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Volumn 12, Issue 5, 2013, Pages 2101-2115

Erratum: Drafting the CLN3 protein interactome in SH-SY5Y human neuroblastoma cells: A label-free quantitative proteomics approach (Journal of Proteome Research (2013) 12:5 (2101-2115) DOI: 10.1021/pr301125k);Drafting the CLN3 protein interactome in SH-SY5Y human neuroblastoma cells: A label-free quantitative proteomics approach

Author keywords

CLN3 disease; co immunoprecipitation; interactome; mass spectrometry; neuronal ceroid lipofuscinoses; tandem affinity purification

Indexed keywords

PROTEIN CLN3; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84877128732     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr4005212     Document Type: Erratum
Times cited : (43)

References (87)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. The cell as a collection of protein machines: preparing the next generation of molecular biologists Cell 1998, 92 (3) 291-4
    • (1998) Cell , vol.92 , Issue.3 , pp. 291-294
    • Alberts, B.1
  • 4
    • 14844314804 scopus 로고    scopus 로고
    • Advances in protein complex analysis using mass spectrometry
    • Gingras, A. C.; Aebersold, R.; Raught, B. Advances in protein complex analysis using mass spectrometry J. Physiol. 2005, 563 (Pt 1) 11-21
    • (2005) J. Physiol. , vol.563 , Issue.PART 1 , pp. 11-21
    • Gingras, A.C.1    Aebersold, R.2    Raught, B.3
  • 8
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C.; Sowa, M. E.; Gygi, S. P.; Harper, J. W. Network organization of the human autophagy system Nature 2010, 466 (7302) 68-76
    • (2010) Nature , vol.466 , Issue.7302 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 10
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E.; Bennett, E. J.; Gygi, S. P.; Harper, J. W. Defining the human deubiquitinating enzyme interaction landscape Cell 2009, 138 (2) 389-403
    • (2009) Cell , vol.138 , Issue.2 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 12
    • 2442438994 scopus 로고    scopus 로고
    • Tandem immunoaffinity purification of protein complexes from Caenorhabditis elegans
    • Polanowska, J.; Martin, J. S.; Fisher, R.; Scopa, T.; Rae, I.; Boulton, S. J. Tandem immunoaffinity purification of protein complexes from Caenorhabditis elegans Biotechniques 2004, 36 (5) 778-80
    • (2004) Biotechniques , vol.36 , Issue.5 , pp. 778-780
    • Polanowska, J.1    Martin, J.S.2    Fisher, R.3    Scopa, T.4    Rae, I.5    Boulton, S.J.6
  • 16
    • 46749110040 scopus 로고    scopus 로고
    • Mapping the human protein interactome
    • Figeys, D. Mapping the human protein interactome Cell Res. 2008, 18 (7) 716-24
    • (2008) Cell Res. , vol.18 , Issue.7 , pp. 716-724
    • Figeys, D.1
  • 18
    • 34548418142 scopus 로고    scopus 로고
    • Methods for the detection and analysis of protein-protein interactions
    • Berggard, T.; Linse, S.; James, P. Methods for the detection and analysis of protein-protein interactions Proteomics 2007, 7 (16) 2833-42
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2833-2842
    • Berggard, T.1    Linse, S.2    James, P.3
  • 21
    • 33750986182 scopus 로고    scopus 로고
    • The neuronal ceroid-lipofuscinoses: From past to present
    • Haltia, M. The neuronal ceroid-lipofuscinoses: from past to present Biochim. Biophys. Acta 2006, 1762 (10) 850-6
    • (2006) Biochim. Biophys. Acta , vol.1762 , Issue.10 , pp. 850-856
    • Haltia, M.1
  • 22
    • 0030738272 scopus 로고    scopus 로고
    • Neuronal ceroid lipofuscinoses in Scandinavia. Epidemiology and clinical pictures
    • Uvebrant, P.; Hagberg, B. Neuronal ceroid lipofuscinoses in Scandinavia. Epidemiology and clinical pictures Neuropediatrics 1997, 28 (1) 6-8
    • (1997) Neuropediatrics , vol.28 , Issue.1 , pp. 6-8
    • Uvebrant, P.1    Hagberg, B.2
  • 23
    • 0029147298 scopus 로고
    • Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium
    • Consortium, B. D. Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium Cell 1995, 82 (6) 949-57
    • (1995) Cell , vol.82 , Issue.6 , pp. 949-957
    • Consortium, B.D.1
  • 24
    • 0034772310 scopus 로고    scopus 로고
    • CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: New clues to Batten disease
    • Luiro, K.; Kopra, O.; Lehtovirta, M.; Jalanko, A. CLN3 protein is targeted to neuronal synapses but excluded from synaptic vesicles: new clues to Batten disease Hum. Mol. Genet. 2001, 10 (19) 2123-31
    • (2001) Hum. Mol. Genet. , vol.10 , Issue.19 , pp. 2123-2131
    • Luiro, K.1    Kopra, O.2    Lehtovirta, M.3    Jalanko, A.4
  • 25
    • 33745976466 scopus 로고    scopus 로고
    • Autophagy is disrupted in a knock-in mouse model of juvenile neuronal ceroid lipofuscinosis
    • Cao, Y.; Espinola, J. A.; Fossale, E.; Massey, A. C.; Cuervo, A. M.; MacDonald, M. E.; Cotman, S. L. Autophagy is disrupted in a knock-in mouse model of juvenile neuronal ceroid lipofuscinosis J. Biol. Chem. 2006, 281 (29) 20483-93
    • (2006) J. Biol. Chem. , vol.281 , Issue.29 , pp. 20483-20493
    • Cao, Y.1    Espinola, J.A.2    Fossale, E.3    Massey, A.C.4    Cuervo, A.M.5    MacDonald, M.E.6    Cotman, S.L.7
  • 26
    • 33847281052 scopus 로고    scopus 로고
    • Neuronal vulnerability of CLN3 deletion to calcium-induced cytotoxicity is mediated by calsenilin
    • Chang, J. W.; Choi, H.; Kim, H. J.; Jo, D. G.; Jeon, Y. J.; Noh, J. Y.; Park, W. J.; Jung, Y. K. Neuronal vulnerability of CLN3 deletion to calcium-induced cytotoxicity is mediated by calsenilin Hum. Mol. Genet. 2007, 16 (3) 317-26
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.3 , pp. 317-326
    • Chang, J.W.1    Choi, H.2    Kim, H.J.3    Jo, D.G.4    Jeon, Y.J.5    Noh, J.Y.6    Park, W.J.7    Jung, Y.K.8
  • 27
    • 66849138215 scopus 로고    scopus 로고
    • S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p
    • Codlin, S.; Mole, S. E. S. pombe btn1, the orthologue of the Batten disease gene CLN3, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p J. Cell Sci. 2009, 122 (Pt 8) 1163-73
    • (2009) J. Cell Sci. , vol.122 , Issue.PART 8 , pp. 1163-1173
    • Codlin, S.1    Mole, S.E.2
  • 28
    • 78449274362 scopus 로고    scopus 로고
    • A novel interaction of CLN3 with nonmuscle myosin-IIB and defects in cell motility of Cln3(-/-) cells
    • Getty, A. L.; Benedict, J. W.; Pearce, D. A. A novel interaction of CLN3 with nonmuscle myosin-IIB and defects in cell motility of Cln3(-/-) cells Exp. Cell Res. 2011, 317 (1) 51-69
    • (2011) Exp. Cell Res. , vol.317 , Issue.1 , pp. 51-69
    • Getty, A.L.1    Benedict, J.W.2    Pearce, D.A.3
  • 29
    • 0033864041 scopus 로고    scopus 로고
    • CLN3 protein regulates lysosomal pH and alters intracellular processing of Alzheimer's amyloid-beta protein precursor and cathepsin D in human cells
    • Golabek, A. A.; Kida, E.; Walus, M.; Kaczmarski, W.; Michalewski, M.; Wisniewski, K. E. CLN3 protein regulates lysosomal pH and alters intracellular processing of Alzheimer's amyloid-beta protein precursor and cathepsin D in human cells Mol. Genet. Metab. 2000, 70 (3) 203-13
    • (2000) Mol. Genet. Metab. , vol.70 , Issue.3 , pp. 203-213
    • Golabek, A.A.1    Kida, E.2    Walus, M.3    Kaczmarski, W.4    Michalewski, M.5    Wisniewski, K.E.6
  • 30
    • 34248200079 scopus 로고    scopus 로고
    • A novel role of the Batten disease gene CLN3: Association with BMP synthesis
    • Hobert, J. A.; Dawson, G. A novel role of the Batten disease gene CLN3: association with BMP synthesis Biochem. Biophys. Res. Commun. 2007, 358 (1) 111-6
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , Issue.1 , pp. 111-116
    • Hobert, J.A.1    Dawson, G.2
  • 31
    • 80155138564 scopus 로고    scopus 로고
    • The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly
    • Kama, R.; Kanneganti, V.; Ungermann, C.; Gerst, J. E. The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly J. Cell Biol. 2011, 195 (2) 203-15
    • (2011) J. Cell Biol. , vol.195 , Issue.2 , pp. 203-215
    • Kama, R.1    Kanneganti, V.2    Ungermann, C.3    Gerst, J.E.4
  • 32
    • 0347364649 scopus 로고    scopus 로고
    • A role in vacuolar arginine transport for yeast Btn1p and for human CLN3, the protein defective in Batten disease
    • Kim, Y.; Ramirez-Montealegre, D.; Pearce, D. A. A role in vacuolar arginine transport for yeast Btn1p and for human CLN3, the protein defective in Batten disease Proc. Natl. Acad. Sci. U.S.A. 2003, 100 (26) 15458-62
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.26 , pp. 15458-15462
    • Kim, Y.1    Ramirez-Montealegre, D.2    Pearce, D.A.3
  • 33
    • 9744254471 scopus 로고    scopus 로고
    • Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway
    • Luiro, K.; Yliannala, K.; Ahtiainen, L.; Maunu, H.; Jarvela, I.; Kyttala, A.; Jalanko, A. Interconnections of CLN3, Hook1 and Rab proteins link Batten disease to defects in the endocytic pathway Hum. Mol. Genet. 2004, 13 (23) 3017-27
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.23 , pp. 3017-3027
    • Luiro, K.1    Yliannala, K.2    Ahtiainen, L.3    Maunu, H.4    Jarvela, I.5    Kyttala, A.6    Jalanko, A.7
  • 34
    • 53849117085 scopus 로고    scopus 로고
    • Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor
    • Metcalf, D. J.; Calvi, A. A.; Seaman, M.; Mitchison, H. M.; Cutler, D. F. Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor Traffic 2008, 9 (11) 1905-14
    • (2008) Traffic , vol.9 , Issue.11 , pp. 1905-1914
    • Metcalf, D.J.1    Calvi, A.A.2    Seaman, M.3    Mitchison, H.M.4    Cutler, D.F.5
  • 35
    • 33845293272 scopus 로고    scopus 로고
    • CLN3P, the Batten's disease protein, is a novel palmitoyl-protein Delta-9 desaturase
    • Narayan, S. B.; Rakheja, D.; Tan, L.; Pastor, J. V.; Bennett, M. J. CLN3P, the Batten's disease protein, is a novel palmitoyl-protein Delta-9 desaturase Ann. Neurol. 2006, 60 (5) 570-7
    • (2006) Ann. Neurol. , vol.60 , Issue.5 , pp. 570-577
    • Narayan, S.B.1    Rakheja, D.2    Tan, L.3    Pastor, J.V.4    Bennett, M.J.5
  • 36
    • 33744530432 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity to regulate pH imbalance in the vacuole
    • Padilla-Lopez, S.; Pearce, D. A. Saccharomyces cerevisiae lacking Btn1p modulate vacuolar ATPase activity to regulate pH imbalance in the vacuole J. Biol. Chem. 2006, 281 (15) 10273-80
    • (2006) J. Biol. Chem. , vol.281 , Issue.15 , pp. 10273-10280
    • Padilla-Lopez, S.1    Pearce, D.A.2
  • 37
    • 28744438595 scopus 로고    scopus 로고
    • Defective lysosomal arginine transport in juvenile Batten disease
    • Ramirez-Montealegre, D.; Pearce, D. A. Defective lysosomal arginine transport in juvenile Batten disease Hum. Mol. Genet. 2005, 14 (23) 3759-73
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.23 , pp. 3759-3773
    • Ramirez-Montealegre, D.1    Pearce, D.A.2
  • 38
    • 45849149313 scopus 로고    scopus 로고
    • CLN3p impacts galactosylceramide transport, raft morphology, and lipid content
    • Rusyn, E.; Mousallem, T.; Persaud-Sawin, D. A.; Miller, S.; Boustany, R. M. CLN3p impacts galactosylceramide transport, raft morphology, and lipid content Pediatr. Res. 2008, 63 (6) 625-31
    • (2008) Pediatr. Res. , vol.63 , Issue.6 , pp. 625-631
    • Rusyn, E.1    Mousallem, T.2    Persaud-Sawin, D.A.3    Miller, S.4    Boustany, R.M.5
  • 39
    • 58949100352 scopus 로고    scopus 로고
    • Interactions between the juvenile Batten disease gene, CLN3, and the Notch and JNK signalling pathways
    • Tuxworth, R. I.; Vivancos, V.; O'Hare, M. B.; Tear, G. Interactions between the juvenile Batten disease gene, CLN3, and the Notch and JNK signalling pathways Hum. Mol. Genet. 2009, 18 (4) 667-78
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.4 , pp. 667-678
    • Tuxworth, R.I.1    Vivancos, V.2    O'Hare, M.B.3    Tear, G.4
  • 40
    • 50249168346 scopus 로고    scopus 로고
    • Novel interactions of CLN3 protein link Batten disease to dysregulation of fodrin-Na+, K+ ATPase complex
    • Uusi-Rauva, K.; Luiro, K.; Tanhuanpaa, K.; Kopra, O.; Martin-Vasallo, P.; Kyttala, A.; Jalanko, A. Novel interactions of CLN3 protein link Batten disease to dysregulation of fodrin-Na+, K+ ATPase complex Exp. Cell Res. 2008, 314 (15) 2895-905
    • (2008) Exp. Cell Res. , vol.314 , Issue.15 , pp. 2895-2905
    • Uusi-Rauva, K.1    Luiro, K.2    Tanhuanpaa, K.3    Kopra, O.4    Martin-Vasallo, P.5    Kyttala, A.6    Jalanko, A.7
  • 41
    • 84862838085 scopus 로고    scopus 로고
    • Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments
    • Uusi-Rauva, K.; Kyttala, A.; van der Kant, R.; Vesa, J.; Tanhuanpaa, K.; Neefjes, J.; Olkkonen, V. M.; Jalanko, A. Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments Cell. Mol. Life Sci. 2012, 69 (12) 2075-89
    • (2012) Cell. Mol. Life Sci. , vol.69 , Issue.12 , pp. 2075-2089
    • Uusi-Rauva, K.1    Kyttala, A.2    Van Der Kant, R.3    Vesa, J.4    Tanhuanpaa, K.5    Neefjes, J.6    Olkkonen, V.M.7    Jalanko, A.8
  • 42
    • 77950536687 scopus 로고    scopus 로고
    • Interaction between Sdo1p and Btn1p in the Saccharomyces cerevisiae model for Batten disease
    • Vitiello, S. P.; Benedict, J. W.; Padilla-Lopez, S.; Pearce, D. A. Interaction between Sdo1p and Btn1p in the Saccharomyces cerevisiae model for Batten disease Hum. Mol. Genet. 2010, 19 (5) 931-42
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.5 , pp. 931-942
    • Vitiello, S.P.1    Benedict, J.W.2    Padilla-Lopez, S.3    Pearce, D.A.4
  • 43
    • 0030038060 scopus 로고    scopus 로고
    • Apoptosis as the mechanism of neurodegeneration in Batten's disease
    • Lane, S. C.; Jolly, R. D.; Schmechel, D. E.; Alroy, J.; Boustany, R. M. Apoptosis as the mechanism of neurodegeneration in Batten's disease J. Neurochem. 1996, 67 (2) 677-83
    • (1996) J. Neurochem. , vol.67 , Issue.2 , pp. 677-683
    • Lane, S.C.1    Jolly, R.D.2    Schmechel, D.E.3    Alroy, J.4    Boustany, R.M.5
  • 46
    • 79953713220 scopus 로고    scopus 로고
    • Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5
    • Skarra, D. V.; Goudreault, M.; Choi, H.; Mullin, M.; Nesvizhskii, A. I.; Gingras, A. C.; Honkanen, R. E. Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5 Proteomics 2011, 11 (8) 1508-16
    • (2011) Proteomics , vol.11 , Issue.8 , pp. 1508-1516
    • Skarra, D.V.1    Goudreault, M.2    Choi, H.3    Mullin, M.4    Nesvizhskii, A.I.5    Gingras, A.C.6    Honkanen, R.E.7
  • 47
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da, W.; Sherman, B. T.; Lempicki, R. A. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources Nat. Protoc. 2009, 4 (1) 44-57
    • (2009) Nat. Protoc. , vol.4 , Issue.1 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 49
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge, R. B.; Tang, P.; Hsia, H. C.; Leong, P. M.; Miller, J. H.; Calos, M. P. Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system Mol. Cell. Biol. 1987, 7 (1) 379-87
    • (1987) Mol. Cell. Biol. , vol.7 , Issue.1 , pp. 379-387
    • Dubridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5    Calos, M.P.6
  • 50
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear, W. S.; Nolan, G. P.; Scott, M. L.; Baltimore, D. Production of high-titer helper-free retroviruses by transient transfection Proc. Natl. Acad. Sci. U.S.A. 1993, 90 (18) 8392-6
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , Issue.18 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 51
    • 0030922804 scopus 로고    scopus 로고
    • Noninfectious virus-like particles produced by Moloney murine leukemia virus-based retrovirus packaging cells deficient in viral envelope become infectious in the presence of lipofection reagents
    • Sharma, S.; Murai, F.; Miyanohara, A.; Friedmann, T. Noninfectious virus-like particles produced by Moloney murine leukemia virus-based retrovirus packaging cells deficient in viral envelope become infectious in the presence of lipofection reagents Proc. Natl. Acad. Sci. U.S.A. 1997, 94 (20) 10803-8
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.20 , pp. 10803-10808
    • Sharma, S.1    Murai, F.2    Miyanohara, A.3    Friedmann, T.4
  • 52
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L.; Blomer, U.; Gallay, P.; Ory, D.; Mulligan, R.; Gage, F. H.; Verma, I. M.; Trono, D. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector Science 1996, 272 (5259) 263-7
    • (1996) Science , vol.272 , Issue.5259 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 53
    • 77149164096 scopus 로고    scopus 로고
    • The neuronal ceroid lipofuscinosis protein CLN5: New insights into cellular maturation, transport, and consequences of mutations
    • Schmiedt, M. L.; Bessa, C.; Heine, C.; Ribeiro, M. G.; Jalanko, A.; Kyttala, A. The neuronal ceroid lipofuscinosis protein CLN5: new insights into cellular maturation, transport, and consequences of mutations Hum. Mutat. 2010, 31 (3) 356-65
    • (2010) Hum. Mutat. , vol.31 , Issue.3 , pp. 356-365
    • Schmiedt, M.L.1    Bessa, C.2    Heine, C.3    Ribeiro, M.G.4    Jalanko, A.5    Kyttala, A.6
  • 55
    • 0344011621 scopus 로고    scopus 로고
    • Characterization of Cln3p, the gene product responsible for juvenile neuronal ceroid lipofuscinosis, as a lysosomal integral membrane glycoprotein
    • Ezaki, J.; Takeda-Ezaki, M.; Koike, M.; Ohsawa, Y.; Taka, H.; Mineki, R.; Murayama, K.; Uchiyama, Y.; Ueno, T.; Kominami, E. Characterization of Cln3p, the gene product responsible for juvenile neuronal ceroid lipofuscinosis, as a lysosomal integral membrane glycoprotein J. Neurochem. 2003, 87 (5) 1296-308
    • (2003) J. Neurochem. , vol.87 , Issue.5 , pp. 1296-1308
    • Ezaki, J.1    Takeda-Ezaki, M.2    Koike, M.3    Ohsawa, Y.4    Taka, H.5    Mineki, R.6    Murayama, K.7    Uchiyama, Y.8    Ueno, T.9    Kominami, E.10
  • 56
    • 0032811446 scopus 로고    scopus 로고
    • Expression studies of CLN3 protein (battenin) in fusion with the green fluorescent protein in mammalian cells in vitro
    • Golabek, A. A.; Kaczmarski, W.; Kida, E.; Kaczmarski, A.; Michalewski, M. P.; Wisniewski, K. E. Expression studies of CLN3 protein (battenin) in fusion with the green fluorescent protein in mammalian cells in vitro Mol. Genet. Metab. 1999, 66 (4) 277-82
    • (1999) Mol. Genet. Metab. , vol.66 , Issue.4 , pp. 277-282
    • Golabek, A.A.1    Kaczmarski, W.2    Kida, E.3    Kaczmarski, A.4    Michalewski, M.P.5    Wisniewski, K.E.6
  • 57
    • 79953311668 scopus 로고    scopus 로고
    • Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells
    • 002642
    • Vandamme, J.; Volkel, P.; Rosnoblet, C.; Le Faou, P.; Angrand, P. O. Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells Mol. Cell. Proteomics 2011, 10 (4) M110 002642
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.4 , pp. 110
    • Vandamme, J.1    Volkel, P.2    Rosnoblet, C.3    Le Faou, P.4    Angrand, P.O.5
  • 58
    • 84864603831 scopus 로고    scopus 로고
    • Interactome of the amyloid precursor protein APP in brain reveals a protein network involved in synaptic vesicle turnover and a close association with Synaptotagmin-1
    • Kohli, B. M.; Pflieger, D.; Mueller, L. N.; Carbonetti, G.; Aebersold, R.; Nitsch, R. M.; Konietzko, U. Interactome of the amyloid precursor protein APP in brain reveals a protein network involved in synaptic vesicle turnover and a close association with Synaptotagmin-1 J. Proteome Res. 2012, 11 (8) 4075-90
    • (2012) J. Proteome Res. , vol.11 , Issue.8 , pp. 4075-4090
    • Kohli, B.M.1    Pflieger, D.2    Mueller, L.N.3    Carbonetti, G.4    Aebersold, R.5    Nitsch, R.M.6    Konietzko, U.7
  • 64
    • 78650679916 scopus 로고    scopus 로고
    • Screening for calcium channel modulators in CLN3 siRNA knock down SH-SY5Y neuroblastoma cells reveals a significant decrease of intracellular calcium levels by selected L-type calcium channel blockers
    • An Haack, K.; Narayan, S. B.; Li, H.; Warnock, A.; Tan, L.; Bennett, M. J. Screening for calcium channel modulators in CLN3 siRNA knock down SH-SY5Y neuroblastoma cells reveals a significant decrease of intracellular calcium levels by selected L-type calcium channel blockers Biochim. Biophys. Acta 2011, 1810 (2) 186-91
    • (2011) Biochim. Biophys. Acta , vol.1810 , Issue.2 , pp. 186-191
    • An Haack, K.1    Narayan, S.B.2    Li, H.3    Warnock, A.4    Tan, L.5    Bennett, M.J.6
  • 65
    • 33646419529 scopus 로고    scopus 로고
    • Over-expression of CLN3P, the Batten disease protein, inhibits PANDER-induced apoptosis in neuroblastoma cells: Further evidence that CLN3P has anti-apoptotic properties
    • Narayan, S. B.; Rakheja, D.; Pastor, J. V.; Rosenblatt, K.; Greene, S. R.; Yang, J.; Wolf, B. A.; Bennett, M. J. Over-expression of CLN3P, the Batten disease protein, inhibits PANDER-induced apoptosis in neuroblastoma cells: further evidence that CLN3P has anti-apoptotic properties Mol. Genet. Metab. 2006, 88 (2) 178-83
    • (2006) Mol. Genet. Metab. , vol.88 , Issue.2 , pp. 178-183
    • Narayan, S.B.1    Rakheja, D.2    Pastor, J.V.3    Rosenblatt, K.4    Greene, S.R.5    Yang, J.6    Wolf, B.A.7    Bennett, M.J.8
  • 66
    • 0035826756 scopus 로고    scopus 로고
    • A favorable response to antiparkinsonian treatment in juvenile neuronal ceroid lipofuscinosis
    • Aberg, L. E.; Rinne, J. O.; Rajantie, I.; Santavuori, P. A favorable response to antiparkinsonian treatment in juvenile neuronal ceroid lipofuscinosis Neurology 2001, 56 (9) 1236-9
    • (2001) Neurology , vol.56 , Issue.9 , pp. 1236-1239
    • Aberg, L.E.1    Rinne, J.O.2    Rajantie, I.3    Santavuori, P.4
  • 72
    • 46349088952 scopus 로고    scopus 로고
    • Diseases caused by defects of mitochondrial carriers: A review
    • Palmieri, F. Diseases caused by defects of mitochondrial carriers: a review Biochim. Biophys. Acta 2008, 1777 (7-8) 564-78
    • (2008) Biochim. Biophys. Acta , vol.1777 , Issue.78 , pp. 564-578
    • Palmieri, F.1
  • 74
    • 79551626607 scopus 로고    scopus 로고
    • Lithium rescues the impaired autophagy process in CbCln3(Deltaex7/8/ Deltaex7/8) cerebellar cells and reduces neuronal vulnerability to cell death via IMPase inhibition
    • Chang, J. W.; Choi, H.; Cotman, S. L.; Jung, Y. K. Lithium rescues the impaired autophagy process in CbCln3(Deltaex7/8/Deltaex7/8) cerebellar cells and reduces neuronal vulnerability to cell death via IMPase inhibition J. Neurochem. 2011, 116 (4) 659-68
    • (2011) J. Neurochem. , vol.116 , Issue.4 , pp. 659-668
    • Chang, J.W.1    Choi, H.2    Cotman, S.L.3    Jung, Y.K.4
  • 75
    • 84862578734 scopus 로고    scopus 로고
    • Synaptic polarity depends on phosphatidylinositol signaling regulated by myo-inositol monophosphatase in Caenorhabditis elegans
    • Kimata, T.; Tanizawa, Y.; Can, Y.; Ikeda, S.; Kuhara, A.; Mori, I. Synaptic polarity depends on phosphatidylinositol signaling regulated by myo-inositol monophosphatase in Caenorhabditis elegans Genetics 2012, 191 (2) 509-21
    • (2012) Genetics , vol.191 , Issue.2 , pp. 509-521
    • Kimata, T.1    Tanizawa, Y.2    Can, Y.3    Ikeda, S.4    Kuhara, A.5    Mori, I.6
  • 76
    • 0034625329 scopus 로고    scopus 로고
    • B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts
    • Courilleau, D.; Chastre, E.; Sabbah, M.; Redeuilh, G.; Atfi, A.; Mester, J. B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts J. Biol. Chem. 2000, 275 (23) 17344-8
    • (2000) J. Biol. Chem. , vol.275 , Issue.23 , pp. 17344-17348
    • Courilleau, D.1    Chastre, E.2    Sabbah, M.3    Redeuilh, G.4    Atfi, A.5    Mester, J.6
  • 77
    • 45549086681 scopus 로고    scopus 로고
    • Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis
    • Ikeda, M.; Kanao, Y.; Yamanaka, M.; Sakuraba, H.; Mizutani, Y.; Igarashi, Y.; Kihara, A. Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis FEBS Lett. 2008, 582 (16) 2435-40
    • (2008) FEBS Lett. , vol.582 , Issue.16 , pp. 2435-2440
    • Ikeda, M.1    Kanao, Y.2    Yamanaka, M.3    Sakuraba, H.4    Mizutani, Y.5    Igarashi, Y.6    Kihara, A.7
  • 79
    • 71949103162 scopus 로고    scopus 로고
    • Novel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteins
    • Lyly, A.; von Schantz, C.; Heine, C.; Schmiedt, M. L.; Sipila, T.; Jalanko, A.; Kyttala, A. Novel interactions of CLN5 support molecular networking between Neuronal Ceroid Lipofuscinosis proteins BMC Cell Biol. 2009, 10, 83
    • (2009) BMC Cell Biol. , vol.10 , pp. 83
    • Lyly, A.1    Von Schantz, C.2    Heine, C.3    Schmiedt, M.L.4    Sipila, T.5    Jalanko, A.6    Kyttala, A.7
  • 84
    • 8744251345 scopus 로고    scopus 로고
    • Hippocampal pathology in the human neuronal ceroid-lipofuscinoses: Distinct patterns of storage deposition, neurodegeneration and glial activation
    • Tyynela, J.; Cooper, J. D.; Khan, M. N.; Shemilts, S. J.; Haltia, M. Hippocampal pathology in the human neuronal ceroid-lipofuscinoses: distinct patterns of storage deposition, neurodegeneration and glial activation Brain Pathol. 2004, 14 (4) 349-357
    • (2004) Brain Pathol. , vol.14 , Issue.4 , pp. 349-357
    • Tyynela, J.1    Cooper, J.D.2    Khan, M.N.3    Shemilts, S.J.4    Haltia, M.5
  • 85
    • 67249116116 scopus 로고    scopus 로고
    • Cln6 mutants associated with neuronal ceroid lipofuscinosis are degraded in a proteasome-dependent manner
    • Oresic, K.; Mueller, B.; Tortorella, D. Cln6 mutants associated with neuronal ceroid lipofuscinosis are degraded in a proteasome-dependent manner Biosci. Rep. 2009, 29 (3) 173-81
    • (2009) Biosci. Rep. , vol.29 , Issue.3 , pp. 173-181
    • Oresic, K.1    Mueller, B.2    Tortorella, D.3
  • 87
    • 84875216538 scopus 로고    scopus 로고
    • PrePPI: A structure-informed database of protein-protein interactions
    • Zhang, Q. C.; Petrey, D.; Garzon, J. I.; Deng, L.; Honig, B. PrePPI: a structure-informed database of protein-protein interactions Nucleic Acids Res. 2013, 41 (D1) D828-33
    • (2013) Nucleic Acids Res. , vol.41 , Issue.D1 , pp. 828-833
    • Zhang, Q.C.1    Petrey, D.2    Garzon, J.I.3    Deng, L.4    Honig, B.5


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