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Volumn 1864, Issue 2, 2018, Pages 640-648

New perspectives for pharmacological chaperoning treatment in methylmalonic aciduria cblB type

Author keywords

ATR; Destabilizing mutations; MMA cblB type; MMAB; Pharmacological chaperones

Indexed keywords

4 [4 (4 FLUOROPHENYL) 5 METHYL 1H PYRAZOL 3 YL]BENZENE 1,3 DIOL; ATP:COB(I)ALAMIN ADENOSYLTRANSFERASE; ATR PROTEIN; CHAPERONE; COBALAMIN; COBAMAMIDE; COMPLEMENTARY DNA; HYDROXOCOBALAMIN; METHYLMALONYL COENZYME A MUTASE; MONOMER; N [[(4 CHLOROPHENYL)CARBAMOTHIOYL]AMINO] 2 PHENYLACETAMIDE; RECOMBINANT PROTEIN; TRANSFERASE; UNCLASSIFIED DRUG; CBL PROTEIN; CBLB PROTEIN, HUMAN; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 85037974346     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2017.11.024     Document Type: Article
Times cited : (10)

References (52)
  • 1
    • 79952302420 scopus 로고    scopus 로고
    • Genetic disorders of vitamin B(1)(2) metabolism: eight complementation groups–eight genes
    • Froese, D.S., Gravel, R.A., Genetic disorders of vitamin B(1)(2) metabolism: eight complementation groups–eight genes. Expert Rev. Mol. Med., 12, 2010, e37.
    • (2010) Expert Rev. Mol. Med. , vol.12 , pp. e37
    • Froese, D.S.1    Gravel, R.A.2
  • 2
    • 33845937432 scopus 로고    scopus 로고
    • Structure of ATP-bound human ATP:cobalamin adenosyltransferase
    • Schubert, H.L., Hill, C.P., Structure of ATP-bound human ATP:cobalamin adenosyltransferase. Biochemistry 45 (2006), 15188–15196.
    • (2006) Biochemistry , vol.45 , pp. 15188-15196
    • Schubert, H.L.1    Hill, C.P.2
  • 5
    • 45849132005 scopus 로고    scopus 로고
    • Causes of and diagnostic approach to methylmalonic acidurias
    • Fowler, B., Leonard, J.V., Baumgartner, M.R., Causes of and diagnostic approach to methylmalonic acidurias. J. Inherit. Metab. Dis. 31 (2008), 350–360.
    • (2008) J. Inherit. Metab. Dis. , vol.31 , pp. 350-360
    • Fowler, B.1    Leonard, J.V.2    Baumgartner, M.R.3
  • 9
    • 85008496913 scopus 로고    scopus 로고
    • When proteostasis goes bad: protein aggregation in the cell
    • Radwan, M., Wood, R.J., Sui, X., Hatters, D.M., When proteostasis goes bad: protein aggregation in the cell. IUBMB Life 69 (2017), 49–54.
    • (2017) IUBMB Life , vol.69 , pp. 49-54
    • Radwan, M.1    Wood, R.J.2    Sui, X.3    Hatters, D.M.4
  • 10
    • 84890204277 scopus 로고
    • Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system
    • Amm, I., Sommer, T., Wolf, D.H., Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim. Biophys. Acta 2014 (1843), 182–196.
    • (1843) Biochim. Biophys. Acta , vol.2014 , pp. 182-196
    • Amm, I.1    Sommer, T.2    Wolf, D.H.3
  • 11
    • 84904099631 scopus 로고    scopus 로고
    • Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators
    • Muntau, A.C., Leandro, J., Staudigl, M., Mayer, F., Gersting, S.W., Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators. J. Inherit. Metab. Dis. 37 (2014), 505–523.
    • (2014) J. Inherit. Metab. Dis. , vol.37 , pp. 505-523
    • Muntau, A.C.1    Leandro, J.2    Staudigl, M.3    Mayer, F.4    Gersting, S.W.5
  • 12
    • 84973121809 scopus 로고    scopus 로고
    • From structural biology to designing therapy for inborn errors of metabolism
    • Yue, W.W., From structural biology to designing therapy for inborn errors of metabolism. J. Inherit. Metab. Dis. 39 (2016), 489–498.
    • (2016) J. Inherit. Metab. Dis. , vol.39 , pp. 489-498
    • Yue, W.W.1
  • 13
    • 84901912352 scopus 로고    scopus 로고
    • Pharmacological chaperoning: a primer on mechanism and pharmacology
    • Leidenheimer, N.J., Ryder, K.G., Pharmacological chaperoning: a primer on mechanism and pharmacology. Pharmacol. Res. 83 (2014), 10–19.
    • (2014) Pharmacol. Res. , vol.83 , pp. 10-19
    • Leidenheimer, N.J.1    Ryder, K.G.2
  • 14
    • 84900131626 scopus 로고    scopus 로고
    • Pharmacological chaperones for enzyme enhancement therapy in genetic diseases
    • Aymami, J., Barril, X., Rodriguez-Pascau, L., Martinell, M., Pharmacological chaperones for enzyme enhancement therapy in genetic diseases. Pharm. Pat. Anal. 2 (2013), 109–124.
    • (2013) Pharm. Pat. Anal. , vol.2 , pp. 109-124
    • Aymami, J.1    Barril, X.2    Rodriguez-Pascau, L.3    Martinell, M.4
  • 16
    • 84873052980 scopus 로고    scopus 로고
    • A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics
    • Jaffe, E.K., Stith, L., Lawrence, S.H., Andrake, M., Dunbrack, R.L. Jr., A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics. Arch. Biochem. Biophys. 530 (2013), 73–82.
    • (2013) Arch. Biochem. Biophys. , vol.530 , pp. 73-82
    • Jaffe, E.K.1    Stith, L.2    Lawrence, S.H.3    Andrake, M.4    Dunbrack, R.L.5
  • 17
    • 84901840776 scopus 로고    scopus 로고
    • Using pharmacological chaperones to restore proteostasis
    • Wang, Y.J., Di, X.J., Mu, T.W., Using pharmacological chaperones to restore proteostasis. Pharmacol. Res. 83 (2014), 3–9.
    • (2014) Pharmacol. Res. , vol.83 , pp. 3-9
    • Wang, Y.J.1    Di, X.J.2    Mu, T.W.3
  • 18
    • 50249175120 scopus 로고    scopus 로고
    • Chemical and biological approaches synergize to ameliorate protein-folding diseases
    • Mu, T.W., Ong, D.S., Wang, Y.J., Balch, W.E., Yates, J.R. 3rd, Segatori, L., Kelly, J.W., Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134 (2008), 769–781.
    • (2008) Cell , vol.134 , pp. 769-781
    • Mu, T.W.1    Ong, D.S.2    Wang, Y.J.3    Balch, W.E.4    Yates, J.R.5    Segatori, L.6    Kelly, J.W.7
  • 19
    • 33645113221 scopus 로고    scopus 로고
    • Impact of cblB mutations on the function of ATP:cob(I)alamin adenosyltransferase in disorders of vitamin B12 metabolism
    • Zhang, J., Dobson, C.M., Wu, X., Lerner-Ellis, J., Rosenblatt, D.S., Gravel, R.A., Impact of cblB mutations on the function of ATP:cob(I)alamin adenosyltransferase in disorders of vitamin B12 metabolism. Mol. Genet. Metab. 87 (2006), 315–322.
    • (2006) Mol. Genet. Metab. , vol.87 , pp. 315-322
    • Zhang, J.1    Dobson, C.M.2    Wu, X.3    Lerner-Ellis, J.4    Rosenblatt, D.S.5    Gravel, R.A.6
  • 20
    • 70349735996 scopus 로고    scopus 로고
    • Ligand-binding by catalytically inactive mutants of the cblB complementation group defective in human ATP:cob(I)alamin adenosyltransferase
    • Zhang, J., Wu, X., Padovani, D., Schubert, H.L., Gravel, R.A., Ligand-binding by catalytically inactive mutants of the cblB complementation group defective in human ATP:cob(I)alamin adenosyltransferase. Mol. Genet. Metab. 98 (2009), 278–284.
    • (2009) Mol. Genet. Metab. , vol.98 , pp. 278-284
    • Zhang, J.1    Wu, X.2    Padovani, D.3    Schubert, H.L.4    Gravel, R.A.5
  • 22
    • 0002056004 scopus 로고
    • Microcalorimetry and the molecular recognition of peptides and proteins
    • Cooper, A., McAuley-Hecht, K., Microcalorimetry and the molecular recognition of peptides and proteins. Philos. Trans. R. Soc. Lond. 345 (1993), 23–35.
    • (1993) Philos. Trans. R. Soc. Lond. , vol.345 , pp. 23-35
    • Cooper, A.1    McAuley-Hecht, K.2
  • 23
    • 77950571108 scopus 로고    scopus 로고
    • New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays
    • Baell, J.B., Holloway, G.A., New substructure filters for removal of pan assay interference compounds (PAINS) from screening libraries and for their exclusion in bioassays. J. Med. Chem. 53 (2010), 2719–2740.
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2
  • 24
    • 84862859338 scopus 로고    scopus 로고
    • Rhodanine as a scaffold in drug discovery: a critical review of its biological activities and mechanisms of target modulation
    • Tomasic, T., Peterlin Masic, L., Rhodanine as a scaffold in drug discovery: a critical review of its biological activities and mechanisms of target modulation. Expert Opin. Drug Discovery 7 (2012), 549–560.
    • (2012) Expert Opin. Drug Discovery , vol.7 , pp. 549-560
    • Tomasic, T.1    Peterlin Masic, L.2
  • 26
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • Veber, D.F., Johnson, S.R., Cheng, H.Y., Smith, B.R., Ward, K.W., Kopple, K.D., Molecular properties that influence the oral bioavailability of drug candidates. J. Med. Chem. 45 (2002), 2615–2623.
    • (2002) J. Med. Chem. , vol.45 , pp. 2615-2623
    • Veber, D.F.1    Johnson, S.R.2    Cheng, H.Y.3    Smith, B.R.4    Ward, K.W.5    Kopple, K.D.6
  • 27
    • 0034609833 scopus 로고    scopus 로고
    • Fast calculation of molecular polar surface area as a sum of fragment-based contributions and its application to the prediction of drug transport properties
    • Ertl, P., Rohde, B., Selzer, P., Fast calculation of molecular polar surface area as a sum of fragment-based contributions and its application to the prediction of drug transport properties. J. Med. Chem. 43 (2000), 3714–3717.
    • (2000) J. Med. Chem. , vol.43 , pp. 3714-3717
    • Ertl, P.1    Rohde, B.2    Selzer, P.3
  • 28
    • 33846078171 scopus 로고    scopus 로고
    • Identification and evaluation of molecular properties related to preclinical optimization and clinical fate
    • Blake, J.F., Identification and evaluation of molecular properties related to preclinical optimization and clinical fate. Med. Chem. 1 (2005), 649–655.
    • (2005) Med. Chem. , vol.1 , pp. 649-655
    • Blake, J.F.1
  • 30
    • 0012286670 scopus 로고    scopus 로고
    • Pharmacokinetically based mapping device for chemical space navigation
    • Oprea, T.I., Zamora, I., Ungell, A.L., Pharmacokinetically based mapping device for chemical space navigation. J. Comb. Chem. 4 (2002), 258–266.
    • (2002) J. Comb. Chem. , vol.4 , pp. 258-266
    • Oprea, T.I.1    Zamora, I.2    Ungell, A.L.3
  • 31
    • 33745172773 scopus 로고    scopus 로고
    • A journey of hope: lessons learned from studies on rare diseases and orphan drugs
    • Wastfelt, M., Fadeel, B., Henter, J.I., A journey of hope: lessons learned from studies on rare diseases and orphan drugs. J. Intern. Med. 260 (2006), 1–10.
    • (2006) J. Intern. Med. , vol.260 , pp. 1-10
    • Wastfelt, M.1    Fadeel, B.2    Henter, J.I.3
  • 34
    • 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 (2009), 268–279.
    • (2009) EMBO Mol. Med. , vol.1 , pp. 268-279
    • Parenti, G.1
  • 35
    • 67349206148 scopus 로고    scopus 로고
    • The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts
    • Porto, C., Cardone, M., Fontana, F., Rossi, B., Tuzzi, M.R., Tarallo, A., Barone, M.V., Andria, G., Parenti, G., The pharmacological chaperone N-butyldeoxynojirimycin enhances enzyme replacement therapy in Pompe disease fibroblasts. Mol. Ther. 17 (2009), 964–971.
    • (2009) Mol. Ther. , vol.17 , pp. 964-971
    • Porto, C.1    Cardone, M.2    Fontana, F.3    Rossi, B.4    Tuzzi, M.R.5    Tarallo, A.6    Barone, M.V.7    Andria, G.8    Parenti, G.9
  • 36
    • 79957628617 scopus 로고    scopus 로고
    • Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders
    • Valenzano, K.J., Khanna, R., Powe, A.C., Boyd, R., Lee, G., Flanagan, J.J., Benjamin, E.R., Identification and characterization of pharmacological chaperones to correct enzyme deficiencies in lysosomal storage disorders. Assay Drug Dev. Technol. 9 (2011), 213–235.
    • (2011) Assay Drug Dev. Technol. , vol.9 , pp. 213-235
    • Valenzano, K.J.1    Khanna, R.2    Powe, A.C.3    Boyd, R.4    Lee, G.5    Flanagan, J.J.6    Benjamin, E.R.7
  • 37
    • 84873397801 scopus 로고    scopus 로고
    • Novel pharmacological strategies to treat cystic fibrosis
    • Hanrahan, J.W., Sampson, H.M., Thomas, D.Y., Novel pharmacological strategies to treat cystic fibrosis. Trends Pharmacol. Sci. 34 (2013), 119–125.
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 119-125
    • Hanrahan, J.W.1    Sampson, H.M.2    Thomas, D.Y.3
  • 38
    • 84912103263 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib reduced cholesterol accumulation in fibroblasts from Niemann-pick type C patients carrying missense mutations
    • Macias-Vidal, J., Giros, M., Guerrero, M., Gascon, P., Serratosa, J., Bachs, O., Coll, M.J., The proteasome inhibitor bortezomib reduced cholesterol accumulation in fibroblasts from Niemann-pick type C patients carrying missense mutations. FEBS J. 281 (2014), 4450–4466.
    • (2014) FEBS J. , vol.281 , pp. 4450-4466
    • Macias-Vidal, J.1    Giros, M.2    Guerrero, M.3    Gascon, P.4    Serratosa, J.5    Bachs, O.6    Coll, M.J.7
  • 41
    • 79958701058 scopus 로고    scopus 로고
    • Growing PAINS in academic drug discovery
    • Whitty, A., Growing PAINS in academic drug discovery. Future Med. Chem. 3 (2011), 797–801.
    • (2011) Future Med. Chem. , vol.3 , pp. 797-801
    • Whitty, A.1
  • 42
    • 84926291678 scopus 로고    scopus 로고
    • Mitigating risk in academic preclinical drug discovery
    • Dahlin, J.L., Inglese, J., Walters, M.A., Mitigating risk in academic preclinical drug discovery. Nat. Rev. Drug Discov. 14 (2015), 279–294.
    • (2015) Nat. Rev. Drug Discov. , vol.14 , pp. 279-294
    • Dahlin, J.L.1    Inglese, J.2    Walters, M.A.3
  • 43
    • 84924708699 scopus 로고    scopus 로고
    • Screening-based translation of public research encounters painful problems
    • Baell, J.B., Screening-based translation of public research encounters painful problems. ACS Med. Chem. Lett. 6 (2015), 229–234.
    • (2015) ACS Med. Chem. Lett. , vol.6 , pp. 229-234
    • Baell, J.B.1
  • 44
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C.A., Lombardo, F., Dominy, B.W., Feeney, P.J., Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46 (2001), 3–26.
    • (2001) Adv. Drug Deliv. Rev. , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 45
    • 13244266921 scopus 로고    scopus 로고
    • Lead- and drug-like compounds: the rule-of-five revolution
    • Lipinski, C.A., Lead- and drug-like compounds: the rule-of-five revolution. Drug Discov. Today Technol. 1 (2004), 337–341.
    • (2004) Drug Discov. Today Technol. , vol.1 , pp. 337-341
    • Lipinski, C.A.1
  • 46
    • 85016268657 scopus 로고    scopus 로고
    • In vitro generated hepatocyte-like cells: a novel tool in regenerative medicine and drug discovery
    • Zakikhan, K., Pournasr, B., Vosough, M., Nassiri-Asl, M., In vitro generated hepatocyte-like cells: a novel tool in regenerative medicine and drug discovery. Cell J. 19 (2017), 204–217.
    • (2017) Cell J. , vol.19 , pp. 204-217
    • Zakikhan, K.1    Pournasr, B.2    Vosough, M.3    Nassiri-Asl, M.4
  • 47
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G., Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62 (1951), 293–300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 48
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976), 248–254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 49
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F.H., Berglund, H., Vedadi, M., The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2 (2007), 2212–2221.
    • (2007) Nat. Protoc. , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 50
    • 84869413146 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis in homocystinuria patients with genetic remethylation defects
    • Richard, E., Desviat, L.R., Ugarte, M., Perez, B., Oxidative stress and apoptosis in homocystinuria patients with genetic remethylation defects. J. Cell. Biochem. 114 (2013), 183–191.
    • (2013) J. Cell. Biochem. , vol.114 , pp. 183-191
    • Richard, E.1    Desviat, L.R.2    Ugarte, M.3    Perez, B.4
  • 52
    • 79958242366 scopus 로고    scopus 로고
    • Fast docking using the CHARMM force field with EADock DSS
    • Grosdidier, A., Zoete, V., Michielin, O., Fast docking using the CHARMM force field with EADock DSS. J. Comput. Chem. 32 (2011), 2149–2159.
    • (2011) J. Comput. Chem. , vol.32 , pp. 2149-2159
    • Grosdidier, A.1    Zoete, V.2    Michielin, O.3


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