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Volumn 1852, Issue 9, 2015, Pages 1950-1959

SUMOylation of the brain-predominant Ataxin-3 isoform modulates its interaction with p97

Author keywords

Amyloid; Polyglutamine; Posttranslational modification; Protein aggregation; Surface plasmon resonance

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMYLOID; ATAXIN 3; LYSINE; POLYGLUTAMINE; PROTEIN P97; SUMO 1 PROTEIN; SUMO 2 PROTEIN; UBIQUITIN;

EID: 84955513053     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2015.06.010     Document Type: Article
Times cited : (32)

References (66)
  • 1
    • 79960668226 scopus 로고    scopus 로고
    • Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease
    • Matos C.A., de Macedo-Ribeiro S., Carvalho A.L. Polyglutamine diseases: the special case of ataxin-3 and Machado-Joseph disease. Prog. Neurobiol. 2011, 95:26-48.
    • (2011) Prog. Neurobiol. , vol.95 , pp. 26-48
    • Matos, C.A.1    de Macedo-Ribeiro, S.2    Carvalho, A.L.3
  • 4
    • 0032735135 scopus 로고    scopus 로고
    • Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix
    • Perez M.K., Paulson H.L., Pittman R.N. Ataxin-3 with an altered conformation that exposes the polyglutamine domain is associated with the nuclear matrix. Hum. Mol. Genet. 1999, 8:2377-2385.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2377-2385
    • Perez, M.K.1    Paulson, H.L.2    Pittman, R.N.3
  • 5
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett B., Li F., Pittman R.N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet. 2003, 12:3195-3205.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 6
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • Doss-Pepe E.W., Stenroos E.S., Johnson W.G., Madura K. Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. Mol. Cell. Biol. 2003, 23:6469-6483.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 7
    • 33747891213 scopus 로고    scopus 로고
    • Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates
    • Zhong X., Pittman R.N. Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates. Hum. Mol. Genet. 2006, 15:2409-2420.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2409-2420
    • Zhong, X.1    Pittman, R.N.2
  • 8
    • 33750962224 scopus 로고    scopus 로고
    • Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation
    • Evert B.O., Araujo J., Vieira-Saecker A.M., de Vos R.A., Harendza S., Klockgether T., Wullner U. Ataxin-3 represses transcription via chromatin binding, interaction with histone deacetylase 3, and histone deacetylation. J. Neurosci. 2006, 26:11474-11486.
    • (2006) J. Neurosci. , vol.26 , pp. 11474-11486
    • Evert, B.O.1    Araujo, J.2    Vieira-Saecker, A.M.3    de Vos, R.A.4    Harendza, S.5    Klockgether, T.6    Wullner, U.7
  • 11
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils
    • Bevivino A.E., Loll P.J. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:11955-11960.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 12
    • 0042357191 scopus 로고    scopus 로고
    • Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature
    • Marchal S., Shehi E., Harricane M.C., Fusi P., Heitz F., Tortora P., Lange R. Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature. J. Biol. Chem. 2003, 278:31554-31563.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31554-31563
    • Marchal, S.1    Shehi, E.2    Harricane, M.C.3    Fusi, P.4    Heitz, F.5    Tortora, P.6    Lange, R.7
  • 13
    • 0345118103 scopus 로고    scopus 로고
    • Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease
    • Chow M.K., Paulson H.L., Bottomley S.P. Destabilization of a non-pathological variant of ataxin-3 results in fibrillogenesis via a partially folded intermediate: a model for misfolding in polyglutamine disease. J. Mol. Biol. 2004, 335:333-341.
    • (2004) J. Mol. Biol. , vol.335 , pp. 333-341
    • Chow, M.K.1    Paulson, H.L.2    Bottomley, S.P.3
  • 14
    • 8544260320 scopus 로고    scopus 로고
    • Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3
    • Masino L., Nicastro G., Menon R.P., Dal Piaz F., Calder L., Pastore A. Characterization of the structure and the amyloidogenic properties of the Josephin domain of the polyglutamine-containing protein ataxin-3. J. Mol. Biol. 2004, 344:1021-1035.
    • (2004) J. Mol. Biol. , vol.344 , pp. 1021-1035
    • Masino, L.1    Nicastro, G.2    Menon, R.P.3    Dal Piaz, F.4    Calder, L.5    Pastore, A.6
  • 15
    • 26244434741 scopus 로고    scopus 로고
    • Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3
    • Gales L., Cortes L., Almeida C., Melo C.V., Costa M.C., Maciel P., Clarke D.T., Damas A.M., Macedo-Ribeiro S. Towards a structural understanding of the fibrillization pathway in Machado-Joseph's disease: trapping early oligomers of non-expanded ataxin-3. J. Mol. Biol. 2005, 353:642-654.
    • (2005) J. Mol. Biol. , vol.353 , pp. 642-654
    • Gales, L.1    Cortes, L.2    Almeida, C.3    Melo, C.V.4    Costa, M.C.5    Maciel, P.6    Clarke, D.T.7    Damas, A.M.8    Macedo-Ribeiro, S.9
  • 16
    • 77955647254 scopus 로고    scopus 로고
    • Towards the treatment of polyglutamine diseases: the modulatory role of protein context
    • Robertson A.L., Bottomley S.P. Towards the treatment of polyglutamine diseases: the modulatory role of protein context. Curr. Med. Chem. 2010, 17:3058-3068.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 3058-3068
    • Robertson, A.L.1    Bottomley, S.P.2
  • 18
    • 84857033477 scopus 로고    scopus 로고
    • The two faces of Janus: functional interactions and protein aggregation
    • Pastore A., Temussi P.A. The two faces of Janus: functional interactions and protein aggregation. Curr. Opin. Struct. Biol. 2012, 22:30-37.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 30-37
    • Pastore, A.1    Temussi, P.A.2
  • 19
    • 84861943506 scopus 로고    scopus 로고
    • Cell biology of spinocerebellar ataxia
    • Orr H.T. Cell biology of spinocerebellar ataxia. J. Cell Biol. 2012, 197:167-177.
    • (2012) J. Cell Biol. , vol.197 , pp. 167-177
    • Orr, H.T.1
  • 21
    • 84861538096 scopus 로고    scopus 로고
    • Evolution and function of CAG/polyglutamine repeats in protein-protein interaction networks
    • Schaefer M.H., Wanker E.E., Andrade-Navarro M.A. Evolution and function of CAG/polyglutamine repeats in protein-protein interaction networks. Nucleic Acids Res. 2012, 40:4273-4287.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4273-4287
    • Schaefer, M.H.1    Wanker, E.E.2    Andrade-Navarro, M.A.3
  • 22
    • 78649811312 scopus 로고    scopus 로고
    • Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117
    • Todi S.V., Scaglione K.M., Blount J.R., Basrur V., Conlon K.P., Pastore A., Elenitoba-Johnson K., Paulson H.L. Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117. J. Biol. Chem. 2010, 285:39303-39313.
    • (2010) J. Biol. Chem. , vol.285 , pp. 39303-39313
    • Todi, S.V.1    Scaglione, K.M.2    Blount, J.R.3    Basrur, V.4    Conlon, K.P.5    Pastore, A.6    Elenitoba-Johnson, K.7    Paulson, H.L.8
  • 23
    • 63149139630 scopus 로고    scopus 로고
    • Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity
    • Pennuto M., Palazzolo I., Poletti A. Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity. Hum. Mol. Genet. 2009, 18:R40-R47.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. R40-R47
    • Pennuto, M.1    Palazzolo, I.2    Poletti, A.3
  • 26
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal
    • Riley B.E., Zoghbi H.Y., Orr H.T. SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal. J. Biol. Chem. 2005, 280:21942-21948.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21942-21948
    • Riley, B.E.1    Zoghbi, H.Y.2    Orr, H.T.3
  • 28
    • 77649184659 scopus 로고    scopus 로고
    • Oxidative stress-enhanced SUMOylation and aggregation of ataxin-1: Implication of JNK pathway
    • Ryu J., Cho S., Park B.C., Lee do H. Oxidative stress-enhanced SUMOylation and aggregation of ataxin-1: Implication of JNK pathway. Biochem. Biophys. Res. Commun. 2010, 393:280-285.
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 280-285
    • Ryu, J.1    Cho, S.2    Park, B.C.3    Lee do, H.4
  • 29
    • 69249090927 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation
    • Mukherjee S., Thomas M., Dadgar N., Lieberman A.P., Iniguez-Lluhi J.A. Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation. J. Biol. Chem. 2009, 284:21296-21306.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21296-21306
    • Mukherjee, S.1    Thomas, M.2    Dadgar, N.3    Lieberman, A.P.4    Iniguez-Lluhi, J.A.5
  • 31
    • 79953009529 scopus 로고    scopus 로고
    • Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity
    • Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J. Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity. J. Biol. Chem. 2011, 286:4555-4565.
    • (2011) J. Biol. Chem. , vol.286 , pp. 4555-4565
    • Weeks, S.D.1    Grasty, K.C.2    Hernandez-Cuebas, L.3    Loll, P.J.4
  • 32
    • 59249095983 scopus 로고    scopus 로고
    • Enhanced detection of in vivo SUMO conjugation by Ubc9 fusion-dependent sumoylation (UFDS)
    • Niedenthal R. Enhanced detection of in vivo SUMO conjugation by Ubc9 fusion-dependent sumoylation (UFDS). Methods Mol. Biol. 2009, 497:63-79.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 63-79
    • Niedenthal, R.1
  • 33
    • 77954957347 scopus 로고    scopus 로고
    • A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants
    • Tang W.K., Li D., Li C.C., Esser L., Dai R., Guo L., Xia D. A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. EMBO J. 2010, 29:2217-2229.
    • (2010) EMBO J. , vol.29 , pp. 2217-2229
    • Tang, W.K.1    Li, D.2    Li, C.C.3    Esser, L.4    Dai, R.5    Guo, L.6    Xia, D.7
  • 37
    • 4444354577 scopus 로고    scopus 로고
    • High Ca(2+)-phosphate transfection efficiency enables single neuron gene analysis
    • Jiang M., Deng L., Chen G. High Ca(2+)-phosphate transfection efficiency enables single neuron gene analysis. Gene Ther. 2004, 11:1303-1311.
    • (2004) Gene Ther. , vol.11 , pp. 1303-1311
    • Jiang, M.1    Deng, L.2    Chen, G.3
  • 38
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 287:252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 39
    • 33745195252 scopus 로고    scopus 로고
    • The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step
    • Ellisdon A.M., Thomas B., Bottomley S.P. The two-stage pathway of ataxin-3 fibrillogenesis involves a polyglutamine-independent step. J. Biol. Chem. 2006, 281:16888-16896.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16888-16896
    • Ellisdon, A.M.1    Thomas, B.2    Bottomley, S.P.3
  • 40
    • 78149430698 scopus 로고    scopus 로고
    • Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties
    • Harris G.M., Dodelzon K., Gong L., Gonzalez-Alegre P., Paulson H.L. Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties. PLoS One 2010, 5:e13695.
    • (2010) PLoS One , vol.5 , pp. e13695
    • Harris, G.M.1    Dodelzon, K.2    Gong, L.3    Gonzalez-Alegre, P.4    Paulson, H.L.5
  • 42
    • 33847649960 scopus 로고    scopus 로고
    • Ubc9 fusion-directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation
    • Jakobs A., Koehnke J., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R. Ubc9 fusion-directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation. Nat. Methods 2007, 4:245-250.
    • (2007) Nat. Methods , vol.4 , pp. 245-250
    • Jakobs, A.1    Koehnke, J.2    Himstedt, F.3    Funk, M.4    Korn, B.5    Gaestel, M.6    Niedenthal, R.7
  • 46
    • 9144264986 scopus 로고    scopus 로고
    • Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease
    • Chow M.K., Ellisdon A.M., Cabrita L.D., Bottomley S.P. Polyglutamine expansion in ataxin-3 does not affect protein stability: implications for misfolding and disease. J. Biol. Chem. 2004, 279:47643-47651.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47643-47651
    • Chow, M.K.1    Ellisdon, A.M.2    Cabrita, L.D.3    Bottomley, S.P.4
  • 47
    • 80053156781 scopus 로고    scopus 로고
    • Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein
    • Saunders H.M., Gilis D., Rooman M., Dehouck Y., Robertson A.L., Bottomley S.P. Flanking domain stability modulates the aggregation kinetics of a polyglutamine disease protein. Protein Sci. 2011, 20:1675-1681.
    • (2011) Protein Sci. , vol.20 , pp. 1675-1681
    • Saunders, H.M.1    Gilis, D.2    Rooman, M.3    Dehouck, Y.4    Robertson, A.L.5    Bottomley, S.P.6
  • 49
    • 84899751309 scopus 로고    scopus 로고
    • Structural basis for ovarian tumor domain-containing protein 1 (OTU1) binding to p97/valosin-containing protein (VCP)
    • Kim S.J., Cho J., Song E.J., Kim H.M., Lee K.E., Suh S.W., Kim E.E. Structural basis for ovarian tumor domain-containing protein 1 (OTU1) binding to p97/valosin-containing protein (VCP). J. Biol. Chem. 2014, 289:12264-12274.
    • (2014) J. Biol. Chem. , vol.289 , pp. 12264-12274
    • Kim, S.J.1    Cho, J.2    Song, E.J.3    Kim, H.M.4    Lee, K.E.5    Suh, S.W.6    Kim, E.E.7
  • 50
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • Jana N.R., Dikshit P., Goswami A., Kotliarova S., Murata S., Tanaka K., Nukina N. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. J. Biol. Chem. 2005, 280:11635-11640.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 52
    • 84860660444 scopus 로고    scopus 로고
    • Toward understanding Machado-Joseph disease
    • Costa Mdo C., Paulson H.L. Toward understanding Machado-Joseph disease. Prog. Neurobiol. 2012, 97:239-257.
    • (2012) Prog. Neurobiol. , vol.97 , pp. 239-257
    • Costa Mdo, C.1    Paulson, H.L.2
  • 53
    • 79251572023 scopus 로고    scopus 로고
    • Functional interactions as a survival strategy against abnormal aggregation
    • Masino L., Nicastro G., Calder L., Vendruscolo M., Pastore A. Functional interactions as a survival strategy against abnormal aggregation. FASEB J. 2011, 25:45-54.
    • (2011) FASEB J. , vol.25 , pp. 45-54
    • Masino, L.1    Nicastro, G.2    Calder, L.3    Vendruscolo, M.4    Pastore, A.5
  • 54
    • 33947586837 scopus 로고    scopus 로고
    • Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein
    • Ellisdon A.M., Pearce M.C., Bottomley S.P. Mechanisms of ataxin-3 misfolding and fibril formation: kinetic analysis of a disease-associated polyglutamine protein. J. Mol. Biol. 2007, 368:595-605.
    • (2007) J. Mol. Biol. , vol.368 , pp. 595-605
    • Ellisdon, A.M.1    Pearce, M.C.2    Bottomley, S.P.3
  • 56
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function?
    • Kerscher O. SUMO junction-what's your function?. EMBO Rep. 2007, 8:550-555.
    • (2007) EMBO Rep. , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 58
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y., Meyer H.H., Rapoport T.A. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 2003, 162:71-84.
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 59
    • 84865602944 scopus 로고    scopus 로고
    • Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin
    • Dantuma N.P., Hoppe T. Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin. Trends Cell Biol. 2012, 22:483-491.
    • (2012) Trends Cell Biol. , vol.22 , pp. 483-491
    • Dantuma, N.P.1    Hoppe, T.2
  • 61
    • 75349101096 scopus 로고    scopus 로고
    • Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97
    • Ewens C.A., Kloppsteck P., Forster A., Zhang X., Freemont P.S. Structural and functional implications of phosphorylation and acetylation in the regulation of the AAA+ protein p97. Biochem. Cell Biol. 2010, 88:41-48.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 41-48
    • Ewens, C.A.1    Kloppsteck, P.2    Forster, A.3    Zhang, X.4    Freemont, P.S.5
  • 62
    • 39449116598 scopus 로고    scopus 로고
    • Roles of VCP in human neurodegenerative disorders
    • Kakizuka A. Roles of VCP in human neurodegenerative disorders. Biochem. Soc. Trans. 2008, 36:105-108.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 105-108
    • Kakizuka, A.1
  • 64
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation
    • Song J., Zhang Z., Hu W., Chen Y. Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J. Biol. Chem. 2005, 280:40122-40129.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 66
    • 79958134700 scopus 로고    scopus 로고
    • Hierarchical binding of cofactors to the AAA ATPase p97
    • Hanzelmann P., Buchberger A., Schindelin H. Hierarchical binding of cofactors to the AAA ATPase p97. Structure 2011, 19:833-843.
    • (2011) Structure , vol.19 , pp. 833-843
    • Hanzelmann, P.1    Buchberger, A.2    Schindelin, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.