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Volumn 8, Issue 7, 2013, Pages

Dimerization of the Glucan Phosphatase Laforin Requires the Participation of Cysteine 329

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; CYSTEINE 329; DIMER; GLUCAN; GLUCAN PHOSPHATASE; LAFORIN; PHOSPHATASE; RECOMBINANT PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 84880839474     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069523     Document Type: Article
Times cited : (9)

References (57)
  • 1
    • 17344362307 scopus 로고    scopus 로고
    • Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy
    • Minassian BA, Lee JR, Herbrick JA, Huizenga J, Soder S, et al. (1998) Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet 20: 171-174.
    • (1998) Nat Genet , vol.20 , pp. 171-174
    • Minassian, B.A.1    Lee, J.R.2    Herbrick, J.A.3    Huizenga, J.4    Soder, S.5
  • 2
    • 0344359726 scopus 로고    scopus 로고
    • A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)
    • Serratosa JM, Gomez-Garre P, Gallardo ME, Anta B, de Bernabe DB, et al. (1999) A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2). Hum Mol Genet 8: 345-352.
    • (1999) Hum Mol Genet , vol.8 , pp. 345-352
    • Serratosa, J.M.1    Gomez-Garre, P.2    Gallardo, M.E.3    Anta, B.4    de Bernabe, D.B.5
  • 3
    • 77953308953 scopus 로고    scopus 로고
    • Lafora disease: epidemiology, pathophysiology and management
    • Monaghan TS, Delanty N, (2010) Lafora disease: epidemiology, pathophysiology and management. CNS Drugs 24: 549-561.
    • (2010) CNS Drugs , vol.24 , pp. 549-561
    • Monaghan, T.S.1    Delanty, N.2
  • 4
    • 0034907260 scopus 로고    scopus 로고
    • Lafora's disease: towards a clinical, pathologic, and molecular synthesis
    • Minassian BA, (2001) Lafora's disease: towards a clinical, pathologic, and molecular synthesis. Pediatr Neurol 25: 21-29.
    • (2001) Pediatr Neurol , vol.25 , pp. 21-29
    • Minassian, B.A.1
  • 5
    • 78149272475 scopus 로고    scopus 로고
    • Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin
    • Rao SN, Maity R, Sharma J, Dey P, Shankar SK, et al. (2010) Sequestration of chaperones and proteasome into Lafora bodies and proteasomal dysfunction induced by Lafora disease-associated mutations of malin. Hum Mol Genet 19: 4726-4734.
    • (2010) Hum Mol Genet , vol.19 , pp. 4726-4734
    • Rao, S.N.1    Maity, R.2    Sharma, J.3    Dey, P.4    Shankar, S.K.5
  • 6
    • 33749620777 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates
    • Worby CA, Gentry MS, Dixon JE, (2006) Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates. J Biol Chem 281: 30412-30418.
    • (2006) J Biol Chem , vol.281 , pp. 30412-30418
    • Worby, C.A.1    Gentry, M.S.2    Dixon, J.E.3
  • 7
    • 37649004558 scopus 로고    scopus 로고
    • Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo
    • Tagliabracci VS, Turnbull J, Wang W, Girard JM, Zhao X, et al. (2007) Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo. Proc Natl Acad Sci U S A 104: 19262-19266.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19262-19266
    • Tagliabracci, V.S.1    Turnbull, J.2    Wang, W.3    Girard, J.M.4    Zhao, X.5
  • 8
    • 70449955237 scopus 로고    scopus 로고
    • Lafora disease: insights into neurodegeneration from plant metabolism
    • Gentry MS, Dixon JE, Worby CA (2009) Lafora disease: insights into neurodegeneration from plant metabolism. Trends Biochem Sci.
    • (2009) Trends Biochem Sci
    • Gentry, M.S.1    Dixon, J.E.2    Worby, C.A.3
  • 9
    • 34547559799 scopus 로고    scopus 로고
    • The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease
    • Gentry MS, Dowen RH 3rd, Worby CA, Mattoo S, Ecker JR, et al (2007) The phosphatase laforin crosses evolutionary boundaries and links carbohydrate metabolism to neuronal disease. J Cell Biol 178: 477-488.
    • (2007) J Cell Biol , vol.178 , pp. 477-488
    • Gentry, M.S.1    Dowen 3rd, R.H.2    Worby, C.A.3    Mattoo, S.4    Ecker, J.R.5
  • 11
    • 80054056849 scopus 로고    scopus 로고
    • Are there errors in glycogen biosynthesis and is laforin a repair enzyme?
    • Roach PJ, (2011) Are there errors in glycogen biosynthesis and is laforin a repair enzyme? FEBS Letters 585: 3216-3218.
    • (2011) FEBS Letters , vol.585 , pp. 3216-3218
    • Roach, P.J.1
  • 12
    • 0014739101 scopus 로고
    • Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea
    • Sakai M, Austin J, Witmer F, Trueb L, (1970) Studies in myoclonus epilepsy (Lafora body form). II. Polyglucosans in the systemic deposits of myoclonus epilepsy and in corpora amylacea. Neurology 20: 160-176.
    • (1970) Neurology , vol.20 , pp. 160-176
    • Sakai, M.1    Austin, J.2    Witmer, F.3    Trueb, L.4
  • 13
    • 0014228289 scopus 로고
    • Histophysical and histochemical investigations of myoclonus bodies
    • Schnabel R, Seitelberger F, (1968) Histophysical and histochemical investigations of myoclonus bodies. Pathol Eur 3: 218-226.
    • (1968) Pathol Eur , vol.3 , pp. 218-226
    • Schnabel, R.1    Seitelberger, F.2
  • 14
    • 57749088693 scopus 로고    scopus 로고
    • Abnormal metabolism of glycogen phosphate as a cause for Lafora disease
    • Tagliabracci VS, Girard JM, Segvich D, Meyer C, Turnbull J, et al. (2008) Abnormal metabolism of glycogen phosphate as a cause for Lafora disease. J Biol Chem 283: 33816-33825.
    • (2008) J Biol Chem , vol.283 , pp. 33816-33825
    • Tagliabracci, V.S.1    Girard, J.M.2    Segvich, D.3    Meyer, C.4    Turnbull, J.5
  • 16
    • 84877293787 scopus 로고    scopus 로고
    • Hyperphosphorylation of glucosyl c6 carbons and altered structure of glycogen in the neurodegenerative epilepsy lafora disease
    • Nitschke F, Wang P, Schmieder P, Girard JM, Awrey DE, et al. (2013) Hyperphosphorylation of glucosyl c6 carbons and altered structure of glycogen in the neurodegenerative epilepsy lafora disease. Cell Metab 17: 756-767.
    • (2013) Cell Metab , vol.17 , pp. 756-767
    • Nitschke, F.1    Wang, P.2    Schmieder, P.3    Girard, J.M.4    Awrey, D.E.5
  • 17
    • 84877721163 scopus 로고    scopus 로고
    • Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii
    • Gentry MS, Romá-Mateo C, Sanz P (2012) Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii. Febs J.
    • (2012) Febs J
    • Gentry, M.S.1    Romá-Mateo, C.2    Sanz, P.3
  • 18
    • 84866711168 scopus 로고    scopus 로고
    • Deciphering the role of malin in the lafora progressive myoclonus epilepsy
    • Romá-Mateo C, Sanz P, Gentry MS, (2012) Deciphering the role of malin in the lafora progressive myoclonus epilepsy. IUBMB Life 64: 801-808.
    • (2012) IUBMB Life , vol.64 , pp. 801-808
    • Romá-Mateo, C.1    Sanz, P.2    Gentry, M.S.3
  • 19
    • 0042831105 scopus 로고    scopus 로고
    • Genetic mapping of a new Lafora progressive myoclonus epilepsy locus (EPM2B) on 6p22
    • Chan EM, Bulman DE, Paterson AD, Turnbull J, Andermann E, et al. (2003) Genetic mapping of a new Lafora progressive myoclonus epilepsy locus (EPM2B) on 6p22. J Med Genet 40: 671-675.
    • (2003) J Med Genet , vol.40 , pp. 671-675
    • Chan, E.M.1    Bulman, D.E.2    Paterson, A.D.3    Turnbull, J.4    Andermann, E.5
  • 20
    • 0141618459 scopus 로고    scopus 로고
    • Mutations in NHLRC1 cause progressive myoclonus epilepsy
    • Chan EM, Young EJ, Ianzano L, Munteanu I, Zhao X, et al. (2003) Mutations in NHLRC1 cause progressive myoclonus epilepsy. Nat Genet 35: 125-127.
    • (2003) Nat Genet , vol.35 , pp. 125-127
    • Chan, E.M.1    Young, E.J.2    Ianzano, L.3    Munteanu, I.4    Zhao, X.5
  • 21
    • 20844463813 scopus 로고    scopus 로고
    • Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin
    • Gentry MS, Worby CA, Dixon JE, (2005) Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc Natl Acad Sci U S A 102: 8501-8506.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8501-8506
    • Gentry, M.S.1    Worby, C.A.2    Dixon, J.E.3
  • 22
    • 35548995067 scopus 로고    scopus 로고
    • Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy
    • Vilchez D, Ros S, Cifuentes D, Pujadas L, Valles J, et al. (2007) Mechanism suppressing glycogen synthesis in neurons and its demise in progressive myoclonus epilepsy. Nat Neurosci 10: 1407-1413.
    • (2007) Nat Neurosci , vol.10 , pp. 1407-1413
    • Vilchez, D.1    Ros, S.2    Cifuentes, D.3    Pujadas, L.4    Valles, J.5
  • 23
    • 34948889895 scopus 로고    scopus 로고
    • A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease
    • Cheng A, Zhang M, Gentry MS, Worby CA, Dixon JE, et al. (2007) A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev 21: 2399-2409.
    • (2007) Genes Dev , vol.21 , pp. 2399-2409
    • Cheng, A.1    Zhang, M.2    Gentry, M.S.3    Worby, C.A.4    Dixon, J.E.5
  • 24
    • 84878903515 scopus 로고    scopus 로고
    • Glycogenic activity of R6; a protein phosphatase 1 regulatory subunit; is modulated by the laforin-malin complex
    • Rubio-Villena C, Garcia-Gimeno MA, Sanz P (2013) Glycogenic activity of R6; a protein phosphatase 1 regulatory subunit; is modulated by the laforin-malin complex. Int J Biochem Cell Biol.
    • (2013) Int J Biochem Cell Biol
    • Rubio-Villena, C.1    Garcia-Gimeno, M.A.2    Sanz, P.3
  • 25
    • 39749136257 scopus 로고    scopus 로고
    • Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway
    • Solaz-Fuster MC, Gimeno-Alcaniz JV, Ros S, Fernandez-Sanchez ME, Garcia-Fojeda B, et al. (2008) Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway. Hum Mol Genet 17: 667-678.
    • (2008) Hum Mol Genet , vol.17 , pp. 667-678
    • Solaz-Fuster, M.C.1    Gimeno-Alcaniz, J.V.2    Ros, S.3    Fernandez-Sanchez, M.E.4    Garcia-Fojeda, B.5
  • 26
    • 79960321996 scopus 로고    scopus 로고
    • Malin and laforin are essential components of a protein complex that protects cells from thermal stress
    • Sengupta S, Badhwar I, Upadhyay M, Singh S, Ganesh S, (2011) Malin and laforin are essential components of a protein complex that protects cells from thermal stress. J Cell Sci 124: 2277-2286.
    • (2011) J Cell Sci , vol.124 , pp. 2277-2286
    • Sengupta, S.1    Badhwar, I.2    Upadhyay, M.3    Singh, S.4    Ganesh, S.5
  • 27
    • 74049116574 scopus 로고    scopus 로고
    • Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease
    • Rao SN, Sharma J, Maity R, Jana NR, (2010) Co-chaperone CHIP stabilizes aggregate-prone malin, a ubiquitin ligase mutated in Lafora disease. J Biol Chem 285: 1404-1413.
    • (2010) J Biol Chem , vol.285 , pp. 1404-1413
    • Rao, S.N.1    Sharma, J.2    Maity, R.3    Jana, N.R.4
  • 28
    • 34447341732 scopus 로고    scopus 로고
    • Lafora disease proteins malin and laforin are recruited to aggresomes in response to proteasomal impairment
    • Mittal S, Dubey D, Yamakawa K, Ganesh S, (2007) Lafora disease proteins malin and laforin are recruited to aggresomes in response to proteasomal impairment. Hum Mol Genet 16: 753-762.
    • (2007) Hum Mol Genet , vol.16 , pp. 753-762
    • Mittal, S.1    Dubey, D.2    Yamakawa, K.3    Ganesh, S.4
  • 29
    • 77954486784 scopus 로고    scopus 로고
    • Laforin, the most common protein mutated in Lafora disease, regulates autophagy
    • Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, et al. (2010) Laforin, the most common protein mutated in Lafora disease, regulates autophagy. Hum Mol Genet 19: 2867-2876.
    • (2010) Hum Mol Genet , vol.19 , pp. 2867-2876
    • Aguado, C.1    Sarkar, S.2    Korolchuk, V.I.3    Criado, O.4    Vernia, S.5
  • 30
    • 84858183902 scopus 로고    scopus 로고
    • Lafora bodies and neurological defects in malin-deficient mice correlate with impaired autophagy
    • Criado O, Aguado C, Gayarre J, Duran-Trio L, Garcia-Cabrero AM, et al. (2012) Lafora bodies and neurological defects in malin-deficient mice correlate with impaired autophagy. Hum Mol Genet 21: 1521-1533.
    • (2012) Hum Mol Genet , vol.21 , pp. 1521-1533
    • Criado, O.1    Aguado, C.2    Gayarre, J.3    Duran-Trio, L.4    Garcia-Cabrero, A.M.5
  • 31
    • 78649240333 scopus 로고    scopus 로고
    • Laforin in autophagy: a possible link between carbohydrate and protein in Lafora disease?
    • Puri R, Ganesh S, (2010) Laforin in autophagy: a possible link between carbohydrate and protein in Lafora disease? Autophagy 6: 1229-1231.
    • (2010) Autophagy , vol.6 , pp. 1229-1231
    • Puri, R.1    Ganesh, S.2
  • 32
    • 67650110001 scopus 로고    scopus 로고
    • Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin
    • Vernia S, Rubio T, Heredia M, Rodriguez de Cordoba S, Sanz P, (2009) Increased endoplasmic reticulum stress and decreased proteasomal function in lafora disease models lacking the phosphatase laforin. PLoS One 4: e5907.
    • (2009) PLoS One , vol.4
    • Vernia, S.1    Rubio, T.2    Heredia, M.3    Rodriguez de Cordoba, S.4    Sanz, P.5
  • 33
    • 1642355290 scopus 로고    scopus 로고
    • The dual-specific protein tyrosine phosphatase family
    • In: Ariño J, & Alexander, D.R., editor, Heidelberg: Springer Berlin
    • Alonso A, Rojas A, Godzik A, Mustelin T (2004) The dual-specific protein tyrosine phosphatase family. In: Ariño J, & Alexander, D.R., editor. Topics in Current Genetics: Protein Phosphatases. Heidelberg: Springer Berlin. 333-358.
    • (2004) Topics in Current Genetics: Protein Phosphatases , pp. 333-358
    • Alonso, A.1    Rojas, A.2    Godzik, A.3    Mustelin, T.4
  • 34
    • 38949123682 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease
    • Pulido R, Hooft van Huijsduijnen R, (2008) Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease. Febs J 275: 848-866.
    • (2008) Febs J , vol.275 , pp. 848-866
    • Pulido, R.1    Hooft van Huijsduijnen, R.2
  • 35
    • 0037169553 scopus 로고    scopus 로고
    • A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen
    • Wang J, Stuckey JA, Wishart MJ, Dixon JE, (2002) A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J Biol Chem 277: 2377-2380.
    • (2002) J Biol Chem , vol.277 , pp. 2377-2380
    • Wang, J.1    Stuckey, J.A.2    Wishart, M.J.3    Dixon, J.E.4
  • 36
    • 0034703182 scopus 로고    scopus 로고
    • Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes
    • Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, et al. (2000) Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum Mol Genet 9: 2251-2261.
    • (2000) Hum Mol Genet , vol.9 , pp. 2251-2261
    • Ganesh, S.1    Agarwala, K.L.2    Ueda, K.3    Akagi, T.4    Shoda, K.5
  • 37
    • 33846025444 scopus 로고    scopus 로고
    • Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling
    • Liu Y, Wang Y, Wu C, Zheng P, (2006) Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling. J Biol Chem 281: 34768-34774.
    • (2006) J Biol Chem , vol.281 , pp. 34768-34774
    • Liu, Y.1    Wang, Y.2    Wu, C.3    Zheng, P.4
  • 38
    • 80052048669 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity
    • Dukhande VV, Rogers DM, Romá-Mateo C, Donderis J, Marina A, et al. (2011) Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity. PLoS One 6: e24040.
    • (2011) PLoS One , vol.6
    • Dukhande, V.V.1    Rogers, D.M.2    Romá-Mateo, C.3    Donderis, J.4    Marina, A.5
  • 39
    • 80052065377 scopus 로고    scopus 로고
    • Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase
    • Romá-Mateo C, Solaz-Fuster Mdel C, Gimeno-Alcaniz JV, Dukhande VV, Donderis J, et al. (2011) Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase. Biochem J 439: 265-275.
    • (2011) Biochem J , vol.439 , pp. 265-275
    • Romá-Mateo, C.1    Solaz-Fuster Mdel, C.2    Gimeno-Alcaniz, J.V.3    Dukhande, V.V.4    Donderis, J.5
  • 41
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl Acids Symp Ser 95-98.
    • (1999) Nucl Acids Symp Ser , pp. 95-98
    • Hall, T.A.1
  • 42
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin
    • Sorimachi K, Le Gal-Coeffet MF, Williamson G, Archer DB, Williamson MP, (1997) Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 5: 647-661.
    • (1997) Structure , vol.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 44
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: a tool for multiple protein sequence and structure alignments
    • Pei J, Kim BH, Grishin NV, (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res 36: 2295-2300.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 45
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 46
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D, (1992) Assessment of protein models with three-dimensional profiles. Nature 356: 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 48
    • 67649760225 scopus 로고    scopus 로고
    • AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex
    • Vernia S, Solaz-Fuster MC, Gimeno-Alcaniz JV, Rubio T, Garcia-Haro L, et al. (2009) AMP-activated protein kinase phosphorylates R5/PTG, the glycogen targeting subunit of the R5/PTG-protein phosphatase 1 holoenzyme, and accelerates its down-regulation by the laforin-malin complex. J Biol Chem 284: 8247-8255.
    • (2009) J Biol Chem , vol.284 , pp. 8247-8255
    • Vernia, S.1    Solaz-Fuster, M.C.2    Gimeno-Alcaniz, J.V.3    Rubio, T.4    Garcia-Haro, L.5
  • 49
    • 34147167177 scopus 로고    scopus 로고
    • Mapping protein-protein interactions for the yeast ABC transporter Ycf1p by integrated split-ubiquitin membrane yeast two-hybrid analysis
    • Paumi CM, Menendez J, Arnoldo A, Engels K, Iyer KR, et al. (2007) Mapping protein-protein interactions for the yeast ABC transporter Ycf1p by integrated split-ubiquitin membrane yeast two-hybrid analysis. Mol Cell 26: 15-25.
    • (2007) Mol Cell , vol.26 , pp. 15-25
    • Paumi, C.M.1    Menendez, J.2    Arnoldo, A.3    Engels, K.4    Iyer, K.R.5
  • 50
    • 0032568542 scopus 로고    scopus 로고
    • Glucose-regulated interaction of a regulatory subunit of protein phosphatase 1 with the Snf1 protein kinase in Saccharomyces cerevisiae
    • Ludin K, Jiang R, Carlson M, (1998) Glucose-regulated interaction of a regulatory subunit of protein phosphatase 1 with the Snf1 protein kinase in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 95: 6245-6250.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6245-6250
    • Ludin, K.1    Jiang, R.2    Carlson, M.3
  • 51
    • 67651244247 scopus 로고    scopus 로고
    • Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism
    • Gentry MS, Pace RM, (2009) Conservation of the glucan phosphatase laforin is linked to rates of molecular evolution and the glucan metabolism of the organism. BMC Evol Biol 9: 138.
    • (2009) BMC Evol Biol , vol.9 , pp. 138
    • Gentry, M.S.1    Pace, R.M.2
  • 52
    • 67649859658 scopus 로고    scopus 로고
    • Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress
    • Liu Y, Wang Y, Wu C, Zheng P, (2009) Deletions and missense mutations of EPM2A exacerbate unfolded protein response and apoptosis of neuronal cells induced by endoplasm reticulum stress. Hum Mol Genet 18: 2622-2631.
    • (2009) Hum Mol Genet , vol.18 , pp. 2622-2631
    • Liu, Y.1    Wang, Y.2    Wu, C.3    Zheng, P.4
  • 53
    • 69449083006 scopus 로고    scopus 로고
    • The carbohydrate-binding module family 20-diversity, structure, and function
    • Christiansen C, Abou Hachem M, Janecek S, Vikso-Nielsen A, Blennow A, et al. (2009) The carbohydrate-binding module family 20-diversity, structure, and function. Febs J 276: 5006-5029.
    • (2009) Febs J , vol.276 , pp. 5006-5029
    • Christiansen, C.1    Abou Hachem, M.2    Janecek, S.3    Vikso-Nielsen, A.4    Blennow, A.5
  • 54
    • 80052048669 scopus 로고    scopus 로고
    • Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity
    • Dukhande VV, Rogers DM, Romá-Mateo C, Donderis J, Marina A, et al. (2011) Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activity. PLoS One 6: e24040.
    • (2011) PLoS One , vol.6
    • Dukhande, V.V.1    Rogers, D.M.2    Romá-Mateo, C.3    Donderis, J.4    Marina, A.5
  • 55
    • 84873334806 scopus 로고    scopus 로고
    • A malachite green-based assay to assess glucan phosphatase activity
    • Sherwood AR, Paasch BC, Worby CA, Gentry MS, (2013) A malachite green-based assay to assess glucan phosphatase activity. Anal Biochem 435: 54-56.
    • (2013) Anal Biochem , vol.435 , pp. 54-56
    • Sherwood, A.R.1    Paasch, B.C.2    Worby, C.A.3    Gentry, M.S.4
  • 56
    • 28844443837 scopus 로고    scopus 로고
    • Is this protein ubiquitinated?
    • Kaiser P, Tagwerker C, (2005) Is this protein ubiquitinated? Methods Enzymol 399: 243-248.
    • (2005) Methods Enzymol , vol.399 , pp. 243-248
    • Kaiser, P.1    Tagwerker, C.2
  • 57
    • 79954592899 scopus 로고    scopus 로고
    • Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701
    • Koksal AC, Cingolani G, (2011) Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701. J Biol Chem 286: 14373-14382.
    • (2011) J Biol Chem , vol.286 , pp. 14373-14382
    • Koksal, A.C.1    Cingolani, G.2


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