by small-molecule compounds
    • Zhang, R. et al. Recovery of PEX1-Gly843Asp peroxisome dysfunction by small-molecule compounds. Proc Natl Acad Sci USA 107, 5569-5574 (2010).
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5569-5574
    • Zhang, R.1
  • 37
    • 0038132253 scopus 로고    scopus 로고
    • Primary hyperoxaluria type 1 in the Canary Islands: A conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase
    • Santana, A., Salido, E., Torres, A. & Shapiro, L. J. Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase. Proc Natl Acad Sci USA 100, 7277-7282 (2003).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7277-7282
    • Santana, A.1    Salido, E.2    Torres, A.3    Shapiro, L.J.4
  • 38
    • 4644224470 scopus 로고    scopus 로고
    • Correlation between enzyme activity and substrate storage in a cell culture model system for Gaucher disease
    • Schueler, U. H. et al. Correlation between enzyme activity and substrate storage in a cell culture model system for Gaucher disease. J Inherit Metab Dis 27, 649-658 (2004).
    • (2004) J Inherit Metab Dis , vol.27 , pp. 649-658
    • Schueler, U.H.1
  • 39
    • 84874310194 scopus 로고    scopus 로고
    • Restoration of cytoskeleton homeostasis after gigaxonin gene transfer for giant axonal neuropathy
    • Mussche, S. et al. Restoration of cytoskeleton homeostasis after gigaxonin gene transfer for giant axonal neuropathy. Hum Gene Ther 24, 209-219 (2013).
    • (2013) Hum Gene Ther , vol.24 , pp. 209-219
    • Mussche, S.1
  • 40
    • 0034252326 scopus 로고    scopus 로고
    • The dileucine motif within the tail of MPR46 is required for sorting of the receptor in endosomes
    • Tikkanen, R. et al. The dileucine motif within the tail of MPR46 is required for sorting of the receptor in endosomes. Traffic 1, 631-640 (2000).
    • (2000) Traffic , vol.1 , pp. 631-640
    • Tikkanen, R.1
  • 41
    • 0027381797 scopus 로고
    • Applications of a new fluorimetric enzyme assay for the diagnosis of aspartylglucosaminuria
    • Voznyi Ya, V. et al. Applications of a new fluorimetric enzyme assay for the diagnosis of aspartylglucosaminuria. J Inherit Metab Dis 16, 929-934 (1993).
    • (1993) J Inherit Metab Dis , vol.16 , pp. 929-934
    • Voznyi Ya, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.