-
1
-
-
33646127577
-
Molecular chaperones and protein quality control
-
doi: 10.1016/j.cell.2006.04.014; pmid: 16678092
-
B. Bukau, J. Weissman, A. Horwich, Molecular chaperones and protein quality control. Cell 125, 443-451 (2006). doi: 10.1016/j.cell.2006.04.014; pmid: 16678092
-
(2006)
Cell
, vol.125
, pp. 443-451
-
-
Bukau, B.1
Weissman, J.2
Horwich, A.3
-
2
-
-
66849109240
-
The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
-
doi: 10.1038/nsmb.1614; pmid: 19491936
-
G. Kramer, D. Boehringer, N. Ban, B. Bukau, The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat. Struct. Mol. Biol. 16, 589-597 (2009). doi: 10.1038/nsmb.1614; pmid: 19491936
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 589-597
-
-
Kramer, G.1
Boehringer, D.2
Ban, N.3
Bukau, B.4
-
3
-
-
66849143696
-
Converging concepts of protein folding in vitro and in vivo
-
doi: 10.1038/nsmb.1591; pmid: 19491934
-
F. U. Hartl, M. Hayer-Hartl, Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574-581 (2009). doi: 10.1038/nsmb.1591; pmid: 19491934
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 574-581
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
4
-
-
80053999780
-
Protein folding in the cell: An inside story
-
doi: 10.1038/nm.2468; pmid: 21989012
-
A. L. Horwich, Protein folding in the cell: An inside story. Nat. Med. 17, 1211-1216 (2011). doi: 10.1038/nm.2468; pmid: 21989012
-
(2011)
Nat. Med.
, vol.17
, pp. 1211-1216
-
-
Horwich, A.L.1
-
5
-
-
79960652801
-
Molecular chaperones in protein folding and proteostasis
-
doi: 10.1038/nature10317; pmid: 21776078
-
F. U. Hartl, A. Bracher, M. Hayer-Hartl, Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332 (2011). doi: 10.1038/nature10317; pmid: 21776078
-
(2011)
Nature
, vol.475
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
6
-
-
84886412961
-
Chaperone machines for protein folding, unfolding and disaggregation
-
doi: 10.1038/nrm3658; pmid: 24026055
-
H. Saibil, Chaperone machines for protein folding, unfolding and disaggregation. Nat. Rev. Cancer 13, 630-642 (2013). doi: 10.1038/nrm3658; pmid: 24026055
-
(2013)
Nat. Rev. Cancer
, vol.13
, pp. 630-642
-
-
Saibil, H.1
-
7
-
-
0037040541
-
Molecular chaperones in the cytosol: From nascent chain to folded protein
-
doi: 10.1126/science.1068408; pmid: 11884745
-
F. Hartl, M. Hayer-Hartl, Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295, 1852-1858 (2002). doi: 10.1126/science.1068408; pmid: 11884745
-
(2002)
Science
, vol.295
, pp. 1852-1858
-
-
Hartl, F.1
Hayer-Hartl, M.2
-
8
-
-
5044239107
-
Pathways of chaperone-mediated protein folding in the cytosol
-
doi: 10.1038/nrm1492; pmid: 15459659
-
J. Young, V. Agashe, K. Siegers, F. Hartl, Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5, 781-791 (2004). doi: 10.1038/nrm1492; pmid: 15459659
-
(2004)
Nat. Rev. Mol. Cell Biol.
, vol.5
, pp. 781-791
-
-
Young, J.1
Agashe, V.2
Siegers, K.3
Hartl, F.4
-
9
-
-
84862848780
-
Ribosome-associated chaperones as key players in proteostasis
-
doi: 10.1016/j.tibs.2012.03.002; pmid: 22503700
-
S. Preissler, E. Deuerling, Ribosome-associated chaperones as key players in proteostasis. Trends Biochem. Sci. 37, 274-283 (2012). doi: 10.1016/j.tibs.2012.03.002; pmid: 22503700
-
(2012)
Trends Biochem. Sci.
, vol.37
, pp. 274-283
-
-
Preissler, S.1
Deuerling, E.2
-
10
-
-
77953027489
-
Structure and function of the molecular chaperone Trigger Factor
-
doi: 10.1016/j.bbamcr.2010.01.017; pmid: 20132842
-
A. Hoffmann, B. Bukau, G. Kramer, Structure and function of the molecular chaperone Trigger Factor. Biochim. Biophys. Acta 1803, 650-661 (2010). doi: 10.1016/j.bbamcr.2010.01.017; pmid: 20132842
-
(2010)
Biochim. Biophys. Acta
, vol.1803
, pp. 650-661
-
-
Hoffmann, A.1
Bukau, B.2
Kramer, G.3
-
11
-
-
0037068441
-
L23 protein functions as a chaperone docking site on the ribosome
-
doi: 10.1038/nature01047; pmid: 12226666
-
G. Kramer et al., L23 protein functions as a chaperone docking site on the ribosome. Nature 419, 171-174 (2002). doi: 10.1038/nature01047; pmid: 12226666
-
(2002)
Nature
, vol.419
, pp. 171-174
-
-
Kramer, G.1
-
12
-
-
4944246094
-
Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
-
doi: 10.1038/nature02899; pmid: 15334087
-
L. Ferbitz et al., Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Nature 431, 590-596 (2004). doi: 10.1038/nature02899; pmid: 15334087
-
(2004)
Nature
, vol.431
, pp. 590-596
-
-
Ferbitz, L.1
-
13
-
-
24744435971
-
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action
-
doi: 10.1073/pnas.0505581102; pmid: 16091460
-
D. Baram et al., Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. Proc. Natl. Acad. Sci. U.S.A. 102, 12017-12022 (2005). doi: 10.1073/pnas.0505581102; pmid: 16091460
-
(2005)
Proc. Natl. Acad. Sci. U.S.A.
, vol.102
, pp. 12017-12022
-
-
Baram, D.1
-
14
-
-
27644447766
-
The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction
-
doi: 10.1016/j.str.2005.08.007; pmid: 16271892
-
F. Schlünzen et al., The binding mode of the trigger factor on the ribosome: Implications for protein folding and SRP interaction. Structure 13, 1685-1694 (2005). doi: 10.1016/j.str.2005.08.007; pmid: 16271892
-
(2005)
Structure
, vol.13
, pp. 1685-1694
-
-
Schlünzen, F.1
-
15
-
-
44649188719
-
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome
-
doi: 10.1038/emboj.2008.89; pmid: 18497744
-
F. Merz et al., Molecular mechanism and structure of Trigger Factor bound to the translating ribosome. EMBO J. 27, 1622-1632 (2008). doi: 10.1038/emboj.2008.89; pmid: 18497744
-
(2008)
EMBO J.
, vol.27
, pp. 1622-1632
-
-
Merz, F.1
-
16
-
-
0034646515
-
Getting newly synthesized proteins into shape
-
doi: 10.1016/S0092-8674(00)80806-5; pmid: 10786831
-
B. Bukau, E. Deuerling, C. Pfund, E. A. Craig, Getting newly synthesized proteins into shape. Cell 101, 119-122 (2000). doi: 10.1016/S0092-8674(00)80806- 5; pmid: 10786831
-
(2000)
Cell
, vol.101
, pp. 119-122
-
-
Bukau, B.1
Deuerling, E.2
Pfund, C.3
Craig, E.A.4
-
17
-
-
0037436348
-
Interaction of trigger factor with the ribosome
-
doi: 10.1016/S0022-2836(02)01427-4; pmid: 12559924
-
R. Maier, B. Eckert, C. Scholz, H. Lilie, F.-X. Schmid, Interaction of trigger factor with the ribosome. J. Mol. Biol. 326, 585-592 (2003). doi: 10.1016/S0022-2836(02)01427-4; pmid: 12559924
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 585-592
-
-
Maier, R.1
Eckert, B.2
Scholz, C.3
Lilie, H.4
Schmid, F.-X.5
-
18
-
-
33751321592
-
Real-time observation of trigger factor function on translating ribosomes
-
doi: 10.1038/nature05225; pmid: 17051157
-
C. M. Kaiser et al., Real-time observation of trigger factor function on translating ribosomes. Nature 444, 455-460 (2006). doi: 10.1038/nature05225; pmid: 17051157
-
(2006)
Nature
, vol.444
, pp. 455-460
-
-
Kaiser, C.M.1
-
19
-
-
42949163134
-
Dynamics of trigger factor interaction with translating ribosomes
-
doi: 10.1074/jbc.M708294200; pmid: 18045873
-
A. Rutkowska et al., Dynamics of trigger factor interaction with translating ribosomes. J. Biol. Chem. 283, 4124-4132 (2008). doi: 10.1074/jbc.M708294200; pmid: 18045873
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 4124-4132
-
-
Rutkowska, A.1
-
20
-
-
0023766740
-
The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane
-
doi: 10.1016/0092-8674(88)90116-X; pmid: 3046750
-
R. Lill, E. Crooke, B. Guthrie, W. Wickner, The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane. Cell 54, 1013-1018 (1988). doi: 10.1016/0092-8674(88)90116-X; pmid: 3046750
-
(1988)
Cell
, vol.54
, pp. 1013-1018
-
-
Lill, R.1
Crooke, E.2
Guthrie, B.3
Wickner, W.4
-
21
-
-
1942421714
-
Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed
-
doi: 10.1016/S0092-8674(04)00299-5; pmid: 15084258
-
V. R. Agashe et al., Function of trigger factor and DnaK in multidomain protein folding: Increase in yield at the expense of folding speed. Cell 117, 199-209 (2004). doi: 10.1016/S0092-8674(04)00299-5; pmid: 15084258
-
(2004)
Cell
, vol.117
, pp. 199-209
-
-
Agashe, V.R.1
-
22
-
-
33646542413
-
Trigger factor forms a protective shield for nascent polypeptides at the ribosome
-
doi: 10.1074/jbc.M512345200; pmid: 16407311
-
A. Hoffmann et al., Trigger factor forms a protective shield for nascent polypeptides at the ribosome. J. Biol. Chem. 281, 6539-6545 (2006). doi: 10.1074/jbc.M512345200; pmid: 16407311
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 6539-6545
-
-
Hoffmann, A.1
-
23
-
-
29344447067
-
Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains
-
doi: 10.1016/j.febslet.2005.11.050; pmid: 16359675
-
S. Tomic, A. E. Johnson, F. U. Hartl, S. A. Etchells, Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains. FEBS Lett. 580, 72-76 (2006). doi: 10.1016/j.febslet.2005. 11.050; pmid: 16359675
-
(2006)
FEBS Lett.
, vol.580
, pp. 72-76
-
-
Tomic, S.1
Johnson, A.E.2
Hartl, F.U.3
Etchells, S.A.4
-
24
-
-
0037338711
-
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities
-
doi: 10.1046/j.1365-2958.2003.03370.x; pmid: 12603737
-
E. Deuerling et al., Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Mol. Microbiol. 47, 1317-1328 (2003). doi: 10.1046/j.1365-2958.2003.03370.x; pmid: 12603737
-
(2003)
Mol. Microbiol.
, vol.47
, pp. 1317-1328
-
-
Deuerling, E.1
-
25
-
-
83255164895
-
Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo
-
doi: 10.1016/j.cell.2011.10.044; pmid: 22153074
-
E. Oh et al., Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo. Cell 147, 1295-1308 (2011). doi: 10.1016/j.cell.2011.10.044; pmid: 22153074
-
(2011)
Cell
, vol.147
, pp. 1295-1308
-
-
Oh, E.1
-
26
-
-
77955659939
-
Versatility of trigger factor interactions with ribosome-nascent chain complexes
-
doi: 10.1074/jbc.M110.134163; pmid: 20595383
-
S. K. Lakshmipathy, R. Gupta, S. Pinkert, S. A. Etchells, F. U. Hartl, Versatility of trigger factor interactions with ribosome-nascent chain complexes. J. Biol. Chem. 285, 27911-27923 (2010). doi: 10.1074/jbc.M110.134163; pmid: 20595383
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 27911-27923
-
-
Lakshmipathy, S.K.1
Gupta, R.2
Pinkert, S.3
Etchells, S.A.4
Hartl, F.U.5
-
27
-
-
69449095153
-
Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone
-
doi: 10.1016/j.cell.2009.07.044; pmid: 19737520
-
E. Martinez-Hackert, W. A. Hendrickson, Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell 138, 923-934 (2009). doi: 10.1016/j.cell.2009.07.044; pmid: 19737520
-
(2009)
Cell
, vol.138
, pp. 923-934
-
-
Martinez-Hackert, E.1
Hendrickson, W.A.2
-
28
-
-
84863528678
-
Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions
-
doi: 10.1021/ja302305u; pmid: 22680285
-
E. P. O'Brien, J. Christodoulou, M. Vendruscolo, C. M. Dobson, Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions. J. Am. Chem. Soc. 134, 10920-10932 (2012). doi: 10.1021/ja302305u; pmid: 22680285
-
(2012)
J. Am. Chem. Soc.
, vol.134
, pp. 10920-10932
-
-
O'Brien, E.P.1
Christodoulou, J.2
Vendruscolo, M.3
Dobson, C.M.4
-
29
-
-
84881480267
-
Reshaping of the conformational search of a protein by the chaperone trigger factor
-
doi: 10.1038/nature12293; pmid: 23831649
-
A. Mashaghi et al., Reshaping of the conformational search of a protein by the chaperone trigger factor. Nature 500, 98-101 (2013). doi: 10.1038/nature12293; pmid: 23831649
-
(2013)
Nature
, vol.500
, pp. 98-101
-
-
Mashaghi, A.1
-
30
-
-
84867379923
-
Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding
-
doi: 10.1016/j.molcel.2012.07.018; pmid: 22921937
-
A. Hoffmann et al., Concerted action of the ribosome and the associated chaperone Trigger Factor confines nascent polypeptide folding. Mol. Cell 48, 63-74 (2012). doi: 10.1016/j.molcel.2012.07.018; pmid: 22921937
-
(2012)
Mol. Cell
, vol.48
, pp. 63-74
-
-
Hoffmann, A.1
-
31
-
-
1642487106
-
In vivo analysis of the overlapping functions of DnaK and trigger factor
-
doi: 10.1038/sj.embor.7400067; pmid: 14726952
-
P. Genevaux et al., In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 5, 195-200 (2004). doi: 10.1038/sj.embor.7400067; pmid: 14726952
-
(2004)
EMBO Rep.
, vol.5
, pp. 195-200
-
-
Genevaux, P.1
-
32
-
-
0033549770
-
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
-
doi: 10.1038/23301; pmid: 10458167
-
E. Deuerling, A. Schulze-Specking, T. Tomoyasu, A. Mogk, B. Bukau, Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400, 693-696 (1999). doi: 10.1038/23301; pmid: 10458167
-
(1999)
Nature
, vol.400
, pp. 693-696
-
-
Deuerling, E.1
Schulze-Specking, A.2
Tomoyasu, T.3
Mogk, A.4
Bukau, B.5
-
33
-
-
0033032592
-
Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
-
doi: 10.1016/S0092-8674(00)80787-4; pmid: 10380927
-
S. A. Teter et al., Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97, 755-765 (1999). doi: 10.1016/S0092-8674(00)80787-4; pmid: 10380927
-
(1999)
Cell
, vol.97
, pp. 755-765
-
-
Teter, S.A.1
-
34
-
-
84861139210
-
DnaK functions as a central hub in the E. coli chaperone network
-
doi: 10.1016/j.celrep.2011.12.007; pmid: 22832197
-
G. Calloni et al., DnaK functions as a central hub in the E. coli chaperone network. Cell Rep. 1, 251-264 (2012). doi: 10.1016/j.celrep.2011.12. 007; pmid: 22832197
-
(2012)
Cell Rep.
, vol.1
, pp. 251-264
-
-
Calloni, G.1
-
35
-
-
36749011854
-
Direct observation of chaperone-induced changes in a protein folding pathway
-
doi: 10.1126/science.1144972; pmid: 18048690
-
P. Bechtluft et al., Direct observation of chaperone-induced changes in a protein folding pathway. Science 318, 1458-1461 (2007). doi: 10.1126/science.1144972; pmid: 18048690
-
(2007)
Science
, vol.318
, pp. 1458-1461
-
-
Bechtluft, P.1
-
36
-
-
33847629610
-
Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli
-
doi: 10.1073/pnas.0608232104; pmid: 17360615
-
R. S. Ullers, D. Ang, F. Schwager, C. Georgopoulos, P. Genevaux, Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 104, 3101-3106 (2007). doi: 10.1073/pnas.0608232104; pmid: 17360615
-
(2007)
Proc. Natl. Acad. Sci. U.S.A.
, vol.104
, pp. 3101-3106
-
-
Ullers, R.S.1
Ang, D.2
Schwager, F.3
Georgopoulos, C.4
Genevaux, P.5
-
37
-
-
0037143625
-
CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90
-
doi: 10.1073/pnas.132393699; pmid: 12163643
-
S. Rudiger, S. M. V. Freund, D. B. Veprintsev, A. R. Fersht, CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. Proc. Natl. Acad. Sci. U.S.A. 99, 11085-11090 (2002). doi: 10.1073/pnas.132393699; pmid: 12163643
-
(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 11085-11090
-
-
Rudiger, S.1
Freund, S.M.V.2
Veprintsev, D.B.3
Fersht, A.R.4
-
38
-
-
24644501099
-
Direct NMR observation of a substrate protein bound to the chaperonin GroEL
-
doi: 10.1073/pnas.0505642102; pmid: 16116078
-
R. Horst et al., Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proc. Natl. Acad. Sci. U.S.A. 102, 12748-12753 (2005). doi: 10.1073/pnas.0505642102; pmid: 16116078
-
(2005)
Proc. Natl. Acad. Sci. U.S.A.
, vol.102
, pp. 12748-12753
-
-
Horst, R.1
-
39
-
-
60549101514
-
The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
-
doi: 10.1073/pnas.0809275106; pmid: 19181847
-
T. A. Walton, C. M. Sandoval, C. A. Fowler, A. Pardi, M. C. Sousa, The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. U.S.A. 106, 1772-1777 (2009). doi: 10.1073/pnas.0809275106; pmid: 19181847
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 1772-1777
-
-
Walton, T.A.1
Sandoval, C.M.2
Fowler, C.A.3
Pardi, A.4
Sousa, M.C.5
-
40
-
-
79955642720
-
The client protein p53 adopts a molten globule-like state in the presence of Hsp90
-
doi: 10.1038/nsmb.2045; pmid: 21460846
-
S. J. Park, B. N. Borin, M. A. Martinez-Yamout, H. J. Dyson, The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat. Struct. Mol. Biol. 18, 537-541 (2011). doi: 10.1038/nsmb.2045; pmid: 21460846
-
(2011)
Nat. Struct. Mol. Biol.
, vol.18
, pp. 537-541
-
-
Park, S.J.1
Borin, B.N.2
Martinez-Yamout, M.A.3
Dyson, H.J.4
-
41
-
-
84870916379
-
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
-
doi: 10.1016/j.cell.2012.11.002; pmid: 23217711
-
A. Zhuravleva, E. M. Clérico, L. M. Gierasch, An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151, 1296-1307 (2012). doi: 10.1016/j.cell.2012.11.002; pmid: 23217711
-
(2012)
Cell
, vol.151
, pp. 1296-1307
-
-
Zhuravleva, A.1
Clérico, E.M.2
Gierasch, L.M.3
-
42
-
-
84887429368
-
Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp
-
doi: 10.1038/nsmb.2677; pmid: 24077225
-
B. M. Burmann, C. Wang, S. Hiller, Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp. Nat. Struct. Mol. Biol. 20, 1265-1272 (2013). doi: 10.1038/nsmb.2677; pmid: 24077225
-
(2013)
Nat. Struct. Mol. Biol.
, vol.20
, pp. 1265-1272
-
-
Burmann, B.M.1
Wang, C.2
Hiller, S.3
-
43
-
-
33846928691
-
Quantitative dynamics and binding studies of the 20S proteasome by NMR
-
doi: 10.1038/nature05512; pmid: 17237764
-
R. Sprangers, L. E. Kay, Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445, 618-622 (2007). doi: 10.1038/nature05512; pmid: 17237764
-
(2007)
Nature
, vol.445
, pp. 618-622
-
-
Sprangers, R.1
Kay, L.E.2
-
44
-
-
36049046667
-
Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR
-
doi: 10.1016/j.cell.2007.09.039; pmid: 18022369
-
I. Gelis et al., Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR. Cell 131, 756-769 (2007). doi: 10.1016/j.cell.2007.09.039; pmid: 18022369
-
(2007)
Cell
, vol.131
, pp. 756-769
-
-
Gelis, I.1
-
45
-
-
77950497745
-
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR
-
doi: 10.1126/science.1184991; pmid: 20360109
-
T. L. Religa, R. Sprangers, L. E. Kay, Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR. Science 328, 98-102 (2010). doi: 10.1126/science.1184991; pmid: 20360109
-
(2010)
Science
, vol.328
, pp. 98-102
-
-
Religa, T.L.1
Sprangers, R.2
Kay, L.E.3
-
46
-
-
84874393637
-
Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction
-
doi: 10.1126/science.1233066; pmid: 23393091
-
R. Rosenzweig, S. Moradi, A. Zarrine-Afsar, J. R. Glover, L. E. Kay, Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science 339, 1080-1083 (2013). doi: 10.1126/science.1233066; pmid: 23393091
-
(2013)
Science
, vol.339
, pp. 1080-1083
-
-
Rosenzweig, R.1
Moradi, S.2
Zarrine-Afsar, A.3
Glover, J.R.4
Kay, L.E.5
-
47
-
-
66349083528
-
Structural basis for cAMP-mediated allosteric control of the catabolite activator protein
-
doi: 10.1073/pnas.0900595106; pmid: 19359484
-
N. Popovych, S.-R. Tzeng, M. Tonelli, R. H. Ebright, C. G. Kalodimos, Structural basis for cAMP-mediated allosteric control of the catabolite activator protein. Proc. Natl. Acad. Sci. U.S.A. 106, 6927-6932 (2009). doi: 10.1073/pnas.0900595106; pmid: 19359484
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 6927-6932
-
-
Popovych, N.1
Tzeng, S.-R.2
Tonelli, M.3
Ebright, R.H.4
Kalodimos, C.G.5
-
48
-
-
83455225628
-
Structural instability tuning as a regulatory mechanism in protein-protein interactions
-
doi: 10.1016/j.molcel.2011.09.022; pmid: 22152477
-
L. Chen et al., Structural instability tuning as a regulatory mechanism in protein-protein interactions. Mol. Cell 44, 734-744 (2011). doi: 10.1016/j.molcel.2011.09.022; pmid: 22152477
-
(2011)
Mol. Cell
, vol.44
, pp. 734-744
-
-
Chen, L.1
-
49
-
-
34249691985
-
Identification of nascent chain interaction sites on trigger factor
-
doi: 10.1074/jbc.M609871200; pmid: 17296610
-
S. K. Lakshmipathy et al., Identification of nascent chain interaction sites on trigger factor. J. Biol. Chem. 282, 12186-12193 (2007). doi: 10.1074/jbc.M609871200; pmid: 17296610
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 12186-12193
-
-
Lakshmipathy, S.K.1
-
50
-
-
33845984939
-
The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
-
doi: 10.1074/jbc.M605164200; pmid: 16926148
-
F. Merz et al., The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity. J. Biol. Chem. 281, 31963-31971 (2006). doi: 10.1074/jbc.M605164200; pmid: 16926148
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 31963-31971
-
-
Merz, F.1
-
51
-
-
0036806274
-
Three-state equilibrium of Escherichia coli trigger factor
-
doi: 10.1515/BC.2002.182; pmid: 12452438
-
H. Patzelt et al., Three-state equilibrium of Escherichia coli trigger factor. Biol. Chem. 383, 1611-1619 (2002). doi: 10.1515/BC.2002.182; pmid: 12452438
-
(2002)
Biol. Chem.
, vol.383
, pp. 1611-1619
-
-
Patzelt, H.1
-
52
-
-
65649125973
-
13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli
-
doi: 10.1007/s12104-008-9130-8; pmid: 19636937
-
13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli. Biomol. NMR Assign. 3, 17-20 (2009). doi: 10.1007/s12104-008-9130-8; pmid: 19636937
-
(2009)
Biomol. NMR Assign.
, vol.3
, pp. 17-20
-
-
Hsu, S.-T.D.1
Dobson, C.M.2
-
53
-
-
37849023833
-
Structure discrimination for the C-terminal domain of Escherichia coli trigger factor in solution
-
doi: 10.1007/s10858-007-9207-1; pmid: 18043871
-
Y. Yao, G. Bhabha, G. Kroon, M. Landes, H. J. Dyson, Structure discrimination for the C-terminal domain of Escherichia coli trigger factor in solution. J. Biomol. NMR 40, 23-30 (2008). doi: 10.1007/s10858-007-9207-1; pmid: 18043871
-
(2008)
J. Biomol. NMR
, vol.40
, pp. 23-30
-
-
Yao, Y.1
Bhabha, G.2
Kroon, G.3
Landes, M.4
Dyson, H.J.5
-
54
-
-
0026091179
-
Identification of a protein required for disulfide bond formation in vivo
-
doi: 10.1016/0092-8674(91)90532-4; pmid: 1934062
-
J. C. Bardwell, K. McGovern, J. Beckwith, Identification of a protein required for disulfide bond formation in vivo. Cell 67, 581-589 (1991). doi: 10.1016/0092-8674(91)90532-4; pmid: 1934062
-
(1991)
Cell
, vol.67
, pp. 581-589
-
-
Bardwell, J.C.1
McGovern, K.2
Beckwith, J.3
-
55
-
-
0024558885
-
Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein
-
pmid: 2535843
-
Y. Akiyama, K. Ito, Export of Escherichia coli alkaline phosphatase attached to an integral membrane protein, SecY. J. Biol. Chem. 264, 437-442 (1989). pmid: 2535843
-
(1989)
SecY. J. Biol. Chem.
, vol.264
, pp. 437-442
-
-
Akiyama, Y.1
Ito, K.2
-
56
-
-
0026567097
-
Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
-
pmid: 1740115
-
S. Kamitani, Y. Akiyama, K. Ito, Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11, 57-62 (1992). pmid: 1740115
-
(1992)
EMBO J.
, vol.11
, pp. 57-62
-
-
Kamitani, S.1
Akiyama, Y.2
Ito, K.3
-
57
-
-
0028799459
-
Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
-
pmid: 8521806
-
Q. A. Valent et al., Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 14, 5494-5505 (1995). pmid: 8521806
-
(1995)
EMBO J.
, vol.14
, pp. 5494-5505
-
-
Valent, Q.A.1
-
58
-
-
0037044752
-
Trigger factor retards protein export in Escherichia coli
-
doi: 10.1074/jbc.M205950200; pmid: 12205085
-
H. C. Lee, H. D. Bernstein, Trigger factor retards protein export in Escherichia coli. J. Biol. Chem. 277, 43527-43535 (2002). doi: 10.1074/jbc.M205950200; pmid: 12205085
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 43527-43535
-
-
Lee, H.C.1
Bernstein, H.D.2
-
59
-
-
33751552347
-
Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation
-
doi: 10.1110/ps.062465306; pmid: 17088319
-
J. A. Marsh, V. K. Singh, Z. Jia, J. D. Forman-Kay, Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation. Protein Sci. 15, 2795-2804 (2006). doi: 10.1110/ps.062465306; pmid: 17088319
-
(2006)
Protein Sci.
, vol.15
, pp. 2795-2804
-
-
Marsh, J.A.1
Singh, V.K.2
Jia, Z.3
Forman-Kay, J.D.4
-
60
-
-
16244419001
-
Elucidation of the protein folding landscape by NMR
-
doi: 10.1016/S0076-6879(05)94011-1; pmid: 15808225
-
H. J. Dyson, P. E. Wright, Elucidation of the protein folding landscape by NMR. Methods Enzymol. 394, 299-321 (2005). doi: 10.1016/S0076-6879(05)94011- 1; pmid: 15808225
-
(2005)
Methods Enzymol.
, vol.394
, pp. 299-321
-
-
Dyson, H.J.1
Wright, P.E.2
-
61
-
-
32344445231
-
NMR studies of protein interactions
-
doi: 10.1016/j.sbi.2006.01.006; pmid: 16427776
-
K. Takeuchi, G. Wagner, NMR studies of protein interactions. Curr. Opin. Struct. Biol. 16, 109-117 (2006). doi: 10.1016/j.sbi.2006.01.006; pmid: 16427776
-
(2006)
Curr. Opin. Struct. Biol.
, vol.16
, pp. 109-117
-
-
Takeuchi, K.1
Wagner, G.2
-
62
-
-
0035807963
-
Binding specificity of Escherichia coli trigger factor
-
doi: 10.1073/pnas.261432298; pmid: 11724963
-
H. Patzelt et al., Binding specificity of Escherichia coli trigger factor. Proc. Natl. Acad. Sci. U.S.A. 98, 14244-14249 (2001). doi: 10.1073/pnas.261432298; pmid: 11724963
-
(2001)
Proc. Natl. Acad. Sci. U.S.A.
, vol.98
, pp. 14244-14249
-
-
Patzelt, H.1
-
63
-
-
0028113299
-
Residues in chaperonin GroEL required for polypeptide binding and release
-
doi: 10.1038/371614a0; pmid: 7935796
-
W. A. Fenton, Y. Kashi, K. Furtak, A. L. Horwich, Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619 (1994). doi: 10.1038/371614a0; pmid: 7935796
-
(1994)
Nature
, vol.371
, pp. 614-619
-
-
Fenton, W.A.1
Kashi, Y.2
Furtak, K.3
Horwich, A.L.4
-
64
-
-
33749538453
-
Convergent evolution of clamp-like binding sites in diverse chaperones
-
doi: 10.1038/nsmb1153; pmid: 17021621
-
P. C. Stirling, S. F. Bakhoum, A. B. Feigl, M. R. Leroux, Convergent evolution of clamp-like binding sites in diverse chaperones. Nat. Struct. Mol. Biol. 13, 865-870 (2006). doi: 10.1038/nsmb1153; pmid: 17021621
-
(2006)
Nat. Struct. Mol. Biol.
, vol.13
, pp. 865-870
-
-
Stirling, P.C.1
Bakhoum, S.F.2
Feigl, A.B.3
Leroux, M.R.4
-
65
-
-
33645834303
-
New tools provide new insights in NMR studies of protein dynamics
-
doi: 10.1126/science.1124964; pmid: 16614210
-
A. Mittermaier, L. E. Kay, New tools provide new insights in NMR studies of protein dynamics. Science 312, 224-228 (2006). doi: 10.1126/science.1124964; pmid: 16614210
-
(2006)
Science
, vol.312
, pp. 224-228
-
-
Mittermaier, A.1
Kay, L.E.2
-
66
-
-
4243155782
-
NMR characterization of the dynamics of biomacromolecules
-
doi: 10.1021/cr030413t; pmid: 15303831
-
A. Palmer, NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 104, 3623-3640 (2004). doi: 10.1021/cr030413t; pmid: 15303831
-
(2004)
Chem. Rev.
, vol.104
, pp. 3623-3640
-
-
Palmer, A.1
-
67
-
-
0032719427
-
A TROSY CPMG sequence for characterizing chemical exchange in large proteins
-
doi: 10.1023/A:1008355631073; pmid: 10605088
-
J. P. Loria, M. Rance, A. G. Palmer, A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 15, 151-155 (1999). doi: 10.1023/A:1008355631073; pmid: 10605088
-
(1999)
J. Biomol. NMR
, vol.15
, pp. 151-155
-
-
Loria, J.P.1
Rance, M.2
Palmer, A.G.3
-
68
-
-
0034759979
-
Studying excited states of proteins by NMR spectroscopy
-
doi: 10.1038/nsb1101-932; pmid: 11685237
-
F. A. Mulder, A. Mittermaier, B. Hon, F. W. Dahlquist, L. E. Kay, Studying excited states of proteins by NMR spectroscopy. Nat. Struct. Biol. 8, 932-935 (2001). doi: 10.1038/nsb1101-932; pmid: 11685237
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 932-935
-
-
Mulder, F.A.1
Mittermaier, A.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
69
-
-
36749058463
-
Measurement of bond vector orientations in invisible excited states of proteins
-
doi: 10.1073/pnas.0708296104; pmid: 18006656
-
P. Vallurupalli, D. F. Hansen, E. Stollar, E. Meirovitch, L. E. Kay, Measurement of bond vector orientations in invisible excited states of proteins. Proc. Natl. Acad. Sci. U.S.A. 104, 18473-18477 (2007). doi: 10.1073/pnas.0708296104; pmid: 18006656
-
(2007)
Proc. Natl. Acad. Sci. U.S.A.
, vol.104
, pp. 18473-18477
-
-
Vallurupalli, P.1
Hansen, D.F.2
Stollar, E.3
Meirovitch, E.4
Kay, L.E.5
-
70
-
-
35948933151
-
Tailoring relaxation dispersion experiments for fast-associating protein complexes
-
doi: 10.1021/ja0762238; pmid: 17935336
-
K. Sugase, J. C. Lansing, H. J. Dyson, P. E. Wright, Tailoring relaxation dispersion experiments for fast-associating protein complexes. J. Am. Chem. Soc. 129, 13406-13407 (2007). doi: 10.1021/ja0762238; pmid: 17935336
-
(2007)
J. Am. Chem. Soc.
, vol.129
, pp. 13406-13407
-
-
Sugase, K.1
Lansing, J.C.2
Dyson, H.J.3
Wright, P.E.4
-
71
-
-
0035861999
-
Dynamic association of trigger factor with protein substrates
-
doi: 10.1006/jmbi.2000.5192; pmid: 11743733
-
R. Maier, C. Scholz, F. Schmid, Dynamic association of trigger factor with protein substrates. J. Mol. Biol. 314, 1181-1190 (2001). doi: 10.1006/jmbi.2000.5192; pmid: 11743733
-
(2001)
J. Mol. Biol.
, vol.314
, pp. 1181-1190
-
-
Maier, R.1
Scholz, C.2
Schmid, F.3
-
72
-
-
39649107959
-
Kinetics and energetics of the translocation of maltose binding protein folding mutants
-
doi: 10.1016/j.jmb.2008.01.014; pmid: 18241889
-
D. Tomkiewicz, N. Nouwen, A. J. M. Driessen, Kinetics and energetics of the translocation of maltose binding protein folding mutants. J. Mol. Biol. 377, 83-90 (2008). doi: 10.1016/j.jmb.2008.01.014; pmid: 18241889
-
(2008)
J. Mol. Biol.
, vol.377
, pp. 83-90
-
-
Tomkiewicz, D.1
Nouwen, N.2
Driessen, A.J.M.3
-
73
-
-
73949133922
-
GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state
-
doi: 10.1073/pnas.0911556106; pmid: 19915138
-
N. K. Tyagi, W. A. Fenton, A. L. Horwich, GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state. Proc. Natl. Acad. Sci. U.S.A. 106, 20264-20269 (2009). doi: 10.1073/pnas.0911556106; pmid: 19915138
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 20264-20269
-
-
Tyagi, N.K.1
Fenton, W.A.2
Horwich, A.L.3
-
74
-
-
77954277524
-
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding
-
doi: 10.1016/j.cell.2010.05.027; pmid: 20603018
-
K. Chakraborty et al., Chaperonin-catalyzed rescue of kinetically trapped states in protein folding. Cell 142, 112-122 (2010). doi: 10.1016/j.cell.2010. 05.027; pmid: 20603018
-
(2010)
Cell
, vol.142
, pp. 112-122
-
-
Chakraborty, K.1
-
75
-
-
0029923189
-
Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies
-
doi: 10.1074/jbc.271.14.8046; pmid: 8626487
-
J. M. Betton, M. Hofnung, Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies. J. Biol. Chem. 271, 8046-8052 (1996). doi: 10.1074/jbc.271.14.8046; pmid: 8626487
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 8046-8052
-
-
Betton, J.M.1
Hofnung, M.2
-
76
-
-
0031764460
-
Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein
-
doi: 10.1002/pro.5560071010; pmid: 9792100
-
S. Raffy, N. Sassoon, M. Hofnung, J. M. Betton, Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein. Protein Sci. 7, 2136-2142 (1998). doi: 10.1002/pro.5560071010; pmid: 9792100
-
(1998)
Protein Sci.
, vol.7
, pp. 2136-2142
-
-
Raffy, S.1
Sassoon, N.2
Hofnung, M.3
Betton, J.M.4
-
77
-
-
0037369139
-
Crystal structure of a defective folding protein
-
doi: 10.1110/ps.0235103; pmid: 12592028
-
F. A. Saul et al., Crystal structure of a defective folding protein. Protein Sci. 12, 577-585 (2003). doi: 10.1110/ps.0235103; pmid: 12592028
-
(2003)
Protein Sci.
, vol.12
, pp. 577-585
-
-
Saul, F.A.1
-
78
-
-
37249067732
-
The origin of protein interactions and allostery in colocalization
-
doi: 10.1038/nature06524; pmid: 18075577
-
J. Kuriyan, D. Eisenberg, The origin of protein interactions and allostery in colocalization. Nature 450, 983-990 (2007). doi: 10.1038/nature06524; pmid: 18075577
-
(2007)
Nature
, vol.450
, pp. 983-990
-
-
Kuriyan, J.1
Eisenberg, D.2
-
79
-
-
0031030202
-
Thermodynamics of maltose binding protein unfolding
-
doi: 10.1002/pro.5560060116; pmid: 9007986
-
V. Novokhatny, K. Ingham, Thermodynamics of maltose binding protein unfolding. Protein Sci. 6, 141-146 (1997). doi: 10.1002/pro.5560060116; pmid: 9007986
-
(1997)
Protein Sci.
, vol.6
, pp. 141-146
-
-
Novokhatny, V.1
Ingham, K.2
-
80
-
-
41149089882
-
Monitoring protein conformation along the pathway of chaperonin-assisted folding
-
doi: 10.1016/j.cell.2008.01.048; pmid: 18394994
-
S. Sharma et al., Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell 133, 142-153 (2008). doi: 10.1016/j.cell.2008. 01.048; pmid: 18394994
-
(2008)
Cell
, vol.133
, pp. 142-153
-
-
Sharma, S.1
-
81
-
-
0034598920
-
Multivalent binding of nonnative substrate proteins by the chaperonin GroEL
-
doi: 10.1016/S0092-8674(00)80692-3; pmid: 10721993
-
G. W. Farr et al., Multivalent binding of nonnative substrate proteins by the chaperonin GroEL. Cell 100, 561-573 (2000). doi: 10.1016/S0092-8674(00) 80692-3; pmid: 10721993
-
(2000)
Cell
, vol.100
, pp. 561-573
-
-
Farr, G.W.1
-
82
-
-
0033617534
-
Chaperonin function: Folding by forced unfolding
-
doi: 10.1126/science.284.5415.822; pmid: 10221918
-
M. Shtilerman, G. H. Lorimer, S. W. Englander, Chaperonin function: Folding by forced unfolding. Science 284, 822-825 (1999). doi: 10.1126/science.284.5415.822; pmid: 10221918
-
(1999)
Science
, vol.284
, pp. 822-825
-
-
Shtilerman, M.1
Lorimer, G.H.2
Englander, S.W.3
-
83
-
-
70349832775
-
Trigger factor finds new jobs and contacts
-
doi: 10.1038/nsmb1009-1006; pmid: 19809489
-
A. Hoffmann, B. Bukau, Trigger factor finds new jobs and contacts. Nat. Struct. Mol. Biol. 16, 1006-1008 (2009). doi: 10.1038/nsmb1009-1006; pmid: 19809489
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 1006-1008
-
-
Hoffmann, A.1
Bukau, B.2
-
84
-
-
2942519292
-
Functional dissection of Escherichia coli trigger factor: Unraveling the function of individual domains
-
doi: 10.1128/JB.186.12.3777-3784.2004; pmid: 15175291
-
G. Kramer et al., Functional dissection of Escherichia coli trigger factor: Unraveling the function of individual domains. J. Bacteriol. 186, 3777-3784 (2004). doi: 10.1128/JB.186.12.3777-3784.2004; pmid: 15175291
-
(2004)
J. Bacteriol.
, vol.186
, pp. 3777-3784
-
-
Kramer, G.1
-
85
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
doi: 10.1007/BF00197809; pmid: 8520220
-
F. Delaglio et al., NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995). doi: 10.1007/BF00197809; pmid: 8520220
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
-
86
-
-
34548304719
-
Solution NMR of supramolecular complexes: Providing new insights into function
-
doi: 10.1038/nmeth1080; pmid: 17762877
-
R. Sprangers, A. Velyvis, L. Kay, Solution NMR of supramolecular complexes: Providing new insights into function. Nat. Methods 4, 697-703 (2007). doi: 10.1038/nmeth1080; pmid: 17762877
-
(2007)
Nat. Methods
, vol.4
, pp. 697-703
-
-
Sprangers, R.1
Velyvis, A.2
Kay, L.3
-
87
-
-
84866272306
-
3-threonine for solution NMR studies of large protein complexes: Application to the 670 kDa proteasome
-
doi: 10.1371/journal.pone.0043725; pmid: 22984438
-
3-threonine for solution NMR studies of large protein complexes: Application to the 670 kDa proteasome. PLOS One 7, e43725 (2012). doi: 10.1371/journal.pone.0043725; pmid: 22984438
-
(2012)
PLOS One
, vol.7
-
-
Velyvis, A.1
Ruschak, A.M.2
Kay, L.E.3
-
88
-
-
4644340524
-
Automated NMR structure calculation with CYANA
-
pmid: 15318003
-
P. Güntert, Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378 (2004). pmid: 15318003
-
(2004)
Methods Mol. Biol.
, vol.278
, pp. 353-378
-
-
Güntert, P.1
-
89
-
-
68349093958
-
TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
-
doi: 10.1007/s10858-009-9333-z; pmid: 19548092
-
Y. Shen, F. Delaglio, G. Cornilescu, A. Bax, TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223 (2009). doi: 10.1007/s10858-009-9333-z; pmid: 19548092
-
(2009)
J. Biomol. NMR
, vol.44
, pp. 213-223
-
-
Shen, Y.1
Delaglio, F.2
Cornilescu, G.3
Bax, A.4
-
90
-
-
33645868288
-
Using Xplor-NIH for NMR molecular structure determination
-
doi: 10.1016/j.pnmrs.2005.10.001
-
C. Schwieters, J. Kuszewski, G.M. Clore, Using Xplor-NIH for NMR molecular structure determination. Prog. Nucl. Magn. Res. Spect. 48, 47-62 (2006). doi: 10.1016/j.pnmrs.2005.10.001
-
(2006)
Prog. Nucl. Magn. Res. Spect.
, vol.48
, pp. 47-62
-
-
Schwieters, C.1
Kuszewski, J.2
Clore, G.M.3
-
91
-
-
37049014272
-
Version 1.2 of the Crystallography and NMR system
-
doi: 10.1038/nprot.2007.406; pmid: 18007608
-
A. T. Brunger, Version 1.2 of the Crystallography and NMR system. Nat. Protoc. 2, 2728-2733 (2007). doi: 10.1038/nprot.2007.406; pmid: 18007608
-
(2007)
Nat. Protoc.
, vol.2
, pp. 2728-2733
-
-
Brunger, A.T.1
-
92
-
-
0002889918
-
2 on the Carr-Purcell pulse separation
-
doi: 10.1016/0022-2364(72)90090-X
-
2 on the Carr-Purcell pulse separation. J. Magn. Reson. 6, 89-105 (1972). doi: 10.1016/0022-2364(72)90090-X
-
(1972)
J. Magn. Reson.
, vol.6
, pp. 89-105
-
-
Carver, J.P.1
Richards, R.E.2
-
93
-
-
84864651001
-
Protein activity regulation by conformational entropy
-
doi: 10.1038/nature11271; pmid: 22801505
-
S.-R. Tzeng, C. G. Kalodimos, Protein activity regulation by conformational entropy. Nature 488, 236-240 (2012). doi: 10.1038/nature11271; pmid: 22801505
-
(2012)
Nature
, vol.488
, pp. 236-240
-
-
Tzeng, S.-R.1
Kalodimos, C.G.2
|