{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,24]],"date-time":"2026-04-24T13:47:29Z","timestamp":1777038449571,"version":"3.51.4"},"reference-count":46,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2003,8,31]],"date-time":"2003-08-31T00:00:00Z","timestamp":1062288000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2003,10]]},"DOI":"10.1038\/nsb972","type":"journal-article","created":{"date-parts":[[2003,8,29]],"date-time":"2003-08-29T14:00:45Z","timestamp":1062165645000},"page":"856-863","source":"Crossref","is-referenced-by-count":341,"title":["Complete structure of p97\/valosin-containing protein reveals communication between nucleotide domains"],"prefix":"10.1038","volume":"10","author":[{"given":"Byron","family":"DeLaBarre","sequence":"first","affiliation":[]},{"given":"Axel T","family":"Brunger","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2003,8,31]]},"reference":[{"key":"BFnsb972_CR1","doi-asserted-by":"publisher","first-page":"1086","DOI":"10.1038\/ncb1201-1086","volume":"3","author":"M Hetzer","year":"2001","unstructured":"Hetzer, M. et al. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nat. Cell Biol. 3, 1086\u20131091 (2001).","journal-title":"Nat. Cell Biol."},{"key":"BFnsb972_CR2","doi-asserted-by":"publisher","first-page":"905","DOI":"10.1016\/0092-8674(95)90270-8","volume":"82","author":"C Rabouille","year":"1995","unstructured":"Rabouille, C., Levine, T.P., Peters, J.M. & Warren, G. An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell 82, 905\u2013914 (1995).","journal-title":"Cell"},{"key":"BFnsb972_CR3","doi-asserted-by":"publisher","first-page":"652","DOI":"10.1038\/414652a","volume":"414","author":"Y Ye","year":"2001","unstructured":"Ye, Y., Meyer, H.H. & Rapoport, T.A. The AAA ATPase Cdc48\/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652\u2013656 (2001).","journal-title":"Nature"},{"key":"BFnsb972_CR4","doi-asserted-by":"publisher","first-page":"626","DOI":"10.1128\/MCB.22.2.626-634.2002","volume":"22","author":"E Rabinovich","year":"2002","unstructured":"Rabinovich, E., Kerem, A., Frohlich, K.U., Diamant, N. & Bar-Nun, S. AAA-ATPase p97\/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell. Biol. 22, 626\u2013634 (2002).","journal-title":"Mol. Cell. Biol."},{"key":"BFnsb972_CR5","doi-asserted-by":"publisher","first-page":"615","DOI":"10.1093\/emboj\/21.4.615","volume":"21","author":"S Braun","year":"2002","unstructured":"Braun, S., Matuschewski, K., Rape, M., Thoms, S. & Jentsch, S. Role of the ubiquitin-selective CDC48(UFD1\/NPL4)chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615\u2013621 (2002).","journal-title":"EMBO J."},{"key":"BFnsb972_CR6","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1111\/j.1349-7006.2002.tb02172.x","volume":"93","author":"T Asai","year":"2002","unstructured":"Asai, T. et al. VCP (p97) regulates NF-\u03baB signaling pathway, which is important for metastasis of osteosarcoma cell line. Jpn. J. Cancer Res. 93, 296\u2013304 (2002).","journal-title":"Jpn. J. Cancer Res."},{"key":"BFnsb972_CR7","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1038\/40411","volume":"388","author":"H Kondo","year":"1997","unstructured":"Kondo, H. et al. p47 is a cofactor for p97-mediated membrane fusion. Nature 388, 75\u201378 (1997).","journal-title":"Nature"},{"key":"BFnsb972_CR8","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1083\/jcb.200208112","volume":"159","author":"K Uchiyama","year":"2002","unstructured":"Uchiyama, K. et al. VCIP135, a novel essential factor for p97\/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. J. Cell Biol. 159, 855\u2013866 (2002).","journal-title":"J. Cell Biol."},{"key":"BFnsb972_CR9","doi-asserted-by":"publisher","first-page":"5645","DOI":"10.1093\/emboj\/cdf579","volume":"21","author":"HH Meyer","year":"2002","unstructured":"Meyer, H.H., Wang, Y. & Warren, G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 21, 5645\u20135652 (2002).","journal-title":"EMBO J."},{"key":"BFnsb972_CR10","doi-asserted-by":"publisher","first-page":"262","DOI":"10.1091\/mbc.02-07-0115","volume":"14","author":"M Nagahama","year":"2003","unstructured":"Nagahama, M. et al. SVIP is a novel VCP\/p97-interacting protein whose expression causes cell vacuolation. Mol. Biol. Cell 14, 262\u2013273 (2003).","journal-title":"Mol. Biol. Cell"},{"key":"BFnsb972_CR11","doi-asserted-by":"publisher","first-page":"977","DOI":"10.1038\/sj.cdd.4400907","volume":"8","author":"M Hirabayashi","year":"2001","unstructured":"Hirabayashi, M. et al. VCP\/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration. Cell Death Differ. 8, 977\u2013984 (2001).","journal-title":"Cell Death Differ."},{"key":"BFnsb972_CR12","doi-asserted-by":"publisher","first-page":"264","DOI":"10.1038\/sj.cdd.4400955","volume":"9","author":"H Higashiyama","year":"2002","unstructured":"Higashiyama, H. et al. Identification of ter94, Drosophila VCP, as a modulator of polyglutamine-induced neurodegeneration. Cell Death Differ. 9, 264\u2013273 (2002).","journal-title":"Cell Death Differ."},{"key":"BFnsb972_CR13","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1016\/S0304-3940(03)00280-5","volume":"343","author":"Y Mizuno","year":"2003","unstructured":"Mizuno, Y., Hori, S., Kakizuka, A. & Okamoto, K. Vacuole-creating protein in neurodegenerative diseases in humans. Neurosci. Lett. 343, 77\u201380 (2003).","journal-title":"Neurosci. Lett."},{"key":"BFnsb972_CR14","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1083\/jcb.114.3.443","volume":"114","author":"KU Frohlich","year":"1991","unstructured":"Frohlich, K.U. et al. Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J. Cell Biol. 114, 443\u2013453 (1991).","journal-title":"J. Cell Biol."},{"key":"BFnsb972_CR15","doi-asserted-by":"publisher","first-page":"21512","DOI":"10.1074\/jbc.M100235200","volume":"276","author":"JR Lamb","year":"2001","unstructured":"Lamb, J.R., Fu, V., Wirtz, E. & Bangs, J.D. Functional analysis of the trypanosomal AAA protein TbVCP with trans-dominant ATP hydrolysis mutants. J. Biol. Chem. 276, 21512\u201321520 (2001).","journal-title":"J. Biol. Chem."},{"key":"BFnsb972_CR16","doi-asserted-by":"publisher","first-page":"5626","DOI":"10.1002\/j.1460-2075.1995.tb00250.x","volume":"14","author":"HS Feiler","year":"1995","unstructured":"Feiler, H.S. et al. The higher plant Arabidopsis thaliana encodes a functional CDC48 homolog which is highly expressed in dividing and expanding cells. EMBO J. 14, 5626\u20135637 (1995).","journal-title":"EMBO J."},{"key":"BFnsb972_CR17","doi-asserted-by":"crossref","first-page":"2662","DOI":"10.1016\/S0021-9258(18)53825-4","volume":"268","author":"M Tagaya","year":"1993","unstructured":"Tagaya, M., Wilson, D.W., Brunner, M., Arango, N. & Rothman, J.E. Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268, 2662\u20132666 (1993).","journal-title":"J. Biol. Chem."},{"key":"BFnsb972_CR18","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/0092-8674(88)90554-5","volume":"54","author":"V Malhotra","year":"1988","unstructured":"Malhotra, V., Orci, L., Glick, B.S., Block, M.R. & Rothman, J.E. Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack. Cell 54, 221\u2013227 (1988).","journal-title":"Cell"},{"key":"BFnsb972_CR19","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/S0014-5793(99)00431-7","volume":"451","author":"B Rockel","year":"1999","unstructured":"Rockel, B. et al. Structure of VAT, a CDC48\/p97 ATPase homolog from the archaeon Thermoplasma acidophilum as studied by electron tomography. FEBS Lett. 451, 27\u201332 (1999).","journal-title":"FEBS Lett."},{"key":"BFnsb972_CR20","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/S1097-2765(00)80191-4","volume":"4","author":"RC Yu","year":"1999","unstructured":"Yu, R.C., Jahn, R. & Brunger, A.T. NSF N-terminal domain crystal structure: models of NSF function. Mol. Cell 4, 97\u2013107 (1999).","journal-title":"Mol. Cell"},{"key":"BFnsb972_CR21","doi-asserted-by":"publisher","first-page":"803","DOI":"10.1038\/1843","volume":"5","author":"RC Yu","year":"1998","unstructured":"Yu, R.C., Hanson, P.I., Jahn, R. & Brunger, A.T. Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol. 5, 803\u2013811 (1998).","journal-title":"Nat. Struct. Biol."},{"key":"BFnsb972_CR22","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1038\/11097","volume":"1","author":"AP May","year":"1999","unstructured":"May, A.P., Misura, K.M., Whiteheart, S.W. & Weis, W.I. Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nat. Cell Biol. 1, 175\u2013182 (1999).","journal-title":"Nat. Cell Biol."},{"key":"BFnsb972_CR23","doi-asserted-by":"publisher","first-page":"525","DOI":"10.1016\/S0092-8674(00)81593-7","volume":"94","author":"CU Lenzen","year":"1998","unstructured":"Lenzen, C.U., Steinmann, D., Whiteheart, S.W. & Weis, W.I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525\u2013536 (1998).","journal-title":"Cell"},{"key":"BFnsb972_CR24","doi-asserted-by":"publisher","first-page":"1158","DOI":"10.1016\/S0960-9822(00)80017-2","volume":"9","author":"M Coles","year":"1999","unstructured":"Coles, M. et al. The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple \u03b2\u03b1\u03b2\u03b2 element. Curr. Biol. 9, 1158\u20131168 (1999).","journal-title":"Curr. Biol."},{"key":"BFnsb972_CR25","doi-asserted-by":"publisher","first-page":"14759","DOI":"10.1073\/pnas.96.26.14759","volume":"96","author":"SM Babor","year":"1999","unstructured":"Babor, S.M. & Fass, D. Crystal structure of the Sec18p N-terminal domain. Proc. Natl. Acad. Sci. USA 96, 14759\u201314764 (1999).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsb972_CR26","doi-asserted-by":"publisher","first-page":"1473","DOI":"10.1016\/S1097-2765(00)00143-X","volume":"6","author":"X Zhang","year":"2000","unstructured":"Zhang, X. et al. Structure of the AAA ATPase p97. Mol. Cell 6, 1473\u20131484 (2000).","journal-title":"Mol. Cell"},{"key":"BFnsb972_CR27","doi-asserted-by":"publisher","first-page":"950","DOI":"10.1038\/nsb872","volume":"9","author":"I Rouiller","year":"2002","unstructured":"Rouiller, I. et al. Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle. Nat. Struct. Biol. 9, 950\u2013957 (2002).","journal-title":"Nat. Struct. Biol."},{"key":"BFnsb972_CR28","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1006\/jmbi.2002.5448","volume":"317","author":"B Rockel","year":"2002","unstructured":"Rockel, B., Jakana, J., Chiu, W. & Baumeister, W. Electron cryo-microscopy of VAT, the archaeal p97\/CDC48 homolog from Thermoplasma acidophilum. J. Mol. Biol. 317, 673\u2013681 (2002).","journal-title":"J. Mol. Biol."},{"key":"BFnsb972_CR29","doi-asserted-by":"crossref","unstructured":"Guo, F., Maurizi, M.R., Esser, L. & Xia, D. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J. Biol. Chem. 277, 46743\u201346752.","DOI":"10.1074\/jbc.M207796200"},{"key":"BFnsb972_CR30","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1016\/S0022-2836(03)00178-5","volume":"327","author":"F Beuron","year":"2003","unstructured":"Beuron, F. et al. Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model. J. Mol. Biol. 327, 619\u2013629 (2003).","journal-title":"J. Mol. Biol."},{"key":"BFnsb972_CR31","doi-asserted-by":"publisher","first-page":"3648","DOI":"10.1074\/jbc.M208422200","volume":"278","author":"C Song","year":"2003","unstructured":"Song, C., Wang, Q. & Li, C.C. ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity. J. Biol. Chem. 278, 3648\u20133655 (2003).","journal-title":"J. Biol. Chem."},{"key":"BFnsb972_CR32","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/S0006-291X(02)02840-1","volume":"300","author":"Q Wang","year":"2003","unstructured":"Wang, Q., Song, C. & Li, C.C. Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities. Biochem. Biophys. Res. Commun. 300, 253\u2013260 (2003).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"BFnsb972_CR33","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1101\/gr.9.1.27","volume":"9","author":"AF Neuwald","year":"1999","unstructured":"Neuwald, A.F., Aravind, L., Spouge, J.L. & Koonin, E.V. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27\u201343 (1999).","journal-title":"Genome Res."},{"key":"BFnsb972_CR34","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1016\/S1097-2765(02)00775-X","volume":"11","author":"N Benaroudj","year":"2003","unstructured":"Benaroudj, N., Zwickl, P., Seemuller, E., Baumeister, W. & Goldberg, A.L. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11, 69\u201378 (2003).","journal-title":"Mol. Cell"},{"key":"BFnsb972_CR35","doi-asserted-by":"publisher","first-page":"2043","DOI":"10.1002\/pro.5560061001","volume":"6","author":"A Beyer","year":"1997","unstructured":"Beyer, A. Sequence analysis of the AAA protein family. Protein Sci. 6, 2043\u20132058 (1997).","journal-title":"Protein Sci."},{"key":"BFnsb972_CR36","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","volume":"276","author":"Z Otwinowski","year":"1997","unstructured":"Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307\u2013326 (1997).","journal-title":"Methods Enzymol."},{"key":"BFnsb972_CR37","unstructured":"Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760\u2013763 (1994)."},{"key":"BFnsb972_CR38","doi-asserted-by":"publisher","first-page":"1582","DOI":"10.1126\/science.1077945","volume":"298","author":"RB Bass","year":"2002","unstructured":"Bass, R.B., Strop, P., Barclay, M. & Rees, D.C. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science 298, 1582\u20131587 (2002).","journal-title":"Science"},{"key":"BFnsb972_CR39","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1107\/S0907444998004119","volume":"54","author":"NS Pannu","year":"1998","unstructured":"Pannu, N.S., Murshudov, G.N., Dodson, E.J. & Read, R.J. Incorporation of prior phase information strengthens maximum-likelihood structure refinement. Acta Crystallogr. D 54, 1285\u20131294 (1998).","journal-title":"Acta Crystallogr. D"},{"key":"BFnsb972_CR40","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1006\/jmbi.1994.1633","volume":"243","author":"JS Jiang","year":"1994","unstructured":"Jiang, J.S. & Brunger, A.T. Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures. J. Mol. Biol. 243, 100\u2013115 (1994).","journal-title":"J. Mol. Biol."},{"key":"BFnsb972_CR41","doi-asserted-by":"publisher","first-page":"905","DOI":"10.1107\/S0907444998003254","volume":"54","author":"AT Brunger","year":"1998","unstructured":"Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905\u2013921 (1998).","journal-title":"Acta Crystallogr. D"},{"key":"BFnsb972_CR42","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1107\/S0108767390010224","volume":"47","author":"TA Jones","year":"1991","unstructured":"Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard . Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110\u2013119 (1991).","journal-title":"Acta Crystallogr. A"},{"key":"BFnsb972_CR43","doi-asserted-by":"publisher","first-page":"721","DOI":"10.1038\/11485","volume":"6","author":"I Schlichting","year":"1999","unstructured":"Schlichting, I. & Reinstein, J. pH influences fluoride coordination number of the AlFx phosphoryl transfer transition state analog. Nat. Struct. Biol. 6, 721\u2013723 (1999).","journal-title":"Nat. Struct. Biol."},{"key":"BFnsb972_CR44","doi-asserted-by":"publisher","first-page":"1083","DOI":"10.1038\/nsb1295-1083","volume":"2","author":"K Braig","year":"1995","unstructured":"Braig, K., Adams, P.D. & Brunger, A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 \u00c5 resolution. Nat. Struct. Biol. 2, 1083\u20131094 (1995).","journal-title":"Nat. Struct. Biol."},{"key":"BFnsb972_CR45","doi-asserted-by":"publisher","first-page":"350","DOI":"10.1016\/S0076-6879(98)95048-0","volume":"295","author":"L Indyk","year":"1998","unstructured":"Indyk, L. & Fisher, H.F. Theoretical aspects of isothermal titration calorimetry. Methods Enzymol. 295, 350\u2013364 (1998).","journal-title":"Methods Enzymol."},{"key":"BFnsb972_CR46","first-page":"946","volume":"24","author":"RA Laskowski","year":"1993","unstructured":"Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 24, 946\u2013950 (1993).","journal-title":"J. Appl. Crystallogr."}],"container-title":["Nature Structural & Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsb972.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsb972","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsb972.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,19]],"date-time":"2023-05-19T04:22:19Z","timestamp":1684470139000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsb972"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,8,31]]},"references-count":46,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2003,10]]}},"alternative-id":["BFnsb972"],"URL":"https:\/\/doi.org\/10.1038\/nsb972","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2003,8,31]]}}}