-
1
-
-
31344467469
-
The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes
-
Bewley M.C., Graziano V., Griffin K., and Flanagan J.M. The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes. J. Struct. Biol. 153 (2006) 113-128
-
(2006)
J. Struct. Biol.
, vol.153
, pp. 113-128
-
-
Bewley, M.C.1
Graziano, V.2
Griffin, K.3
Flanagan, J.M.4
-
3
-
-
0034677361
-
The structures of HsIU and the ATP-dependent protease HsIU-HsIV
-
Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., and Huber R. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature 403 (2000) 800-805
-
(2000)
Nature
, vol.403
, pp. 800-805
-
-
Bochtler, M.1
Hartmann, C.2
Song, H.K.3
Bourenkov, G.P.4
Bartunik, H.D.5
Huber, R.6
-
4
-
-
48149085922
-
Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop
-
Bohon J., Jennings L.D., Phillips C.M., Licht S., and Chance M.R. Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop. Structure 16 (2008) 1157-1165
-
(2008)
Structure
, vol.16
, pp. 1157-1165
-
-
Bohon, J.1
Jennings, L.D.2
Phillips, C.M.3
Licht, S.4
Chance, M.R.5
-
5
-
-
1242271992
-
Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study
-
Bolon D.N., Wah D.A., Hersch G.L., Baker T.A., and Sauer R.T. Bivalent tethering of SspB to ClpXP is required for efficient substrate delivery: a protein-design study. Mol. Cell 13 (2004) 443-449
-
(2004)
Mol. Cell
, vol.13
, pp. 443-449
-
-
Bolon, D.N.1
Wah, D.A.2
Hersch, G.L.3
Baker, T.A.4
Sauer, R.T.5
-
6
-
-
0035875890
-
Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
-
Burton R.E., Siddiqui S.M., Kim Y.I., Baker T.A., and Sauer R.T. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J. 20 (2001) 3092-3100
-
(2001)
EMBO J.
, vol.20
, pp. 3092-3100
-
-
Burton, R.E.1
Siddiqui, S.M.2
Kim, Y.I.3
Baker, T.A.4
Sauer, R.T.5
-
7
-
-
27144502022
-
Control of peptide product sizes by the energy-dependent protease ClpAP
-
Choi K.H., and Licht S. Control of peptide product sizes by the energy-dependent protease ClpAP. Biochemistry 44 (2005) 13921-13931
-
(2005)
Biochemistry
, vol.44
, pp. 13921-13931
-
-
Choi, K.H.1
Licht, S.2
-
8
-
-
41249085227
-
The flexible attachment of the N-domains to the ClpA ring body allows their use on demand
-
Cranz-Mileva S., Imkamp F., Kolygo K., Maglica Z., Kress W., and Weber-Ban E. The flexible attachment of the N-domains to the ClpA ring body allows their use on demand. J. Mol. Biol. 378 (2008) 412-424
-
(2008)
J. Mol. Biol.
, vol.378
, pp. 412-424
-
-
Cranz-Mileva, S.1
Imkamp, F.2
Kolygo, K.3
Maglica, Z.4
Kress, W.5
Weber-Ban, E.6
-
9
-
-
0036210995
-
ClpS, a substrate modulator of the ClpAP machine
-
Dougan D.A., Reid B.G., Horwich A.L., and Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9 (2002) 673-683
-
(2002)
Mol. Cell
, vol.9
, pp. 673-683
-
-
Dougan, D.A.1
Reid, B.G.2
Horwich, A.L.3
Bukau, B.4
-
10
-
-
0141957392
-
Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX
-
Dougan D.A., Weber-Ban E., and Bukau B. Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Mol. Cell 12 (2003) 373-380
-
(2003)
Mol. Cell
, vol.12
, pp. 373-380
-
-
Dougan, D.A.1
Weber-Ban, E.2
Bukau, B.3
-
11
-
-
32544432878
-
ClpS is an essential component of the N-end rule pathway in Escherichia coli
-
Erbse A., Schmidt R., Bornemann T., Schneider-Mergener J., Mogk A., Zahn R., Dougan D.A., and Bukau B. ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature 439 (2006) 753-756
-
(2006)
Nature
, vol.439
, pp. 753-756
-
-
Erbse, A.1
Schmidt, R.2
Bornemann, T.3
Schneider-Mergener, J.4
Mogk, A.5
Zahn, R.6
Dougan, D.A.7
Bukau, B.8
-
12
-
-
58149159717
-
Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA
-
Farbman M.E., Gershenson A., and Licht S. Role of a conserved pore residue in the formation of a prehydrolytic high substrate affinity state in the AAA+ chaperone ClpA. Biochemistry 47 (2008) 13497-13505
-
(2008)
Biochemistry
, vol.47
, pp. 13497-13505
-
-
Farbman, M.E.1
Gershenson, A.2
Licht, S.3
-
13
-
-
33845981507
-
Altered specificity of a AAA+ protease
-
Farrell C.M., Baker T.A., and Sauer R.T. Altered specificity of a AAA+ protease. Mol. Cell 25 (2007) 161-166
-
(2007)
Mol. Cell
, vol.25
, pp. 161-166
-
-
Farrell, C.M.1
Baker, T.A.2
Sauer, R.T.3
-
14
-
-
25144452838
-
Cytoplasmic degradation of ssrA-tagged proteins
-
Farrell C.M., Grossman A.D., and Sauer R.T. Cytoplasmic degradation of ssrA-tagged proteins. Mol. Microbiol. 57 (2005) 1750-1761
-
(2005)
Mol. Microbiol.
, vol.57
, pp. 1750-1761
-
-
Farrell, C.M.1
Grossman, A.D.2
Sauer, R.T.3
-
15
-
-
0035845498
-
Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
-
Flynn J.M., Levchenko I., Seidel M., Wickner S.H., Sauer R.T., and Baker T.A. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 10584-10589
-
(2001)
Proc. Natl. Acad. Sci. U.S.A.
, vol.98
, pp. 10584-10589
-
-
Flynn, J.M.1
Levchenko, I.2
Seidel, M.3
Wickner, S.H.4
Sauer, R.T.5
Baker, T.A.6
-
16
-
-
18144426344
-
The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N-termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation
-
Gribun A., Kimber M.S., Ching R., Sprangers R., Fiebig K.M., and Houry W.A. The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N-termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation. J. Biol. Chem. 280 (2005) 16185-16196
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 16185-16196
-
-
Gribun, A.1
Kimber, M.S.2
Ching, R.3
Sprangers, R.4
Fiebig, K.M.5
Houry, W.A.6
-
17
-
-
0037195961
-
Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA
-
Guo F., Esser L., Singh S.K., Maurizi M.R., and Xia D. Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. J. Biol. Chem. 277 (2002) 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
-
18
-
-
0037195418
-
Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
-
Guo F., Maurizi M.R., Esser L., and Xia D. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J. Biol. Chem. 277 (2002) 46743-46752
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 46743-46752
-
-
Guo, F.1
Maurizi, M.R.2
Esser, L.3
Xia, D.4
-
19
-
-
21244482459
-
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., and Sauer R.T. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121 (2005) 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
-
20
-
-
21244480104
-
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., and Horwich A.L. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121 (2005) 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
-
21
-
-
40949141846
-
Distinct structural elements of the adaptor ClpS are required for regulating degradation by ClpAP
-
Hou J.Y., Sauer R.T., and Baker T.A. Distinct structural elements of the adaptor ClpS are required for regulating degradation by ClpAP. Nat. Struct. Mol. Biol. 15 (2008) 288-294
-
(2008)
Nat. Struct. Mol. Biol.
, vol.15
, pp. 288-294
-
-
Hou, J.Y.1
Sauer, R.T.2
Baker, T.A.3
-
22
-
-
33846654174
-
Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1
-
Ingvarsson H., Mate M.J., Hogbom M., Portnoi D., Benaroudj N., Alzari P.M., Ortiz-Lombardia M., and Unge T. Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 249-259
-
(2007)
Acta Crystallogr. D Biol. Crystallogr.
, vol.63
, pp. 249-259
-
-
Ingvarsson, H.1
Mate, M.J.2
Hogbom, M.3
Portnoi, D.4
Benaroudj, N.5
Alzari, P.M.6
Ortiz-Lombardia, M.7
Unge, T.8
-
23
-
-
1242345623
-
The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease
-
Ishikawa T., Maurizi M.R., and Steven A.C. The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease. J. Struct. Biol. 146 (2004) 180-188
-
(2004)
J. Struct. Biol.
, vol.146
, pp. 180-188
-
-
Ishikawa, T.1
Maurizi, M.R.2
Steven, A.C.3
-
24
-
-
54349084780
-
The ClpP N-terminus coordinates substrate access with protease active site reactivity
-
Jennings L.D., Bohon J., Chance M.R., and Licht S. The ClpP N-terminus coordinates substrate access with protease active site reactivity. Biochemistry 47 (2008) 11031-11040
-
(2008)
Biochemistry
, vol.47
, pp. 11031-11040
-
-
Jennings, L.D.1
Bohon, J.2
Chance, M.R.3
Licht, S.4
-
25
-
-
55249118150
-
ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis
-
Jennings L.D., Lun D.S., Medard M., and Licht S. ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis. Biochemistry 47 (2008) 11536-11546
-
(2008)
Biochemistry
, vol.47
, pp. 11536-11546
-
-
Jennings, L.D.1
Lun, D.S.2
Medard, M.3
Licht, S.4
-
26
-
-
7444254844
-
Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP
-
Kang S.G., Maurizi M.R., Thompson M., Mueser T., and Ahvazi B. Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP. J. Struct. Biol. 148 (2004) 338-352
-
(2004)
J. Struct. Biol.
, vol.148
, pp. 338-352
-
-
Kang, S.G.1
Maurizi, M.R.2
Thompson, M.3
Mueser, T.4
Ahvazi, B.5
-
27
-
-
0042329502
-
Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
-
Kenniston J.A., Baker T.A., Fernandez J.M., and Sauer R.T. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114 (2003) 511-520
-
(2003)
Cell
, vol.114
, pp. 511-520
-
-
Kenniston, J.A.1
Baker, T.A.2
Fernandez, J.M.3
Sauer, R.T.4
-
28
-
-
0348010311
-
Crystal structure of ClpX molecular chaperone from Helicobacter pylori
-
Kim D.Y., and Kim K.K. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J. Biol. Chem. 278 (2003) 50664-50670
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 50664-50670
-
-
Kim, D.Y.1
Kim, K.K.2
-
29
-
-
44149116183
-
The structural basis for the activation and peptide recognition of bacterial ClpP
-
Kim D.Y., and Kim K.K. The structural basis for the activation and peptide recognition of bacterial ClpP. J. Mol. Biol. 379 (2008) 760-771
-
(2008)
J. Mol. Biol.
, vol.379
, pp. 760-771
-
-
Kim, D.Y.1
Kim, K.K.2
-
30
-
-
0035122947
-
Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase
-
Kim Y.I., Levchenko I., Fraczkowska K., Woodruff R.V., Sauer R.T., and Baker T.A. Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. Nat. Struct. Biol. 8 (2001) 230-233
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 230-233
-
-
Kim, Y.I.1
Levchenko, I.2
Fraczkowska, K.3
Woodruff, R.V.4
Sauer, R.T.5
Baker, T.A.6
-
31
-
-
33645741669
-
Adaptor protein controlled oligomerization activates the AAA+ protein ClpC
-
Kirstein J., Schlothauer T., Dougan D.A., Lilie H., Tischendorf G., Mogk A., Bukau B., and Turgay K. Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. EMBO J. 25 (2006) 1481-1491
-
(2006)
EMBO J.
, vol.25
, pp. 1481-1491
-
-
Kirstein, J.1
Schlothauer, T.2
Dougan, D.A.3
Lilie, H.4
Tischendorf, G.5
Mogk, A.6
Bukau, B.7
Turgay, K.8
-
32
-
-
70349445398
-
Studying chaperone-proteases using a real-time approach based on FRET
-
Kolygo K., Ranjan N., Kress W., Striebel F., Hollenstein K., Neelsen K., Steiner M., Summer H., and Weber-Ban E. Studying chaperone-proteases using a real-time approach based on FRET. J. Struct. Biol. (2009)
-
(2009)
J. Struct. Biol.
-
-
Kolygo, K.1
Ranjan, N.2
Kress, W.3
Striebel, F.4
Hollenstein, K.5
Neelsen, K.6
Steiner, M.7
Summer, H.8
Weber-Ban, E.9
-
33
-
-
34249734248
-
Assembly pathway of an AAA+ protein: tracking ClpA and ClpAP complex formation in real time
-
Kress W., Mutschler H., and Weber-Ban E. Assembly pathway of an AAA+ protein: tracking ClpA and ClpAP complex formation in real time. Biochemistry 46 (2007) 6183-6193
-
(2007)
Biochemistry
, vol.46
, pp. 6183-6193
-
-
Kress, W.1
Mutschler, H.2
Weber-Ban, E.3
-
34
-
-
0035266072
-
ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
-
Lee C., Schwartz M.P., Prakash S., Iwakura M., and Matouschek A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7 (2001) 627-637
-
(2001)
Mol. Cell
, vol.7
, pp. 627-637
-
-
Lee, C.1
Schwartz, M.P.2
Prakash, S.3
Iwakura, M.4
Matouschek, A.5
-
35
-
-
0141992126
-
Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag
-
Levchenko I., Grant R.A., Wah D.A., Sauer R.T., and Baker T.A. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Mol. Cell 12 (2003) 365-372
-
(2003)
Mol. Cell
, vol.12
, pp. 365-372
-
-
Levchenko, I.1
Grant, R.A.2
Wah, D.A.3
Sauer, R.T.4
Baker, T.A.5
-
36
-
-
0034730496
-
A specificity-enhancing factor for the ClpXP degradation machine
-
Levchenko I., Seidel M., Sauer R.T., and Baker T.A. A specificity-enhancing factor for the ClpXP degradation machine. Science 289 (2000) 2354-2356
-
(2000)
Science
, vol.289
, pp. 2354-2356
-
-
Levchenko, I.1
Seidel, M.2
Sauer, R.T.3
Baker, T.A.4
-
37
-
-
64049095981
-
Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry
-
Maglica Z., Kolygo K., and Weber-Ban E. Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry. Structure 17 (2009) 508-516
-
(2009)
Structure
, vol.17
, pp. 508-516
-
-
Maglica, Z.1
Kolygo, K.2
Weber-Ban, E.3
-
38
-
-
54849425578
-
An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity
-
Maglica Z., Striebel F., and Weber-Ban E. An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity. J. Mol. Biol. 384 (2008) 503-511
-
(2008)
J. Mol. Biol.
, vol.384
, pp. 503-511
-
-
Maglica, Z.1
Striebel, F.2
Weber-Ban, E.3
-
39
-
-
34250850205
-
Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease
-
Martin A., Baker T.A., and Sauer R.T. Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease. Mol. Cell 27 (2007) 41-52
-
(2007)
Mol. Cell
, vol.27
, pp. 41-52
-
-
Martin, A.1
Baker, T.A.2
Sauer, R.T.3
-
40
-
-
39549084936
-
Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates
-
Martin A., Baker T.A., and Sauer R.T. Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. Mol. Cell 29 (2008) 441-450
-
(2008)
Mol. Cell
, vol.29
, pp. 441-450
-
-
Martin, A.1
Baker, T.A.2
Sauer, R.T.3
-
41
-
-
55549088522
-
Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
-
Martin A., Baker T.A., and Sauer R.T. Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding. Nat. Struct. Mol. Biol. 15 (2008) 1147-1151
-
(2008)
Nat. Struct. Mol. Biol.
, vol.15
, pp. 1147-1151
-
-
Martin, A.1
Baker, T.A.2
Sauer, R.T.3
-
42
-
-
27144474906
-
Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
-
Martin A., Baker T.A., and Sauer R.T. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437 (2005) 1115-1120
-
(2005)
Nature
, vol.437
, pp. 1115-1120
-
-
Martin, A.1
Baker, T.A.2
Sauer, R.T.3
-
44
-
-
0032568504
-
Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP
-
Maurizi M.R., Singh S.K., Thompson M.W., Kessel M., and Ginsburg A. Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. Biochemistry 37 (1998) 7778-7786
-
(1998)
Biochemistry
, vol.37
, pp. 7778-7786
-
-
Maurizi, M.R.1
Singh, S.K.2
Thompson, M.W.3
Kessel, M.4
Ginsburg, A.5
-
45
-
-
33947713897
-
The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies
-
Mogk A., Schmidt R., and Bukau B. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol. 17 (2007) 165-172
-
(2007)
Trends Cell Biol.
, vol.17
, pp. 165-172
-
-
Mogk, A.1
Schmidt, R.2
Bukau, B.3
-
46
-
-
34247103448
-
The tmRNA system for translational surveillance and ribosome rescue
-
Moore S.D., and Sauer R.T. The tmRNA system for translational surveillance and ribosome rescue. Annu. Rev. Biochem. 76 (2007) 101-124
-
(2007)
Annu. Rev. Biochem.
, vol.76
, pp. 101-124
-
-
Moore, S.D.1
Sauer, R.T.2
-
47
-
-
20744457369
-
Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase
-
Park E., Rho Y.M., Koh O.J., Ahn S.W., Seong I.S., Song J.J., Bang O., Seol J.H., Wang J., Eom S.H., and Chung C.H. Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase. J. Biol. Chem. 280 (2005) 22892-22898
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 22892-22898
-
-
Park, E.1
Rho, Y.M.2
Koh, O.J.3
Ahn, S.W.4
Seong, I.S.5
Song, J.J.6
Bang, O.7
Seol, J.H.8
Wang, J.9
Eom, S.H.10
Chung, C.H.11
-
48
-
-
0037188514
-
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY)
-
Ramachandran R., Hartmann C., Song H.K., Huber R., and Bochtler M. Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY). Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 7396-7401
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 7396-7401
-
-
Ramachandran, R.1
Hartmann, C.2
Song, H.K.3
Huber, R.4
Bochtler, M.5
-
50
-
-
67349099562
-
Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS
-
Schuenemann V.J., Kralik S.M., Albrecht R., Spall S.K., Truscott K.N., Dougan D.A., and Zeth K. Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS. EMBO Rep. 10 (2009) 508-514
-
(2009)
EMBO Rep.
, vol.10
, pp. 508-514
-
-
Schuenemann, V.J.1
Kralik, S.M.2
Albrecht, R.3
Spall, S.K.4
Truscott, K.N.5
Dougan, D.A.6
Zeth, K.7
-
51
-
-
0035800729
-
Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis
-
Singh S.K., Rozycki J., Ortega J., Ishikawa T., Lo J., Steven A.C., and Maurizi M.R. Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J. Biol. Chem. 276 (2001) 29420-29429
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 29420-29429
-
-
Singh, S.K.1
Rozycki, J.2
Ortega, J.3
Ishikawa, T.4
Lo, J.5
Steven, A.C.6
Maurizi, M.R.7
-
52
-
-
39449115385
-
AAA+ proteins: diversity in function, similarity in structure
-
Snider J., and Houry W.A. AAA+ proteins: diversity in function, similarity in structure. Biochem. Soc. Trans. 36 (2008) 72-77
-
(2008)
Biochem. Soc. Trans.
, vol.36
, pp. 72-77
-
-
Snider, J.1
Houry, W.A.2
-
53
-
-
0015734383
-
Peptide acceptors in the leucine, phenylalanine transfer reaction
-
Soffer R.L. Peptide acceptors in the leucine, phenylalanine transfer reaction. J. Biol. Chem. 248 (1973) 8424-8428
-
(1973)
J. Biol. Chem.
, vol.248
, pp. 8424-8428
-
-
Soffer, R.L.1
-
54
-
-
0043128700
-
Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine
-
Song H.K., and Eck M.J. Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine. Mol. Cell 12 (2003) 75-86
-
(2003)
Mol. Cell
, vol.12
, pp. 75-86
-
-
Song, H.K.1
Eck, M.J.2
-
55
-
-
0033681249
-
Crystal and solution structures of an HslUV protease-chaperone complex
-
Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., and McKay D.B. Crystal and solution structures of an HslUV protease-chaperone complex. Cell 103 (2000) 633-643
-
(2000)
Cell
, vol.103
, pp. 633-643
-
-
Sousa, M.C.1
Trame, C.B.2
Tsuruta, H.3
Wilbanks, S.M.4
Reddy, V.S.5
McKay, D.B.6
-
56
-
-
28044440088
-
Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release
-
Sprangers R., Gribun A., Hwang P.M., Houry W.A., and Kay L.E. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 16678-16683
-
(2005)
Proc. Natl. Acad. Sci. U.S.A.
, vol.102
, pp. 16678-16683
-
-
Sprangers, R.1
Gribun, A.2
Hwang, P.M.3
Houry, W.A.4
Kay, L.E.5
-
57
-
-
64549106859
-
Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes
-
Striebel F., Kress W., and Weber-Ban E. Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes. Curr. Opin. Struct. Biol. 19 (2009) 209-217
-
(2009)
Curr. Opin. Struct. Biol.
, vol.19
, pp. 209-217
-
-
Striebel, F.1
Kress, W.2
Weber-Ban, E.3
-
59
-
-
0029861143
-
The N-end rule: functions, mysteries, uses
-
Varshavsky A. The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 12142-12149
-
(1996)
Proc. Natl. Acad. Sci. U.S.A.
, vol.93
, pp. 12142-12149
-
-
Varshavsky, A.1
-
60
-
-
0141888401
-
Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease
-
Wah D.A., Levchenko I., Rieckhof G.E., Bolon D.N., Baker T.A., and Sauer R.T. Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell 12 (2003) 355-363
-
(2003)
Mol. Cell
, vol.12
, pp. 355-363
-
-
Wah, D.A.1
Levchenko, I.2
Rieckhof, G.E.3
Bolon, D.N.4
Baker, T.A.5
Sauer, R.T.6
-
61
-
-
0030691115
-
The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
-
Wang J., Hartling J.A., and Flanagan J.M. The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell 91 (1997) 447-456
-
(1997)
Cell
, vol.91
, pp. 447-456
-
-
Wang, J.1
Hartling, J.A.2
Flanagan, J.M.3
-
62
-
-
0035096082
-
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
-
Wang J., Song J.J., Franklin M.C., Kamtekar S., Im Y.J., Rho S.H., Seong I.S., Lee C.S., Chung C.H., and Eom S.H. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure 9 (2001) 177-184
-
(2001)
Structure
, vol.9
, pp. 177-184
-
-
Wang, J.1
Song, J.J.2
Franklin, M.C.3
Kamtekar, S.4
Im, Y.J.5
Rho, S.H.6
Seong, I.S.7
Lee, C.S.8
Chung, C.H.9
Eom, S.H.10
-
63
-
-
35348938968
-
Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase
-
Watanabe K., Toh Y., Suto K., Shimizu Y., Oka N., Wada T., and Tomita K. Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase. Nature 449 (2007) 867-871
-
(2007)
Nature
, vol.449
, pp. 867-871
-
-
Watanabe, K.1
Toh, Y.2
Suto, K.3
Shimizu, Y.4
Oka, N.5
Wada, T.6
Tomita, K.7
-
64
-
-
45849107940
-
Asymmetric nucleotide transactions of the HslUV protease
-
Yakamavich J.A., Baker T.A., and Sauer R.T. Asymmetric nucleotide transactions of the HslUV protease. J. Mol. Biol. 380 (2008) 946-957
-
(2008)
J. Mol. Biol.
, vol.380
, pp. 946-957
-
-
Yakamavich, J.A.1
Baker, T.A.2
Sauer, R.T.3
-
65
-
-
34447511284
-
ClpP: a distinctive family of cylindrical energy-dependent serine proteases
-
Yu A.Y., and Houry W.A. ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett. 581 (2007) 3749-3757
-
(2007)
FEBS Lett.
, vol.581
, pp. 3749-3757
-
-
Yu, A.Y.1
Houry, W.A.2
-
66
-
-
0036896886
-
Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
-
Zeth K., Ravelli R.B., Paal K., Cusack S., Bukau B., and Dougan D.A. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat. Struct. Biol. 9 (2002) 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
-
67
-
-
71449115274
-
-
Kress, W., Mutschler, H., Weber-Ban, E. (2009) Both ATPase domains of ClpA are critical for processing of stable protein substrates. J. Biol. Chem., doi:10.1074/jbc.M109.022319.
-
Kress, W., Mutschler, H., Weber-Ban, E. (2009) Both ATPase domains of ClpA are critical for processing of stable protein substrates. J. Biol. Chem., doi:10.1074/jbc.M109.022319.
-
-
-
|