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Volumn 1823, Issue 1, 2012, Pages 2-14

Structure and function of the AAA+ nucleotide binding pocket

Author keywords

AAA+ ATPases; Functional analysis; Nucleotide binding pocket; Structural analysis

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARGININE; BINDING PROTEIN; NUCLEOTIDE BINDING PROTEIN;

EID: 84855198520     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.06.014     Document Type: Review
Times cited : (234)

References (122)
  • 1
    • 0032410805 scopus 로고    scopus 로고
    • The case for a common ancestor: kinesin and myosin motor proteins and G proteins
    • Kull F.J., Vale R.D., Fletterick R.J. The case for a common ancestor: kinesin and myosin motor proteins and G proteins. J. Muscle Res. Cell Motil. 1998, 19:877-886.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 877-886
    • Kull, F.J.1    Vale, R.D.2    Fletterick, R.J.3
  • 2
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: looking under the hood of molecular motor proteins
    • Vale R.D., Milligan R.A. The way things move: looking under the hood of molecular motor proteins. Science 2000, 288:88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 3
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialization in superfamily 1 and 2 helicases
    • Singleton M.R., Wigley D.B. Modularity and specialization in superfamily 1 and 2 helicases. J. Bacteriol. 2002, 184:1819-1826.
    • (2002) J. Bacteriol. , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 4
    • 79953187302 scopus 로고    scopus 로고
    • Superfamily I helicases as modular components of DNA-processing machines
    • Dillingham M.S. Superfamily I helicases as modular components of DNA-processing machines. Biochem. Soc. Trans. 2011, 39:413-423.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 413-423
    • Dillingham, M.S.1
  • 5
    • 25844487733 scopus 로고    scopus 로고
    • Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates
    • Dean M., Annilo T. Evolution of the ATP-binding cassette (ABC) transporter superfamily in vertebrates. Annu. Rev. Genomics Hum. Genet. 2005, 6:123-142.
    • (2005) Annu. Rev. Genomics Hum. Genet. , vol.6 , pp. 123-142
    • Dean, M.1    Annilo, T.2
  • 6
    • 79952254224 scopus 로고    scopus 로고
    • Crystal structure of the dynein motor domain
    • Carter A.P., Cho C., Jin L., Vale R.D. Crystal structure of the dynein motor domain. Science 2011, 331:1159-1165.
    • (2011) Science , vol.331 , pp. 1159-1165
    • Carter, A.P.1    Cho, C.2    Jin, L.3    Vale, R.D.4
  • 9
    • 0025965277 scopus 로고
    • PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases
    • Erdmann R., Wiebel F.F., Flessau A., Rytka J., Beyer A., Frohlich K.U., Kunau W.H. PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases. Cell 1991, 64:499-510.
    • (1991) Cell , vol.64 , pp. 499-510
    • Erdmann, R.1    Wiebel, F.F.2    Flessau, A.3    Rytka, J.4    Beyer, A.5    Frohlich, K.U.6    Kunau, W.H.7
  • 10
    • 0142091549 scopus 로고    scopus 로고
    • Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains
    • Lee S.Y., De La Torre A., Yan D., Kustu S., Nixon B.T., Wemmer D.E. Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains. Genes Dev. 2003, 17:2552-2563.
    • (2003) Genes Dev. , vol.17 , pp. 2552-2563
    • Lee, S.Y.1    De La Torre, A.2    Yan, D.3    Kustu, S.4    Nixon, B.T.5    Wemmer, D.E.6
  • 11
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer L.M., Leipe D.D., Koonin E.V., Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J. Struct. Biol. 2004, 146:11-31.
    • (2004) J. Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 12
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger J.P., Berger J.M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 2006, 35:93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 14
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough J., Karplus K., Hughey R., Chothia C. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J. Mol. Biol. 2001, 313:903-919.
    • (2001) J. Mol. Biol. , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 15
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982, 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 16
    • 55549132236 scopus 로고    scopus 로고
    • The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins
    • Zhang X., Wigley D.B. The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins. Nat. Struct. Mol. Biol. 2008, 15:1223-1227.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1223-1227
    • Zhang, X.1    Wigley, D.B.2
  • 18
    • 28244447739 scopus 로고    scopus 로고
    • GTPase activating proteins: structural and functional insights 18 years after discovery
    • Scheffzek K., Ahmadian M.R. GTPase activating proteins: structural and functional insights 18 years after discovery. Cell. Mol. Life Sci. 2005, 62:3014-3038.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 3014-3038
    • Scheffzek, K.1    Ahmadian, M.R.2
  • 20
  • 21
    • 0037080611 scopus 로고    scopus 로고
    • Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
    • Hattendorf D.A., Lindquist S.L. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J. 2002, 21:12-21.
    • (2002) EMBO J. , vol.21 , pp. 12-21
    • Hattendorf, D.A.1    Lindquist, S.L.2
  • 22
    • 0035793721 scopus 로고    scopus 로고
    • The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites
    • Schlee S., Groemping Y., Herde P., Seidel R., Reinstein J. The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J. Mol. Biol. 2001, 306:889-899.
    • (2001) J. Mol. Biol. , vol.306 , pp. 889-899
    • Schlee, S.1    Groemping, Y.2    Herde, P.3    Seidel, R.4    Reinstein, J.5
  • 23
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart S.W., Rossnagel K., Buhrow S.A., Brunner M., Jaenicke R., Rothman J.E. N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 1994, 126:945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 24
    • 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 T.C., Ma J., Kondo H., Zhang X., Freemont P.S. Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model. J. Mol. Biol. 2003, 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
  • 25
    • 79955525976 scopus 로고    scopus 로고
    • Positive cooperativity of the p97 AAA ATPase is critical for essential functions
    • Nishikori S., Esaki M., Yamanaka K., Sugimoto S., Ogura T. Positive cooperativity of the p97 AAA ATPase is critical for essential functions. J. Biol. Chem. 2011, 286:15815-15820.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15815-15820
    • Nishikori, S.1    Esaki, M.2    Yamanaka, K.3    Sugimoto, S.4    Ogura, T.5
  • 26
    • 0037427531 scopus 로고    scopus 로고
    • Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities
    • 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. 2003, 300:253-260.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 253-260
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 27
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre B., Brunger A.T. Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat. Struct. Biol. 2003, 10:856-863.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 28
    • 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
  • 29
    • 0032546911 scopus 로고    scopus 로고
    • The ATPase activity of Hsp104, effects of environmental conditions and mutations
    • Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., Lindquist S. The ATPase activity of Hsp104, effects of environmental conditions and mutations. J. Biol. Chem. 1998, 273:15546-15552.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15546-15552
    • Schirmer, E.C.1    Queitsch, C.2    Kowal, A.S.3    Parsell, D.A.4    Lindquist, S.5
  • 31
    • 0036295232 scopus 로고    scopus 로고
    • Electron cryo-microscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum
    • Rockel B., Jakana J., Chiu W., Baumeister W. Electron cryo-microscopy of VAT, the archaeal p97/CDC48 homologue from Thermoplasma acidophilum. J. Mol. Biol. 2002, 317:673-681.
    • (2002) J. Mol. Biol. , vol.317 , pp. 673-681
    • Rockel, B.1    Jakana, J.2    Chiu, W.3    Baumeister, W.4
  • 32
    • 1842576796 scopus 로고    scopus 로고
    • Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47
    • Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S. Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. EMBO J. 2004, 23:1030-1039.
    • (2004) EMBO J. , vol.23 , pp. 1030-1039
    • Dreveny, I.1    Kondo, H.2    Uchiyama, K.3    Shaw, A.4    Zhang, X.5    Freemont, P.S.6
  • 33
    • 60849118366 scopus 로고    scopus 로고
    • Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2
    • Effantin G., Rosenzweig R., Glickman M.H., Steven A.C. Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2. J. Mol. Biol. 2009, 386:1204-1211.
    • (2009) J. Mol. Biol. , vol.386 , pp. 1204-1211
    • Effantin, G.1    Rosenzweig, R.2    Glickman, M.H.3    Steven, A.C.4
  • 34
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch J., Fenton W.A., Furtak K.J., Farr G.W., Horwich A.L. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 2005, 121:1029-1041.
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 35
    • 33746550224 scopus 로고    scopus 로고
    • Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone
    • Thibault G., Tsitrin Y., Davidson T., Gribun A., Houry W.A. Large nucleotide-dependent movement of the N-terminal domain of the ClpX chaperone. EMBO J. 2006, 25:3367-3376.
    • (2006) EMBO J. , vol.25 , pp. 3367-3376
    • Thibault, G.1    Tsitrin, Y.2    Davidson, T.3    Gribun, A.4    Houry, W.A.5
  • 36
    • 70350772363 scopus 로고    scopus 로고
    • Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
    • Glynn S.E., Martin A., Nager A.R., Baker T.A., Sauer R.T. Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 2009, 139:744-756.
    • (2009) Cell , vol.139 , pp. 744-756
    • Glynn, S.E.1    Martin, A.2    Nager, A.R.3    Baker, T.A.4    Sauer, R.T.5
  • 37
    • 79952816898 scopus 로고    scopus 로고
    • Structure and mechanism of the hexameric MecA-ClpC molecular machine
    • Wang F., Mei Z., Qi Y., Yan C., Hu Q., Wang J., Shi Y. Structure and mechanism of the hexameric MecA-ClpC molecular machine. Nature 2011, 471:331-335.
    • (2011) Nature , vol.471 , pp. 331-335
    • Wang, F.1    Mei, Z.2    Qi, Y.3    Yan, C.4    Hu, Q.5    Wang, J.6    Shi, Y.7
  • 38
    • 73649108245 scopus 로고    scopus 로고
    • Dissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domains
    • Zhao C., Matveeva E.A., Ren Q., Whiteheart S.W. Dissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domains. J. Biol. Chem. 2010, 285:761-772.
    • (2010) J. Biol. Chem. , vol.285 , pp. 761-772
    • Zhao, C.1    Matveeva, E.A.2    Ren, Q.3    Whiteheart, S.W.4
  • 39
    • 0041736713 scopus 로고    scopus 로고
    • Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 A resolution
    • Furst J., Sutton R.B., Chen J., Brunger A.T., Grigorieff N. Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 A resolution. EMBO J. 2003, 22:4365-4374.
    • (2003) EMBO J. , vol.22 , pp. 4365-4374
    • Furst, J.1    Sutton, R.B.2    Chen, J.3    Brunger, A.T.4    Grigorieff, N.5
  • 40
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst M., Wendland B., Estepa E.J., Emr S.D. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 1998, 17:2982-2993.
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 42
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story R.M., Steitz T.A. Structure of the recA protein-ADP complex. Nature 1992, 355:374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 43
    • 71449115274 scopus 로고    scopus 로고
    • Both ATPase domains of ClpA are critical for processing of stable protein structures
    • Kress W., Mutschler H., Weber-Ban E. Both ATPase domains of ClpA are critical for processing of stable protein structures. J. Biol. Chem. 2009, 284:31441-31452.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31441-31452
    • Kress, W.1    Mutschler, H.2    Weber-Ban, E.3
  • 44
    • 30044443816 scopus 로고    scopus 로고
    • VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase
    • Gerega A., Rockel B., Peters J., Tamura T., Baumeister W., Zwickl P. VAT, the thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase. J. Biol. Chem. 2005, 280:42856-42862.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42856-42862
    • Gerega, A.1    Rockel, B.2    Peters, J.3    Tamura, T.4    Baumeister, W.5    Zwickl, P.6
  • 46
    • 0037155139 scopus 로고    scopus 로고
    • Roles of the two ATP binding sites of ClpB from Thermus thermophilus
    • Watanabe Y.H., Motohashi K., Yoshida M. Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J. Biol. Chem. 2002, 277:5804-5809.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5804-5809
    • Watanabe, Y.H.1    Motohashi, K.2    Yoshida, M.3
  • 47
    • 0037705402 scopus 로고    scopus 로고
    • Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity
    • Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J. Biol. Chem. 2003, 278:17615-17624.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17615-17624
    • Mogk, A.1    Schlieker, C.2    Strub, C.3    Rist, W.4    Weibezahn, J.5    Bukau, B.6
  • 49
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 1998, 94:525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 50
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai D., Zhao R., Li D., Finkielstein C.V., Chen X.S. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 2004, 119:47-60.
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 51
    • 78149460165 scopus 로고    scopus 로고
    • Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase
    • Chen B., Sysoeva T.A., Chowdhury S., Guo L., De Carlo S., Hanson J.A., Yang H., Nixon B.T. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure 2010, 18:1420-1430.
    • (2010) Structure , vol.18 , pp. 1420-1430
    • Chen, B.1    Sysoeva, T.A.2    Chowdhury, S.3    Guo, L.4    De Carlo, S.5    Hanson, J.A.6    Yang, H.7    Nixon, B.T.8
  • 52
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther B., Onrust R., Sali A., O'Donnell M., Kuriyan J. Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 1997, 91:335-345.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 53
    • 42949164124 scopus 로고    scopus 로고
    • Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change
    • Davies J.M., Brunger A.T., Weis W.I. Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. Structure 2008, 16:715-726.
    • (2008) Structure , vol.16 , pp. 715-726
    • Davies, J.M.1    Brunger, A.T.2    Weis, W.I.3
  • 54
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • 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. 1999, 9:27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 55
    • 0026544877 scopus 로고
    • Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9A resolution. A model for a catalytic transition state
    • Muller C.W., Schulz G.E. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9A resolution. A model for a catalytic transition state. J. Mol. Biol. 1992, 224:159-177.
    • (1992) J. Mol. Biol. , vol.224 , pp. 159-177
    • Muller, C.W.1    Schulz, G.E.2
  • 56
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • Ogura T., Whiteheart S.W., Wilkinson A.J. Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. J. Struct. Biol. 2004, 146:106-112.
    • (2004) J. Struct. Biol. , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 57
    • 2542443628 scopus 로고    scopus 로고
    • Communication between ClpX and ClpP during substrate processing and degradation
    • Joshi S.A., Hersch G.L., Baker T.A., Sauer R.T. Communication between ClpX and ClpP during substrate processing and degradation. Nat. Struct. Mol. Biol. 2004, 11:404-411.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 404-411
    • Joshi, S.A.1    Hersch, G.L.2    Baker, T.A.3    Sauer, R.T.4
  • 58
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata K., Inagawa T., Wilkinson A.J., Tatsuta T., Ogura T. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 1999, 274:26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 59
    • 28844446882 scopus 로고    scopus 로고
    • Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein
    • Wang Q., Song C., Irizarry L., Dai R., Zhang X., Li C.C. Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein. J. Biol. Chem. 2005, 280:40515-40523.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40515-40523
    • Wang, Q.1    Song, C.2    Irizarry, L.3    Dai, R.4    Zhang, X.5    Li, C.C.6
  • 62
    • 70350734536 scopus 로고    scopus 로고
    • Nucleotide binding and allosteric modulation of the second AAA+ domain of ClpB probed by transient kinetic studies
    • Werbeck N.D., Kellner J.N., Barends T.R., Reinstein J. Nucleotide binding and allosteric modulation of the second AAA+ domain of ClpB probed by transient kinetic studies. Biochemistry 2009, 48:7240-7250.
    • (2009) Biochemistry , vol.48 , pp. 7240-7250
    • Werbeck, N.D.1    Kellner, J.N.2    Barends, T.R.3    Reinstein, J.4
  • 63
    • 75349090585 scopus 로고    scopus 로고
    • ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97
    • Esaki M., Ogura T. ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97. Biochem. Cell Biol. 2010, 88:109-117.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 109-117
    • Esaki, M.1    Ogura, T.2
  • 67
    • 39649122369 scopus 로고    scopus 로고
    • The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly
    • Mackay R.G., Helsen C.W., Tkach J.M., Glover J.R. The C-terminal extension of Saccharomyces cerevisiae Hsp104 plays a role in oligomer assembly. Biochemistry 2008, 47:1918-1927.
    • (2008) Biochemistry , vol.47 , pp. 1918-1927
    • Mackay, R.G.1    Helsen, C.W.2    Tkach, J.M.3    Glover, J.R.4
  • 69
    • 33846286030 scopus 로고    scopus 로고
    • Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
    • Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R. Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J. Mol. Biol. 2007, 366:179-192.
    • (2007) J. Mol. Biol. , vol.366 , pp. 179-192
    • Puri, T.1    Wendler, P.2    Sigala, B.3    Saibil, H.4    Tsaneva, I.R.5
  • 71
    • 33646535590 scopus 로고    scopus 로고
    • Central pore residues mediate the p97/VCP activity required for ERAD
    • DeLaBarre B., Christianson J.C., Kopito R.R., Brunger A.T. Central pore residues mediate the p97/VCP activity required for ERAD. Mol. Cell 2006, 22:451-462.
    • (2006) Mol. Cell , vol.22 , pp. 451-462
    • DeLaBarre, B.1    Christianson, J.C.2    Kopito, R.R.3    Brunger, A.T.4
  • 72
    • 37449008520 scopus 로고    scopus 로고
    • Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
    • Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S., Saibil H.R. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 2007, 131:1366-1377.
    • (2007) Cell , vol.131 , pp. 1366-1377
    • Wendler, P.1    Shorter, J.2    Plisson, C.3    Cashikar, A.G.4    Lindquist, S.5    Saibil, H.R.6
  • 73
    • 35348971984 scopus 로고    scopus 로고
    • ATPase site architecture and helicase mechanism of an archaeal MCM
    • Moreau M.J., McGeoch A.T., Lowe A.R., Itzhaki L.S., Bell S.D. ATPase site architecture and helicase mechanism of an archaeal MCM. Mol. Cell 2007, 28:304-314.
    • (2007) Mol. Cell , vol.28 , pp. 304-314
    • Moreau, M.J.1    McGeoch, A.T.2    Lowe, A.R.3    Itzhaki, L.S.4    Bell, S.D.5
  • 77
    • 79953888421 scopus 로고    scopus 로고
    • Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine
    • Aubin-Tam M.E., Olivares A.O., Sauer R.T., Baker T.A., Lang M.J. Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine. Cell 2011, 145:257-267.
    • (2011) Cell , vol.145 , pp. 257-267
    • Aubin-Tam, M.E.1    Olivares, A.O.2    Sauer, R.T.3    Baker, T.A.4    Lang, M.J.5
  • 78
  • 79
    • 41149169488 scopus 로고    scopus 로고
    • Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB
    • Werbeck N.D., Schlee S., Reinstein J. Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB. J. Mol. Biol. 2008, 378:178-190.
    • (2008) J. Mol. Biol. , vol.378 , pp. 178-190
    • Werbeck, N.D.1    Schlee, S.2    Reinstein, J.3
  • 81
    • 0028077782 scopus 로고
    • Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli
    • Singh S.K., Maurizi M.R. Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli. J. Biol. Chem. 1994, 269:29537-29545.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29537-29545
    • Singh, S.K.1    Maurizi, M.R.2
  • 83
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst M., Sato T.K., Banta L.M., Emr S.D. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 1997, 16:1820-1831.
    • (1997) EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 85
    • 0033959713 scopus 로고    scopus 로고
    • ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking
    • Bishop N., Woodman P. ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Mol. Biol. Cell 2000, 11:227-239.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 227-239
    • Bishop, N.1    Woodman, P.2
  • 86
    • 77958478316 scopus 로고    scopus 로고
    • A specific docking site for DNA polymerase {alpha}-primase on the SV40 helicase is required for viral primosome activity, but helicase activity is dispensable
    • Huang H., Zhao K., Arnett D.R., Fanning E. A specific docking site for DNA polymerase {alpha}-primase on the SV40 helicase is required for viral primosome activity, but helicase activity is dispensable. J. Biol. Chem. 2010, 285:33475-33484.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33475-33484
    • Huang, H.1    Zhao, K.2    Arnett, D.R.3    Fanning, E.4
  • 87
    • 44949197849 scopus 로고    scopus 로고
    • Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase
    • Greenleaf W.B., Shen J., Gai D., Chen X.S. Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase. J. Virol. 2008, 82:6017-6023.
    • (2008) J. Virol. , vol.82 , pp. 6017-6023
    • Greenleaf, W.B.1    Shen, J.2    Gai, D.3    Chen, X.S.4
  • 88
    • 0026062628 scopus 로고
    • Specific mutation of a regulatory site within the ATP-binding region of simian virus 40 large T antigen
    • Weiner B.M., Bradley M.K. Specific mutation of a regulatory site within the ATP-binding region of simian virus 40 large T antigen. J. Virol. 1991, 65:4973-4984.
    • (1991) J. Virol. , vol.65 , pp. 4973-4984
    • Weiner, B.M.1    Bradley, M.K.2
  • 89
    • 0034634334 scopus 로고    scopus 로고
    • Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli
    • Kim K.I., Cheong G.W., Park S.C., Ha J.S., Woo K.M., Choi S.J., Chung C.H. Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. J. Mol. Biol. 2000, 303:655-666.
    • (2000) J. Mol. Biol. , vol.303 , pp. 655-666
    • Kim, K.I.1    Cheong, G.W.2    Park, S.C.3    Ha, J.S.4    Woo, K.M.5    Choi, S.J.6    Chung, C.H.7
  • 90
    • 0030846170 scopus 로고    scopus 로고
    • Trans-Dominant and non-trans-dominant mutant simian virus 40 large T antigens show distinct responses to ATP
    • Castellino A.M., Cantalupo P., Marks I.M., Vartikar J.V., Peden K.W., Pipas J.M. trans-Dominant and non-trans-dominant mutant simian virus 40 large T antigens show distinct responses to ATP. J. Virol. 1997, 71:7549-7559.
    • (1997) J. Virol. , vol.71 , pp. 7549-7559
    • Castellino, A.M.1    Cantalupo, P.2    Marks, I.M.3    Vartikar, J.V.4    Peden, K.W.5    Pipas, J.M.6
  • 91
    • 0023147631 scopus 로고
    • Trans-Dominant defective mutants of simian virus 40 T antigen
    • Farber J.M., Peden K.W., Nathans D. trans-Dominant defective mutants of simian virus 40 T antigen. J. Virol. 1987, 61:436-445.
    • (1987) J. Virol. , vol.61 , pp. 436-445
    • Farber, J.M.1    Peden, K.W.2    Nathans, D.3
  • 92
    • 4444372098 scopus 로고    scopus 로고
    • Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum
    • Besche H., Tamura N., Tamura T., Zwickl P. Mutational analysis of conserved AAA+ residues in the archaeal Lon protease from Thermoplasma acidophilum. FEBS Lett. 2004, 574:161-166.
    • (2004) FEBS Lett. , vol.574 , pp. 161-166
    • Besche, H.1    Tamura, N.2    Tamura, T.3    Zwickl, P.4
  • 93
    • 0026070143 scopus 로고
    • The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription
    • Weiss D.S., Batut J., Klose K.E., Keener J., Kustu S. The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription. Cell 1991, 67:155-167.
    • (1991) Cell , vol.67 , pp. 155-167
    • Weiss, D.S.1    Batut, J.2    Klose, K.E.3    Keener, J.4    Kustu, S.5
  • 94
    • 0032110626 scopus 로고    scopus 로고
    • Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders
    • Perkins G., Diffley J.F. Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders. Mol. Cell 1998, 2:23-32.
    • (1998) Mol. Cell , vol.2 , pp. 23-32
    • Perkins, G.1    Diffley, J.F.2
  • 95
    • 0032143408 scopus 로고    scopus 로고
    • Mutational analysis of the two ATP-binding sites in ClpB, a heat shock protein with protein-activated ATPase activity in Escherichia coli
    • Kim K.I., Woo K.M., Seong I.S., Lee Z.W., Baek S.H., Chung C.H. Mutational analysis of the two ATP-binding sites in ClpB, a heat shock protein with protein-activated ATPase activity in Escherichia coli. Biochem. J. 1998, 333(Pt 3):671-676.
    • (1998) Biochem. J. , vol.333 , Issue.PART 3 , pp. 671-676
    • Kim, K.I.1    Woo, K.M.2    Seong, I.S.3    Lee, Z.W.4    Baek, S.H.5    Chung, C.H.6
  • 97
    • 0033582262 scopus 로고    scopus 로고
    • The Cdc6p nucleotide-binding motif is required for loading mcm proteins onto chromatin
    • Weinreich M., Liang C., Stillman B. The Cdc6p nucleotide-binding motif is required for loading mcm proteins onto chromatin. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:441-446.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 441-446
    • Weinreich, M.1    Liang, C.2    Stillman, B.3
  • 98
    • 0030593512 scopus 로고    scopus 로고
    • Repressor forms of the enhancer-binding protein NrtC: some fail in coupling ATP hydrolysis to open complex formation by sigma 54-holoenzyme
    • North A.K., Weiss D.S., Suzuki H., Flashner Y., Kustu S. Repressor forms of the enhancer-binding protein NrtC: some fail in coupling ATP hydrolysis to open complex formation by sigma 54-holoenzyme. J. Mol. Biol. 1996, 260:317-331.
    • (1996) J. Mol. Biol. , vol.260 , pp. 317-331
    • North, A.K.1    Weiss, D.S.2    Suzuki, H.3    Flashner, Y.4    Kustu, S.5
  • 99
    • 1942503398 scopus 로고    scopus 로고
    • Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader
    • Seybert A., Wigley D.B. Distinct roles for ATP binding and hydrolysis at individual subunits of an archaeal clamp loader. EMBO J. 2004, 23:1360-1371.
    • (2004) EMBO J. , vol.23 , pp. 1360-1371
    • Seybert, A.1    Wigley, D.B.2
  • 100
    • 65649123769 scopus 로고    scopus 로고
    • Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii
    • Zhang F., Wu Z., Zhang P., Tian G., Finley D., Shi Y. Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol. Cell 2009, 34:485-496.
    • (2009) Mol. Cell , vol.34 , pp. 485-496
    • Zhang, F.1    Wu, Z.2    Zhang, P.3    Tian, G.4    Finley, D.5    Shi, Y.6
  • 101
    • 0034975987 scopus 로고    scopus 로고
    • Mutational analysis of conserved sequence motifs in the budding yeast Cdc6 protein
    • Schepers A., Diffley J.F. Mutational analysis of conserved sequence motifs in the budding yeast Cdc6 protein. J. Mol. Biol. 2001, 308:597-608.
    • (2001) J. Mol. Biol. , vol.308 , pp. 597-608
    • Schepers, A.1    Diffley, J.F.2
  • 102
    • 0033583219 scopus 로고    scopus 로고
    • The essential role of Saccharomyces cerevisiae CDC6 nucleotide-binding site in cell growth, DNA synthesis, and Orc1 association
    • Wang B., Feng L., Hu Y., Huang S.H., Reynolds C.P., Wu L., Jong A.Y. The essential role of Saccharomyces cerevisiae CDC6 nucleotide-binding site in cell growth, DNA synthesis, and Orc1 association. J. Biol. Chem. 1999, 274:8291-8298.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8291-8298
    • Wang, B.1    Feng, L.2    Hu, Y.3    Huang, S.H.4    Reynolds, C.P.5    Wu, L.6    Jong, A.Y.7
  • 103
    • 34547963061 scopus 로고    scopus 로고
    • ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea
    • Horwitz A.A., Navon A., Groll M., Smith D.M., Reis C., Goldberg A.L. ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea. J. Biol. Chem. 2007, 282:22921-22929.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22921-22929
    • Horwitz, A.A.1    Navon, A.2    Groll, M.3    Smith, D.M.4    Reis, C.5    Goldberg, A.L.6
  • 104
    • 0037013301 scopus 로고    scopus 로고
    • Functions of sensor 1 and sensor 2 regions of Saccharomyces cerevisiae Cdc6p in vivo and in vitro
    • Takahashi N., Tsutsumi S., Tsuchiya T., Stillman B., Mizushima T. Functions of sensor 1 and sensor 2 regions of Saccharomyces cerevisiae Cdc6p in vivo and in vitro. J. Biol. Chem. 2002, 277:16033-16040.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16033-16040
    • Takahashi, N.1    Tsutsumi, S.2    Tsuchiya, T.3    Stillman, B.4    Mizushima, T.5
  • 106
    • 0035164972 scopus 로고    scopus 로고
    • Roles of the two ClpC ATP binding sites in the regulation of competence and the stress response
    • Turgay K., Persuh M., Hahn J., Dubnau D. Roles of the two ClpC ATP binding sites in the regulation of competence and the stress response. Mol. Microbiol. 2001, 42:717-727.
    • (2001) Mol. Microbiol. , vol.42 , pp. 717-727
    • Turgay, K.1    Persuh, M.2    Hahn, J.3    Dubnau, D.4
  • 107
    • 31444442284 scopus 로고    scopus 로고
    • Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides
    • Bosl B., Grimminger V., Walter S. Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J. Biol. Chem. 2005, 280:38170-38176.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38170-38176
    • Bosl, B.1    Grimminger, V.2    Walter, S.3
  • 108
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell D.A., Kowal A.S., Singer M.A., Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature 1994, 372:475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 109
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell D.A., Kowal A.S., Lindquist S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem. 1994, 269:4480-4487.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 110
    • 4143115896 scopus 로고    scopus 로고
    • Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation
    • Tkach J.M., Glover J.R. Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J. Biol. Chem. 2004, 279:35692-35701.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35692-35701
    • Tkach, J.M.1    Glover, J.R.2
  • 111
    • 0035824878 scopus 로고    scopus 로고
    • Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein
    • Krzewska J., Konopa G., Liberek K. Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein. J. Mol. Biol. 2001, 314:901-910.
    • (2001) J. Mol. Biol. , vol.314 , pp. 901-910
    • Krzewska, J.1    Konopa, G.2    Liberek, K.3
  • 113
    • 46649111025 scopus 로고    scopus 로고
    • Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase
    • Briggs L.C., Baldwin G.S., Miyata N., Kondo H., Zhang X., Freemont P.S. Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase. J. Biol. Chem. 2008, 283:13745-13752.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13745-13752
    • Briggs, L.C.1    Baldwin, G.S.2    Miyata, N.3    Kondo, H.4    Zhang, X.5    Freemont, P.S.6
  • 114
    • 21244482459 scopus 로고    scopus 로고
    • Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine
    • Hersch G.L., Burton R.E., Bolon D.N., Baker T.A., Sauer R.T. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 2005, 121:1017-1027.
    • (2005) Cell , vol.121 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 115
    • 0037080165 scopus 로고    scopus 로고
    • Uncoupling the ATPase activity of the N-ethylmaleimide sensitive factor (NSF) from 20S complex disassembly
    • Matveeva E.A., May A.P., He P., Whiteheart S.W. Uncoupling the ATPase activity of the N-ethylmaleimide sensitive factor (NSF) from 20S complex disassembly. Biochemistry 2002, 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
  • 116
    • 0037423187 scopus 로고    scopus 로고
    • ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity
    • 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. 2003, 278:3648-3655.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3648-3655
    • Song, C.1    Wang, Q.2    Li, C.C.3
  • 117
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman G.D., O'Donnell M., Kuriyan J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 2004, 429:724-730.
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 118
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • Akiyama Y., Kihara A., Tokuda H., Ito K. FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J. Biol. Chem. 1996, 271:31196-31201.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 119
    • 0037022645 scopus 로고    scopus 로고
    • Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding
    • Hattendorf D.A., Lindquist S.L. Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:2732-2737.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2732-2737
    • Hattendorf, D.A.1    Lindquist, S.L.2
  • 120
    • 0030566835 scopus 로고    scopus 로고
    • Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli
    • Shin D.H., Yoo S.J., Shim Y.K., Seol J.H., Kang M.S., Chung C.H. Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli. FEBS Lett. 1996, 398:151-154.
    • (1996) FEBS Lett. , vol.398 , pp. 151-154
    • Shin, D.H.1    Yoo, S.J.2    Shim, Y.K.3    Seol, J.H.4    Kang, M.S.5    Chung, C.H.6
  • 121
    • 0033520395 scopus 로고    scopus 로고
    • Role of walker motif A of RuvB protein in promoting branch migration of holliday junctions. Walker motif a mutations affect Atp binding, Atp hydrolyzing, and DNA binding activities of Ruvb
    • Hishida T., Iwasaki H., Yagi T., Shinagawa H. Role of walker motif A of RuvB protein in promoting branch migration of holliday junctions. Walker motif a mutations affect Atp binding, Atp hydrolyzing, and DNA binding activities of Ruvb. J. Biol. Chem. 1999, 274:25335-25342.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25335-25342
    • Hishida, T.1    Iwasaki, H.2    Yagi, T.3    Shinagawa, H.4
  • 122
    • 0037515607 scopus 로고    scopus 로고
    • Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine
    • Johnson A., O'Donnell M. Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine. J. Biol. Chem. 2003, 278:14406-14413.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14406-14413
    • Johnson, A.1    O'Donnell, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.