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Volumn 23, Issue 5, 2004, Pages 1030-1039

Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47

Author keywords

AAA + ATPase; P47; P97; Ubiquitin; UBX

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATASE; N ETHYLMALEIMIDE; PROTEIN P47; PROTEIN P97; UBIQUITIN;

EID: 1842576796     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600139     Document Type: Article
Times cited : (166)

References (67)
  • 1
    • 0037076507 scopus 로고    scopus 로고
    • Cdc48-ufd1-npl4: Stuck in the middle with ub
    • Bays NW, Hampton RY (2002) Cdc48-ufd1-npl4: stuck in the middle with ub. Curr Biol 12: R366-R371
    • (2002) Curr Biol , vol.12
    • Bays, N.W.1    Hampton, R.Y.2
  • 2
    • 0344091553 scopus 로고    scopus 로고
    • Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model
    • Beuron F, Flynn TC, Ma J, Kondo H, Zhang X, Freemont PS (2003) Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model. J Mol Biol 327: 619-629
    • (2003) J Mol Biol , vol.327 , pp. 619-629
    • Beuron, F.1    Flynn, T.C.2    Ma, J.3    Kondo, H.4    Zhang, X.5    Freemont, P.S.6
  • 4
    • 0036569345 scopus 로고    scopus 로고
    • From UBA to UBX: New words in the ubiquitin vocabulary
    • Buchberger A (2002) From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol 12: 216-221
    • (2002) Trends Cell Biol , vol.12 , pp. 216-221
    • Buchberger, A.1
  • 7
    • 0037012104 scopus 로고    scopus 로고
    • Structure of GABARAP in two conformations: Implications for GABA(A) receptor localization and tubulin binding
    • Coyle JE, Qamar S, Rajashankar KR, Nikolov DB (2002) Structure of GABARAP in two conformations: implications for GABA(A) receptor localization and tubulin binding. Neuron 33: 63-74
    • (2002) Neuron , vol.33 , pp. 63-74
    • Coyle, J.E.1    Qamar, S.2    Rajashankar, K.R.3    Nikolov, D.B.4
  • 8
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha
    • Dai RM, Chen E, Longo DL, Gorbea CM, Li CC (1998) Involvement of valosin-containing protein, an ATPase co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J Biol Chem 273: 3562-3573
    • (1998) J Biol Chem , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.C.5
  • 9
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai RM, Li CC (2001) Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat Cell Biol 3: 740-744
    • (2001) Nat Cell Biol , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 10
    • 0037010120 scopus 로고    scopus 로고
    • AAA + proteins and substrate recognition, it all depends on their partner in crime
    • Dougan DA, Mogk A, Zeth K, Turgay K, Bukau B (2002) AAA + proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett 529: 6-10
    • (2002) FEBS Lett , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 11
    • 0032825282 scopus 로고    scopus 로고
    • The Janus face of the archaeal Cdc48/p97 homologue VAT: Protein folding versus unfolding
    • Golbik R, Lupas AN, Koretke KK, Baumeister W, Peters J (1999) The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding. Biol Chem 380: 1049-1062
    • (1999) Biol Chem , vol.380 , pp. 1049-1062
    • Golbik, R.1    Lupas, A.N.2    Koretke, K.K.3    Baumeister, W.4    Peters, J.5
  • 12
    • 0037195961 scopus 로고    scopus 로고
    • Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA + chaperone, ClpA
    • Guo F, Esser L, Singh SK, Maurizi MR, Xia D (2002a) Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA + chaperone, ClpA. J Biol Chem 277: 46753-46762
    • (2002) J Biol Chem , vol.277 , pp. 46753-46762
    • Guo, F.1    Esser, L.2    Singh, S.K.3    Maurizi, M.R.4    Xia, D.5
  • 13
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • Guo F, Maurizi MR, Esser L, Xia D (2002b) Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J Biol Chem 277: 46743-46752
    • (2002) J Biol Chem , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 15
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson PI, Roth R, Morisaki H, Jahn R, Heuser JE (1997) Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90: 523-535
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 17
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K, Bucher P (1996) The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem Sci 21: 172-173
    • (1996) Trends Biochem Sci , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 18
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes
    • Hohl TM, Parlati F, Wimmer C, Rothman JE, Sollner TH, Engelhardt H (1998) Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes. Mol Cell 2: 539-548
    • (1998) Mol Cell , vol.2 , pp. 539-548
    • Hohl, T.M.1    Parlati, F.2    Wimmer, C.3    Rothman, J.E.4    Sollner, T.H.5    Engelhardt, H.6
  • 19
    • 0031778630 scopus 로고    scopus 로고
    • Structural basis for the interaction of Ras with RalGDS
    • Huang L, Hofer F, Martin GS, Kim SH (1998) Structural basis for the interaction of Ras with RalGDS. Nat Struct Biol 5: 422-426
    • (1998) Nat Struct Biol , vol.5 , pp. 422-426
    • Huang, L.1    Hofer, F.2    Martin, G.S.3    Kim, S.H.4
  • 21
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch S, Pyrowolakis G (2000) Ubiquitin and its kin: how close are the family ties? Trends Cell Biol 10: 335-342
    • (2000) Trends Cell Biol , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan S, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47: 110-119
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 24
    • 0037085253 scopus 로고    scopus 로고
    • The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein
    • Knight D, Harris R, McAlister MS, Phelan JP, Geddes S, Moss SJ, Driscoll PC, Keep NH (2002) The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein. J Biol Chem 277: 5556-5561
    • (2002) J Biol Chem , vol.277 , pp. 5556-5561
    • Knight, D.1    Harris, R.2    McAlister, M.S.3    Phelan, J.P.4    Geddes, S.5    Moss, S.J.6    Driscoll, P.C.7    Keep, N.H.8
  • 26
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24: 946-950
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 27
    • 0036054289 scopus 로고    scopus 로고
    • The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution
    • Krzywda S, Brzozowski AM, Verma C, Karata K, Ogura T, Wilkinson AJ (2002) The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 A resolution. Structure (Camb) 10: 1073-1083
    • (2002) Structure (Camb) , vol.10 , pp. 1073-1083
    • Krzywda, S.1    Brzozowski, A.M.2    Verma, C.3    Karata, K.4    Ogura, T.5    Wilkinson, A.J.6
  • 28
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam YA, Lawson TG, Velayutham M, Zweier JL, Pickart CM (2002) A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416: 763-767
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 31
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L, Chothia C, Janin J (1999) The atomic structure of protein-protein recognition sites. J Mol Biol 285: 2177-2198
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 33
    • 0037080165 scopus 로고    scopus 로고
    • Uncoupling the ATPase activity of the N-ethylmaleimide sensitive factor (NSF) from 20S complex disassembly
    • Matveeva EA, May AP, He P, Whiteheart SW (2002) Uncoupling the ATPase activity of the N-ethylmaleimide sensitive factor (NSF) from 20S complex disassembly. Biochemistry 41: 530-536
    • (2002) Biochemistry , vol.41 , pp. 530-536
    • Matveeva, E.A.1    May, A.P.2    He, P.3    Whiteheart, S.W.4
  • 34
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein
    • May AP, Misura KM, Whiteheart SW, Weis WI (1999) Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nat Cell Biol 1: 175-182
    • (1999) Nat Cell Biol , vol.1 , pp. 175-182
    • May, A.P.1    Misura, K.M.2    Whiteheart, S.W.3    Weis, W.I.4
  • 35
    • 0035933710 scopus 로고    scopus 로고
    • Unraveling the mechanism of the vesicle transport ATPase NSF, the N-ethylmaleimide-sensitive factor
    • May AP, Whiteheart SW, Weis WI (2001) Unraveling the mechanism of the vesicle transport ATPase NSF, the N-ethylmaleimide-sensitive factor. J Biol Chem 276: 21991-21994
    • (2001) J Biol Chem , vol.276 , pp. 21991-21994
    • May, A.P.1    Whiteheart, S.W.2    Weis, W.I.3
  • 36
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ (1997) Raster3D: photorealistic molecular graphics. Meth Enzymol 277: 505-524
    • (1997) Meth Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 37
    • 0032561398 scopus 로고    scopus 로고
    • The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
    • Meyer HH, Kondo H, Warren G (1998) The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. FEBS Lett 437: 255-257
    • (1998) FEBS Lett , vol.437 , pp. 255-257
    • Meyer, H.H.1    Kondo, H.2    Warren, G.3
  • 38
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19: 2181-2192
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 39
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • Meyer HH, Wang Y, Warren G (2002) Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J 21: 5645-5652
    • (2002) EMBO J , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 42
    • 0036773132 scopus 로고    scopus 로고
    • Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8
    • Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K (2002) Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure (Camb) 10: 1415-1423
    • (2002) Structure (Camb) , vol.10 , pp. 1415-1423
    • Niwa, H.1    Tsuchiya, D.2    Makyio, H.3    Yoshida, M.4    Morikawa, K.5
  • 43
    • 0034885052 scopus 로고    scopus 로고
    • AAA + superfamily ATPases: Common structure - Diverse function
    • Ogura T, Wilkinson AJ (2001) AAA + superfamily ATPases: common structure - diverse function. Genes Cells 6: 575-597
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of x-ray diffraction data collected in oscillation mode. Meth Enzymol 276: 307-326
    • (1997) Meth Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 0034682843 scopus 로고    scopus 로고
    • Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p
    • Paz Y, Elazar Z, Fass D (2000) Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p. J Biol Chem 275: 25445-25450
    • (2000) J Biol Chem , vol.275 , pp. 25445-25450
    • Paz, Y.1    Elazar, Z.2    Fass, D.3
  • 46
    • 0027493180 scopus 로고
    • Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein
    • Pleasure IT, Black MM, Keen JH (1993) Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. Nature 565: 459-462
    • (1993) Nature , vol.565 , pp. 459-462
    • Pleasure, I.T.1    Black, M.M.2    Keen, J.H.3
  • 47
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille C, Kondo H, Newman R, Hui N, Freemont P, Warren G (1998) Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92: 603-610
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, P.5    Warren, G.6
  • 48
    • 0028268603 scopus 로고
    • Synthetic, structural and biological studies of the ubiquitin system: The total chemical synthesis of ubiquitin
    • Ramage R, Green J, Muir TW, Ogunjobi OM, Love S, Shaw K (1994) Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin. Biochem J 299 (Part 1): 151-158
    • (1994) Biochem J , vol.299 , Issue.PART 1 , pp. 151-158
    • Ramage, R.1    Green, J.2    Muir, T.W.3    Ogunjobi, O.M.4    Love, S.5    Shaw, K.6
  • 49
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaper-one
    • Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaper-one. Cell 107: 667-677
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 50
    • 0033165863 scopus 로고    scopus 로고
    • Crystal structure of the vesicular transport protein Sec17: Implications for SNAP function in SNARE complex disassembly
    • Rice LM, Brunger AT (1999) Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly. Mol Cell 4: 85-95
    • (1999) Mol Cell , vol.4 , pp. 85-95
    • Rice, L.M.1    Brunger, A.T.2
  • 53
    • 0001417555 scopus 로고    scopus 로고
    • GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28
    • Sagiv Y, Legesse-Miller A, Porat A, Elazar Z (2000) GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28. EMBO J 19: 1494-1504
    • (2000) EMBO J , vol.19 , pp. 1494-1504
    • Sagiv, Y.1    Legesse-Miller, A.2    Porat, A.3    Elazar, Z.4
  • 55
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumor suppressor function
    • Stebbins CE, Kaelin Jr WG, Pavletich NP (1999) Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284: 455-461
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 56
    • 0037449938 scopus 로고    scopus 로고
    • GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3
    • Tanida I, Komatsu M, Ueno T, Kominami E (2003) GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3. Biochem Biophys Res Commun 300: 637-644
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 637-644
    • Tanida, I.1    Komatsu, M.2    Ueno, T.3    Kominami, E.4
  • 57
    • 0037024380 scopus 로고    scopus 로고
    • Cdc48 can distinguish between native and non-native proteins in the absence of cofactors
    • Thoms S (2002) Cdc48 can distinguish between native and non-native proteins in the absence of cofactors. FEBS Lett 520: 107-110
    • (2002) FEBS Lett , vol.520 , pp. 107-110
    • Thoms, S.1
  • 60
    • 0037815483 scopus 로고    scopus 로고
    • The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle
    • Uchiyama K, Jokitalo E, Lindman M, Jackman M, Kano F, Murata M, Zhang X, Kondo H (2003) The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle. J Cell Biol 161: 1067-1079
    • (2003) J Cell Biol , vol.161 , pp. 1067-1079
    • Uchiyama, K.1    Jokitalo, E.2    Lindman, M.3    Jackman, M.4    Kano, F.5    Murata, M.6    Zhang, X.7    Kondo, H.8
  • 61
    • 0035003581 scopus 로고    scopus 로고
    • N-ethylmaleimide sensitive factor (NSF) structure and function
    • Whiteheart SW, Schraw T, Matveeva EA (2001) N-ethylmaleimide sensitive factor (NSF) structure and function. Int Rev Cytol 207: 71-112
    • (2001) Int Rev Cytol , vol.207 , pp. 71-112
    • Whiteheart, S.W.1    Schraw, T.2    Matveeva, E.A.3
  • 62
    • 0033959478 scopus 로고    scopus 로고
    • p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication
    • Yamada T, Okuhara K, Iwamatsu A, Seo H, Ohta K, Shibata T, Murofushi H (2000) p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication. FEBS Lett 466: 287-291
    • (2000) FEBS Lett , vol.466 , pp. 287-291
    • Yamada, T.1    Okuhara, K.2    Iwamatsu, A.3    Seo, H.4    Ohta, K.5    Shibata, T.6    Murofushi, H.7
  • 63
    • 0033165864 scopus 로고    scopus 로고
    • NSF N-terminal domain crystal structure: Models of NSF function
    • Yu RC, Jahn R, Brunger AT (1999) NSF N-terminal domain crystal structure: models of NSF function. Mol Cell 4: 97-107
    • (1999) Mol Cell , vol.4 , pp. 97-107
    • Yu, R.C.1    Jahn, R.2    Brunger, A.T.3
  • 64
    • 0035839113 scopus 로고    scopus 로고
    • Solution structure and interaction surface of the C-terminal domain from p47: A major p97-cofactor involved in SNARE disassembly
    • Yuan X, Shaw A, Zhang X, Kondo H, Lally J, Freemont PS, Matthews S (2001) Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly. J Mol Biol 311: 255-263
    • (2001) J Mol Biol , vol.311 , pp. 255-263
    • Yuan, X.1    Shaw, A.2    Zhang, X.3    Kondo, H.4    Lally, J.5    Freemont, P.S.6    Matthews, S.7
  • 65
    • 0036896886 scopus 로고    scopus 로고
    • Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
    • Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA (2002) Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat Struct Biol 9: 906-911
    • (2002) Nat Struct Biol , vol.9 , pp. 906-911
    • Zeth, K.1    Ravelli, R.B.2    Paal, K.3    Cusack, S.4    Bukau, B.5    Dougan, D.A.6
  • 66
    • 0033855808 scopus 로고    scopus 로고
    • VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells
    • Zhang H, Wang Q, Kajino K, Greene MI (2000a) VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol 19: 253-263
    • (2000) DNA Cell Biol , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4


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