-
2
-
-
33745041480
-
Evolutionary relationships and structural mechanisms of AAA+ proteins
-
Erzberger J.P., and Berger J.M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu Rev Biophys Biomol Struct 35 (2006) 93-114
-
(2006)
Annu Rev Biophys Biomol Struct
, vol.35
, pp. 93-114
-
-
Erzberger, J.P.1
Berger, J.M.2
-
3
-
-
27144474906
-
Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
-
In this paper, the authors constructed single-chain pseudo-hexamers consisting of combinations of active or inactive ClpX subunits. They were able to show, using these constructs, that the ClpX power stroke results from ATP hydrolysis in a single subunit and consequently, for ClpX at least, concerted or sequential ATP hydrolysis is not required to translocate the polypeptide.
-
Martin A., Baker T.A., and Sauer R.T. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437 (2005) 1115-1120. In this paper, the authors constructed single-chain pseudo-hexamers consisting of combinations of active or inactive ClpX subunits. They were able to show, using these constructs, that the ClpX power stroke results from ATP hydrolysis in a single subunit and consequently, for ClpX at least, concerted or sequential ATP hydrolysis is not required to translocate the polypeptide.
-
(2005)
Nature
, vol.437
, pp. 1115-1120
-
-
Martin, A.1
Baker, T.A.2
Sauer, R.T.3
-
4
-
-
25844525796
-
Cellular functions, mechanism of action, and regulation of FtsH protease
-
Ito K., and Akiyama Y. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu Rev Microbiol 59 (2005) 211-231
-
(2005)
Annu Rev Microbiol
, vol.59
, pp. 211-231
-
-
Ito, K.1
Akiyama, Y.2
-
5
-
-
33744552902
-
Structure of the whole cytosolic region of ATP-dependent protease FtsH
-
In this and the following paper, the structure of the cytosolic part of FtsH from different thermophiles is reported. The structures are similar, though in one case two, and in the other case three, distinct conformations are observed. They agree in that the protease domain forms a hexamer whereas the AAA+ domains (which all have bound ADP) vary in orientation, suggesting a mechanism whereby threading of the polypeptide into the protease active site can occur.
-
Suno R., Niwa H., Tsuchiya D., Zhang X., Yoshida M., and Morikawa K. Structure of the whole cytosolic region of ATP-dependent protease FtsH. Mol Cell 22 (2006) 575-585. In this and the following paper, the structure of the cytosolic part of FtsH from different thermophiles is reported. The structures are similar, though in one case two, and in the other case three, distinct conformations are observed. They agree in that the protease domain forms a hexamer whereas the AAA+ domains (which all have bound ADP) vary in orientation, suggesting a mechanism whereby threading of the polypeptide into the protease active site can occur.
-
(2006)
Mol Cell
, vol.22
, pp. 575-585
-
-
Suno, R.1
Niwa, H.2
Tsuchiya, D.3
Zhang, X.4
Yoshida, M.5
Morikawa, K.6
-
7
-
-
0036054289
-
The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 15 Å resolution
-
Krzywda S., Brzozowski A.M., Verma C., Karata K., Ogura T., and Wilkinson A.J. The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 15 Å resolution. Structure 10 (2002) 1073-1083
-
(2002)
Structure
, 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
-
8
-
-
0036773132
-
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., and Morikawa K. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure 10 (2002) 1415-1423
-
(2002)
Structure
, vol.10
, pp. 1415-1423
-
-
Niwa, H.1
Tsuchiya, D.2
Makyio, H.3
Yoshida, M.4
Morikawa, K.5
-
9
-
-
33749257470
-
Going through the motions: the ATPase cycle of p97
-
Pye V.E., Dreveny I., Briggs L.C., Sands C., Beuron F., Zhang X., and Freemont P.S. Going through the motions: the ATPase cycle of p97. J Struct Biol 156 (2006) 12-28
-
(2006)
J Struct Biol
, vol.156
, pp. 12-28
-
-
Pye, V.E.1
Dreveny, I.2
Briggs, L.C.3
Sands, C.4
Beuron, F.5
Zhang, X.6
Freemont, P.S.7
-
10
-
-
13844253945
-
Conformational changes of p97 during nucleotide hydrolysis determined by small-angle X-ray scattering
-
x, and ADP states, indicating different shapes, especially with regard to the positioning of the N-domain.
-
x, and ADP states, indicating different shapes, especially with regard to the positioning of the N-domain.
-
(2005)
Structure
, vol.13
, pp. 183-195
-
-
Davies, J.M.1
Tsuruta, H.2
May, A.P.3
Weis, W.I.4
-
11
-
-
14644415865
-
Nucleotide dependent motion and mechanism of action of p97/VCP
-
3 and ADP-bound states of p97 were explored using X-ray crystallography. Despite the relatively low resolution of the structures, a description of the relative domain movements between states is given.
-
3 and ADP-bound states of p97 were explored using X-ray crystallography. Despite the relatively low resolution of the structures, a description of the relative domain movements between states is given.
-
(2005)
J Mol Biol
, vol.347
, pp. 437-452
-
-
DeLaBarre, B.1
Brunger, A.T.2
-
12
-
-
33846277910
-
Structural insights into the p97-Ufd1-Np14 complex
-
In this paper, using negative stain EM single-particle averaging, the authors show that only one Ufd1-Np14 complex binds per p97 hexamer, and that ubiquitin binds to the Ufd1 part of the adaptor complex.
-
Pye V.E., Beuron F., Keetch C.A., McKeown C., Robinson C.V., Meyer H.H., Zhang Z., and Freemont P.S. Structural insights into the p97-Ufd1-Np14 complex. Proc Natl Acad Sci U S A 104 (2007) 467-472. In this paper, using negative stain EM single-particle averaging, the authors show that only one Ufd1-Np14 complex binds per p97 hexamer, and that ubiquitin binds to the Ufd1 part of the adaptor complex.
-
(2007)
Proc Natl Acad Sci U S A
, vol.104
, pp. 467-472
-
-
Pye, V.E.1
Beuron, F.2
Keetch, C.A.3
McKeown, C.4
Robinson, C.V.5
Meyer, H.H.6
Zhang, Z.7
Freemont, P.S.8
-
13
-
-
28844446882
-
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., and Li C.C. Multifunctional roles of the conserved Arg residues in the second region of homology of p97/valosin-containing protein. J Biol Chem 280 (2005) 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
-
14
-
-
21744460209
-
Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
-
Park S., Isaacson R., Kim H.T., Silver P.A., and Wagner G. Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13 (2005) 995-1005
-
(2005)
Structure
, vol.13
, pp. 995-1005
-
-
Park, S.1
Isaacson, R.2
Kim, H.T.3
Silver, P.A.4
Wagner, G.5
-
15
-
-
34547097772
-
-
Isaacson RL, Pye VE, Simpson P, Meyer HH, Zhang X, Freemont PS, Matthews S: Detailed structural insight into the p97-Npl4-Ufd1 interface. J Biol Chem 2007 [Epub ahead of print].
-
-
-
-
16
-
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33646582995
-
Conformational changes in the AAA ATPase p97-p47 adaptor complex
-
In this paper, the differences in shape of the p97/p47 complex in ADP-bound and AMPNP-bound states are described using cryo-EM single-particle averaging. The complex has a 6:3 stoichiometry with clear differences in the positioning of the N-domains and the p47 adaptor.
-
Beuron F., Dreveny I., Yuan X., Pye V.E., McKeown C., Briggs L.C., Cliff M.J., Kaneko Y., Wallis R., Isaacson R.L., et al. Conformational changes in the AAA ATPase p97-p47 adaptor complex. EMBO J 25 (2006) 1967-1976. In this paper, the differences in shape of the p97/p47 complex in ADP-bound and AMPNP-bound states are described using cryo-EM single-particle averaging. The complex has a 6:3 stoichiometry with clear differences in the positioning of the N-domains and the p47 adaptor.
-
(2006)
EMBO J
, vol.25
, pp. 1967-1976
-
-
Beuron, F.1
Dreveny, I.2
Yuan, X.3
Pye, V.E.4
McKeown, C.5
Briggs, L.C.6
Cliff, M.J.7
Kaneko, Y.8
Wallis, R.9
Isaacson, R.L.10
-
17
-
-
33646127577
-
Molecular chaperones and protein quality control
-
Bukau B., Weissman J., and Horwich A. Molecular chaperones and protein quality control. Cell 125 (2006) 443-451
-
(2006)
Cell
, vol.125
, pp. 443-451
-
-
Bukau, B.1
Weissman, J.2
Horwich, A.3
-
18
-
-
33846231395
-
M domains couple the ClpB threading motor with the DnaK chaperone activity
-
Haslberger T., Weibezahn J., Zahn R., Lee S., Tsai F.T., Bukau B., and Mogk A. M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell 25 (2007) 247-260
-
(2007)
Mol Cell
, vol.25
, pp. 247-260
-
-
Haslberger, T.1
Weibezahn, J.2
Zahn, R.3
Lee, S.4
Tsai, F.T.5
Bukau, B.6
Mogk, A.7
-
19
-
-
27844460608
-
Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity
-
Beinker P., Schlee S., Auvula R., and Reinstein J. Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity. J Biol Chem 280 (2005) 37965-37973
-
(2005)
J Biol Chem
, vol.280
, pp. 37965-37973
-
-
Beinker, P.1
Schlee, S.2
Auvula, R.3
Reinstein, J.4
-
20
-
-
33846188909
-
Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB
-
In this paper, cryo-EM reconstructions of ClpB in Apo, ADP, and AMPPNP states are described. The ATP state was investigated using a double Walker B mutation that binds but does not hydrolyze ATP. Arguably the most important finding is that ATP is essential for high-affinity substrate binding, and the structural reason for this is described.
-
Lee S., Choi J.M., and Tsai F.T. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol Cell 25 (2007) 261-271. In this paper, cryo-EM reconstructions of ClpB in Apo, ADP, and AMPPNP states are described. The ATP state was investigated using a double Walker B mutation that binds but does not hydrolyze ATP. Arguably the most important finding is that ATP is essential for high-affinity substrate binding, and the structural reason for this is described.
-
(2007)
Mol Cell
, vol.25
, pp. 261-271
-
-
Lee, S.1
Choi, J.M.2
Tsai, F.T.3
-
21
-
-
33750085293
-
The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97
-
Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N., Shirakawa M., and Hiroaki H. The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97. FEBS J 273 (2006) 4959-4971
-
(2006)
FEBS J
, vol.273
, pp. 4959-4971
-
-
Shiozawa, K.1
Goda, N.2
Shimizu, T.3
Mizuguchi, K.4
Kondo, N.5
Shimozawa, N.6
Shirakawa, M.7
Hiroaki, H.8
-
22
-
-
27144444327
-
Structural and mechanistic studies of VPS4 proteins
-
This paper reports that the crystal structure of the AAA+ region of human VPS4B shows a β-domain insert into the α subdomain which is shown to be involved in binding to the adaptor protein LIP5. ATP appears necessary to form higher oligomers, which are then able to bind the adaptors.
-
Scott A., Chung H.Y., Gonciarz-Swiatek M., Hill G.C., Whitby F.G., Gaspar J., Holton J.M., Viswanathan R., Ghaffarian S., Hill C.P., and Sundquist W.I. Structural and mechanistic studies of VPS4 proteins. EMBO J 24 (2005) 3658-3669. This paper reports that the crystal structure of the AAA+ region of human VPS4B shows a β-domain insert into the α subdomain which is shown to be involved in binding to the adaptor protein LIP5. ATP appears necessary to form higher oligomers, which are then able to bind the adaptors.
-
(2005)
EMBO J
, vol.24
, pp. 3658-3669
-
-
Scott, A.1
Chung, H.Y.2
Gonciarz-Swiatek, M.3
Hill, G.C.4
Whitby, F.G.5
Gaspar, J.6
Holton, J.M.7
Viswanathan, R.8
Ghaffarian, S.9
Hill, C.P.10
Sundquist, W.I.11
-
23
-
-
25444442371
-
Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A
-
Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J., and Sundquist W.I. Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A. Proc Natl Acad Sci U S A 102 (2005) 13813-13818
-
(2005)
Proc Natl Acad Sci U S A
, vol.102
, pp. 13813-13818
-
-
Scott, A.1
Gaspar, J.2
Stuchell-Brereton, M.D.3
Alam, S.L.4
Skalicky, J.J.5
Sundquist, W.I.6
-
24
-
-
33846895023
-
Bacterial enhancer-binding proteins: unlocking sigma54-dependent gene transcription
-
Rappas M., Bose D., and Zhang X. Bacterial enhancer-binding proteins: unlocking sigma54-dependent gene transcription. Curr Opin Struct Biol 17 (2007) 110-116
-
(2007)
Curr Opin Struct Biol
, vol.17
, pp. 110-116
-
-
Rappas, M.1
Bose, D.2
Zhang, X.3
-
25
-
-
25144472529
-
Negative regulation of AAA+ ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria
-
Doucleff M., Chen B., Maris A.E., Wemmer D.E., Kondrashkina E., and Nixon B.T. Negative regulation of AAA+ ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria. J Mol Biol 353 (2005) 242-255
-
(2005)
J Mol Biol
, vol.353
, pp. 242-255
-
-
Doucleff, M.1
Chen, B.2
Maris, A.E.3
Wemmer, D.E.4
Kondrashkina, E.5
Nixon, B.T.6
-
28
-
-
33845919591
-
Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator
-
Joly N., Schumacher J., and Buck M. Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator. J Biol Chem 281 (2006) 34997-35007
-
(2006)
J Biol Chem
, vol.281
, pp. 34997-35007
-
-
Joly, N.1
Schumacher, J.2
Buck, M.3
-
29
-
-
33344469160
-
Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF
-
54 subunit of the RNAP. When ATP is bound changes in the orientation of the linker between β2 and α3 result in destabilization of this conformation.
-
54 subunit of the RNAP. When ATP is bound changes in the orientation of the linker between β2 and α3 result in destabilization of this conformation.
-
(2006)
J Mol Biol
, vol.357
, pp. 481-492
-
-
Rappas, M.1
Schumacher, J.2
Niwa, H.3
Buck, M.4
Zhang, X.5
-
30
-
-
34047267824
-
ATP ground- and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54
-
Chen B., Doucleff M., Wemmer D.E., De Carlo S., Huang H.H., Nogales E., Hoover T.R., Kondrashkina E., Guo L., and Nixon B.T. ATP ground- and transition states of bacterial enhancer binding AAA+ ATPases support complex formation with their target protein, sigma54. Structure 15 (2007) 429-440
-
(2007)
Structure
, vol.15
, pp. 429-440
-
-
Chen, B.1
Doucleff, M.2
Wemmer, D.E.3
De Carlo, S.4
Huang, H.H.5
Nogales, E.6
Hoover, T.R.7
Kondrashkina, E.8
Guo, L.9
Nixon, B.T.10
-
31
-
-
20144366027
-
Structural insights into the activity of enhancer-binding proteins
-
Rappas M., Schumacher J., Beuron F., Niwa H., Bordes P., Wigneshweraraj S., Keetch C.A., Robinson C.V., Buck M., and Zhang X. Structural insights into the activity of enhancer-binding proteins. Science 307 (2005) 1972-1975
-
(2005)
Science
, vol.307
, pp. 1972-1975
-
-
Rappas, M.1
Schumacher, J.2
Beuron, F.3
Niwa, H.4
Bordes, P.5
Wigneshweraraj, S.6
Keetch, C.A.7
Robinson, C.V.8
Buck, M.9
Zhang, X.10
-
32
-
-
34248206721
-
Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of sigma 54-RNA polymerase
-
Schumacher J., Joly N., Rappas M., Bradley D., Wigneshweraraj S.R., Zhang X., and Buck M. Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of sigma 54-RNA polymerase. J Biol Chem 282 (2007) 9825-9833
-
(2007)
J Biol Chem
, vol.282
, pp. 9825-9833
-
-
Schumacher, J.1
Joly, N.2
Rappas, M.3
Bradley, D.4
Wigneshweraraj, S.R.5
Zhang, X.6
Buck, M.7
-
33
-
-
33847704586
-
A role for the conserved GAFTGA motif of AAA+ transcription activators in sensing promoter DNA conformation
-
Dago A.E., Wigneshweraraj S.R., Buck M., and Morett E. A role for the conserved GAFTGA motif of AAA+ transcription activators in sensing promoter DNA conformation. J Biol Chem 282 (2007) 1087-1097
-
(2007)
J Biol Chem
, vol.282
, pp. 1087-1097
-
-
Dago, A.E.1
Wigneshweraraj, S.R.2
Buck, M.3
Morett, E.4
-
34
-
-
33846007717
-
Crystal structure of the human AAA+ protein RuvBL1
-
This paper reports that the crystal structure of human RuvBL1 shows, in contrast to the prokaryotic RuvB protein, an extra DNA/RNA-binding domain of unknown function, inserted in the α/β subdomain of the AAA+ core.
-
Matias P.M., Gorynia S., Donner P., and Carrondo M.A. Crystal structure of the human AAA+ protein RuvBL1. J Biol Chem 281 (2006) 38918-38929. This paper reports that the crystal structure of human RuvBL1 shows, in contrast to the prokaryotic RuvB protein, an extra DNA/RNA-binding domain of unknown function, inserted in the α/β subdomain of the AAA+ core.
-
(2006)
J Biol Chem
, vol.281
, pp. 38918-38929
-
-
Matias, P.M.1
Gorynia, S.2
Donner, P.3
Carrondo, M.A.4
-
35
-
-
33846286030
-
Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex
-
Puri T., Wendler P., Sigala B., Saibil H., and Tsaneva I.R. Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex. J Mol Biol 366 (2007) 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
-
36
-
-
22244478079
-
Cellular DNA replicases: components and dynamics at the replication fork
-
Johnson A., and O'Donnell M. Cellular DNA replicases: components and dynamics at the replication fork. Annu Rev Biochem 74 (2005) 283-315
-
(2005)
Annu Rev Biochem
, vol.74
, pp. 283-315
-
-
Johnson, A.1
O'Donnell, M.2
-
37
-
-
33746375404
-
Mechanism of DNA translocation in a replicative hexameric helicase
-
In this paper, the crystal structure of the papillomavirus E1 helicase in complex with single-stranded DNA shows the DNA in the central pore of the hexameric ring. Observed variations in the orientation of the DNA-binding hairpin lead to the suggestion that the helicase functions in a sequential manner such that, in a complete cycle, each protomer binds, and hydrolyzes, ATP, releases ADP and translocates one nucleotide through the pore.
-
Enemark E.J., and Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442 (2006) 270-445. In this paper, the crystal structure of the papillomavirus E1 helicase in complex with single-stranded DNA shows the DNA in the central pore of the hexameric ring. Observed variations in the orientation of the DNA-binding hairpin lead to the suggestion that the helicase functions in a sequential manner such that, in a complete cycle, each protomer binds, and hydrolyzes, ATP, releases ADP and translocates one nucleotide through the pore.
-
(2006)
Nature
, vol.442
, pp. 270-445
-
-
Enemark, E.J.1
Joshua-Tor, L.2
-
38
-
-
33746860263
-
Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
-
1 symmetry. The bound nucleotide mimics ATP, which is known to be required for selfassembly of DnaA at replication origins. This spiral AAA+ assembly occurs in the replication initiators in all three domains of life.
-
1 symmetry. The bound nucleotide mimics ATP, which is known to be required for selfassembly of DnaA at replication origins. This spiral AAA+ assembly occurs in the replication initiators in all three domains of life.
-
(2006)
Nat Struct Mol Biol
, vol.13
, pp. 676-683
-
-
Erzberger, J.P.1
Mott, M.L.2
Berger, J.M.3
-
39
-
-
33746800642
-
Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex
-
Clarey M.G., Erzberger J.P., Grob P., Leschziner A.E., Berger J.M., Nogales E., and Botchan M. Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex. Nat Struct Mol Biol 13 (2006) 684-690
-
(2006)
Nat Struct Mol Biol
, vol.13
, pp. 684-690
-
-
Clarey, M.G.1
Erzberger, J.P.2
Grob, P.3
Leschziner, A.E.4
Berger, J.M.5
Nogales, E.6
Botchan, M.7
-
40
-
-
23044464806
-
Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR
-
Sallai L., and Tucker P.A. Crystal structure of the central and C-terminal domain of the sigma(54)-activator ZraR. J Struct Biol 151 (2005) 160-170
-
(2005)
J Struct Biol
, vol.151
, pp. 160-170
-
-
Sallai, L.1
Tucker, P.A.2
-
41
-
-
33749266161
-
Structural studies of the archaeal MCM complex in different functional states
-
Costa A., Pape T., van Heel M., Brick P., Patwardhan A., and Onesti S. Structural studies of the archaeal MCM complex in different functional states. J Struct Biol 156 (2006) 210-219
-
(2006)
J Struct Biol
, vol.156
, pp. 210-219
-
-
Costa, A.1
Pape, T.2
van Heel, M.3
Brick, P.4
Patwardhan, A.5
Onesti, S.6
-
42
-
-
33751534800
-
The dynein family at a glance
-
Hook P., and Vallee R.B. The dynein family at a glance. J Cell Sci 119 (2006) 4369-4371
-
(2006)
J Cell Sci
, vol.119
, pp. 4369-4371
-
-
Hook, P.1
Vallee, R.B.2
-
43
-
-
3242809790
-
25 Angstrom resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring
-
Samso M., and Koonce M.P. 25 Angstrom resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring. J Mol Biol 340 (2004) 1059-1072
-
(2004)
J Mol Biol
, vol.340
, pp. 1059-1072
-
-
Samso, M.1
Koonce, M.P.2
-
44
-
-
33644957493
-
A flexible linkage between the dynein motor and its cargo
-
Meng X., Samso M., and Koonce M.P. A flexible linkage between the dynein motor and its cargo. J Mol Biol 357 (2006) 701-706
-
(2006)
J Mol Biol
, vol.357
, pp. 701-706
-
-
Meng, X.1
Samso, M.2
Koonce, M.P.3
-
45
-
-
33845507258
-
A structural model reveals energy transduction in dynein
-
In this paper, a structural model of the force generating mechanism of the motor protein dynein is proposed based on recent EM reconstructions and homology models of the different domains.
-
Serohijos A.W., Chen Y., Ding F., Elston T.C., and Dokholyan N.V. A structural model reveals energy transduction in dynein. Proc Natl Acad Sci U S A 103 (2006) 18540-18545. In this paper, a structural model of the force generating mechanism of the motor protein dynein is proposed based on recent EM reconstructions and homology models of the different domains.
-
(2006)
Proc Natl Acad Sci U S A
, vol.103
, pp. 18540-18545
-
-
Serohijos, A.W.1
Chen, Y.2
Ding, F.3
Elston, T.C.4
Dokholyan, N.V.5
-
46
-
-
33747598723
-
The molecular architecture of axonemes revealed by cryoelectron tomography
-
Nicastro D., Schwartz C., Pierson J., Gaudette R., Porter M.E., and McIntosh J.R. The molecular architecture of axonemes revealed by cryoelectron tomography. Science 313 (2006) 944-948
-
(2006)
Science
, vol.313
, pp. 944-948
-
-
Nicastro, D.1
Schwartz, C.2
Pierson, J.3
Gaudette, R.4
Porter, M.E.5
McIntosh, J.R.6
-
47
-
-
33845214634
-
Two modes of microtubule sliding driven by cytoplasmic dynein
-
Shima T., Kon T., Imamula K., Ohkura R., and Sutoh K. Two modes of microtubule sliding driven by cytoplasmic dynein. Proc Natl Acad Sci U S A 103 (2006) 17736-17740
-
(2006)
Proc Natl Acad Sci U S A
, vol.103
, pp. 17736-17740
-
-
Shima, T.1
Kon, T.2
Imamula, K.3
Ohkura, R.4
Sutoh, K.5
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