-
1
-
-
74849106907
-
Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase
-
19961227 10.1021/ja9064574 1:CAS:528:DC%2BD1MXhsFWmurrI
-
Q Bashir, et al. 2010 Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase J Am Chem Soc 132 241 247 19961227 10.1021/ja9064574 1:CAS:528: DC%2BD1MXhsFWmurrI
-
(2010)
J Am Chem Soc
, vol.132
, pp. 241-247
-
-
Bashir, Q.1
-
2
-
-
0037215324
-
Weak alignment offers new NMR opportunities to study protein structure and dynamics
-
DOI 10.1110/ps.0233303
-
A Bax 2003 Weak alignment offers new NMR opportunities to study protein structure and dynamics Protein Sci 12 1 16 12493823 10.1110/ps.0233303 1:CAS:528:DC%2BD3sXht1ehuw%3D%3D (Pubitemid 36020129)
-
(2003)
Protein Science
, vol.12
, Issue.1
, pp. 1-16
-
-
Bax, A.1
-
3
-
-
25844506708
-
Weak alignment NMR: A hawk-eyed view of biomolecular structure
-
DOI 10.1016/j.sbi.2005.08.006, PII S0959440X05001545, Carbohydrates and Glycoconjugates/Biophysical Methods
-
A Bax A Grishaev 2005 Weak alignment NMR: a hawk-eyed view of biomolecular structure Curr Opin Struct Biol 15 563 570 16140525 10.1016/j.sbi.2005.08.006 1:CAS:528:DC%2BD2MXhtVKjsLzJ (Pubitemid 41393488)
-
(2005)
Current Opinion in Structural Biology
, vol.15
, Issue.5
, pp. 563-570
-
-
Bax, A.1
Grishaev, A.2
-
4
-
-
67650539779
-
Simultaneous measurement of residual dipolar couplings for proteins in complex using the isotopically discriminated NMR approach
-
19485366 10.1021/ja901602c 1:CAS:528:DC%2BD1MXms1egu7g%3D
-
W Bermel, et al. 2009 Simultaneous measurement of residual dipolar couplings for proteins in complex using the isotopically discriminated NMR approach J Am Chem Soc 131 8564 8570 19485366 10.1021/ja901602c 1:CAS:528:DC%2BD1MXms1egu7g%3D
-
(2009)
J Am Chem Soc
, vol.131
, pp. 8564-8570
-
-
Bermel, W.1
-
5
-
-
3042588804
-
Local dynamic amplitudes on the protein backbone from dipolar couplings: Toward the elucidation of slower motions in biomolecules
-
DOI 10.1021/ja048785m
-
P Bernadó M Blackledge 2004 Local dynamic amplitudes on the protein backbone from dipolar couplings: toward the elucidation of slower motions in biomolecules J Am Chem Soc 126 7760 7761 15212507 10.1021/ja048785m (Pubitemid 38812751)
-
(2004)
Journal of the American Chemical Society
, vol.126
, Issue.25
, pp. 7760-7761
-
-
Bernado, P.1
Blackledge, M.2
-
6
-
-
50149104140
-
Interactions between the three CIN85 SH3 domains and ubiquitin: Implications for CIN85 ubiquitination
-
18680311 10.1021/bi800439t 1:CAS:528:DC%2BD1cXptlejs7Y%3D
-
I Bezsonova, et al. 2008 Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination Biochemistry 47 8937 8949 18680311 10.1021/bi800439t 1:CAS:528:DC%2BD1cXptlejs7Y%3D
-
(2008)
Biochemistry
, vol.47
, pp. 8937-8949
-
-
Bezsonova, I.1
-
7
-
-
14844353335
-
Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings
-
DOI 10.1016/j.pnmrs.2004.11.002, PII S0079656504000603
-
M Blackledge 2005 Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings Prog Nucl Magn Reson Spectrosc 46 23 61 10.1016/j.pnmrs.2004.11.002 1:CAS:528:DC%2BD2MXisFahtrY%3D (Pubitemid 40357061)
-
(2005)
Progress in Nuclear Magnetic Resonance Spectroscopy
, vol.46
, Issue.1
, pp. 23-61
-
-
Blackledge, M.1
-
8
-
-
0033569503
-
Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex
-
DOI 10.1006/jmbi.1999.3133
-
PJ Bolon HM Al-Hashimi JH Prestegard 1999 Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex J Mol Biol 293 107 115 10512719 10.1006/jmbi.1999.3133 1:CAS:528:DyaK1MXmtlCrsb0%3D (Pubitemid 29494873)
-
(1999)
Journal of Molecular Biology
, vol.293
, Issue.1
, pp. 107-115
-
-
Bolon, P.J.1
Al-Hashimi, H.M.2
Prestegard, J.H.3
-
9
-
-
25444532318
-
Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings
-
DOI 10.1073/pnas.0505129102
-
G Bouvignies, et al. 2005 Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings Proc Natl Acad Sci USA 102 13885 13890 16172390 10.1073/pnas.0505129102 1:CAS:528:DC%2BD2MXhtVOqsbvK (Pubitemid 41377673)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.39
, pp. 13885-13890
-
-
Bouvignies, G.1
Bernado, P.2
Meier, S.3
Cho, K.4
Grzesiek, S.5
Bruschweiler, R.6
Blackledge, M.7
-
10
-
-
33845203743
-
Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings
-
DOI 10.1021/ja066704b
-
G Bouvignies P Markwick R Brüschweiler M Blackledge 2006 Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings J Am Chem Soc 128 15100 15101 17117856 10.1021/ja066704b 1:CAS:528:DC%2BD28XhtFKrs7bL (Pubitemid 44853519)
-
(2006)
Journal of the American Chemical Society
, vol.128
, Issue.47
, pp. 15100-15101
-
-
Bouvignies, G.1
Markwick, P.2
Bruschweiler, R.3
Blackledge, M.4
-
11
-
-
1542317796
-
How Much Backbone Motion in Ubiquitin Is Required to Account for Dipolar Coupling Data Measured in Multiple Alignment Media as Assessed by Independent Cross-Validation?
-
DOI 10.1021/ja0386804
-
GM Clore CD Schwieters 2004 How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation? J Am Chem Soc 126 2923 2938 14995210 10.1021/ja0386804 1:CAS:528:DC%2BD2cXhtFagtrg%3D (Pubitemid 38314298)
-
(2004)
Journal of the American Chemical Society
, vol.126
, Issue.9
, pp. 2923-2938
-
-
Clore, G.M.1
Schwieters, C.D.2
-
12
-
-
0032517327
-
Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses [15]
-
DOI 10.1021/ja982592f
-
GM Clore MR Starich AM Gronenborn 1998 Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses J Am Chem Soc 120 10571 10572 10.1021/ja982592f 1:CAS:528:DyaK1cXmtV2ltbs%3D (Pubitemid 28500376)
-
(1998)
Journal of the American Chemical Society
, vol.120
, Issue.40
, pp. 10571-10572
-
-
Clore, G.M.1
Starich, M.R.2
Gronenborn, A.M.3
-
13
-
-
0037442962
-
HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
-
DOI 10.1021/ja026939x
-
C Dominguez R Boelens AMJJ Bonvin 2003 HADDOCK: a protein-protein docking approach based on biochemical or biophysical information J Am Chem Soc 125 1731 1737 12580598 10.1021/ja026939x 1:CAS:528:DC%2BD3sXkvFGquw%3D%3D (Pubitemid 36232568)
-
(2003)
Journal of the American Chemical Society
, vol.125
, Issue.7
, pp. 1731-1737
-
-
Dominguez, C.1
Boelens, R.2
Bonvin, A.M.J.J.3
-
15
-
-
35948942349
-
NMR methods for the determination of protein-ligand dissociation constants
-
DOI 10.1016/j.pnmrs.2007.04.001, PII S0079656507000258
-
L Fielding 2007 NMR methods for the determination of protein-ligand dissociation constants Prog Nucl Magn Reson Spectrosc 51 219 242 10.1016/j.pnmrs.2007.04.001 1:CAS:528:DC%2BD2sXht1ynu77I (Pubitemid 350064300)
-
(2007)
Progress in Nuclear Magnetic Resonance Spectroscopy
, vol.51
, Issue.4
, pp. 219-242
-
-
Fielding, L.1
-
16
-
-
0031760503
-
Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
-
DOI 10.1038/4176
-
MR Hansen L Mueller A Pardi 1998 Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions Nat Struct Biol 5 1065 1074 9846877 10.1038/4176 1:CAS:528:DyaK1cXnvFOlu7k%3D (Pubitemid 28546270)
-
(1998)
Nature Structural Biology
, vol.5
, Issue.12
, pp. 1065-1074
-
-
Hansen, M.R.1
Mueller, L.2
Pardi, A.3
-
17
-
-
34548564106
-
Structural Basis for Ubiquitin Recognition by SH3 Domains
-
DOI 10.1016/j.jmb.2007.07.074, PII S0022283607010522
-
Y He L Hicke I Radhakrishnan 2007 Structural basis for ubiquitin recognition by SH3 domains J Mol Biol 373 190 196 17765920 10.1016/j.jmb.2007. 07.074 1:CAS:528:DC%2BD2sXhtVCgtbbO (Pubitemid 47390722)
-
(2007)
Journal of Molecular Biology
, vol.373
, Issue.1
, pp. 190-196
-
-
He, Y.1
Hicke, L.2
Radhakrishnan, I.3
-
18
-
-
56749158755
-
16-fold degeneracy of peptide plane orientations from residual dipolar couplings: Analytical treatment and implications for protein structure determination
-
18959402 10.1021/ja804274s 1:CAS:528:DC%2BD1cXhtlWqurjK
-
J Hus, et al. 2008 16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination J Am Chem Soc 130 15927 15937 18959402 10.1021/ja804274s 1:CAS:528:DC%2BD1cXhtlWqurjK
-
(2008)
J Am Chem Soc
, vol.130
, pp. 15927-15937
-
-
Hus, J.1
-
19
-
-
0037466291
-
Structural characterization of a mannose-binding protein - Trimannoside complex using residual dipolar couplings
-
DOI 10.1016/S0022-2836(03)00268-7
-
NU Jain S Noble JH Prestegard 2003 Structural characterization of a mannose-binding protein-trimannoside complex using residual dipolar couplings J Mol Biol 328 451 462 12691753 10.1016/S0022-2836(03)00268-7 1:CAS:528: DC%2BD3sXisleht78%3D (Pubitemid 36407587)
-
(2003)
Journal of Molecular Biology
, vol.328
, Issue.2
, pp. 451-462
-
-
Jain, N.U.1
Noble, S.2
Prestegard, J.H.3
-
20
-
-
6344231261
-
Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: The 95 kDa complex of LpxA with acyl carrier protein
-
DOI 10.1016/j.jmb.2004.08.103, PII S0022283604011143
-
NU Jain, et al. 2004 Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein J Mol Biol 343 1379 1389 15491619 10.1016/j.jmb.2004.08.103 1:CAS:528:DC%2BD2cXos1Kksr4%3D (Pubitemid 39387832)
-
(2004)
Journal of Molecular Biology
, vol.343
, Issue.5
, pp. 1379-1389
-
-
Jain, N.U.1
Wyckoff, T.J.O.2
Raetz, C.R.H.3
Prestegard, J.H.4
-
21
-
-
45749102885
-
Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: Application to the molecular recognition element of Sendai virus nucleoprotein
-
DOI 10.1021/ja801332d
-
MR Jensen, et al. 2008 Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein J Am Chem Soc 130 8055 8061 18507376 10.1021/ja801332d 1:CAS:528:DC%2BD1cXmsVelsbg%3D (Pubitemid 351875082)
-
(2008)
Journal of the American Chemical Society
, vol.130
, Issue.25
, pp. 8055-8061
-
-
Jensen, M.R.1
Houben, K.2
Lescop, E.3
Blanchard, L.4
Ruigrok, R.W.H.5
Blackledge, M.6
-
22
-
-
69849103777
-
Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
-
19748338 10.1016/j.str.2009.08.001 1:CAS:528:DC%2BD1MXhtFanu7jN
-
MR Jensen, et al. 2009 Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings Structure 17 1169 1185 19748338 10.1016/j.str.2009.08.001 1:CAS:528:DC%2BD1MXhtFanu7jN
-
(2009)
Structure
, vol.17
, pp. 1169-1185
-
-
Jensen, M.R.1
-
23
-
-
53149091683
-
Distinct interactions between ubiquitin and the SH3 domains involved in immune signaling
-
18539162 1:CAS:528:DC%2BD1cXhtVShs73I
-
J Kang, et al. 2008 Distinct interactions between ubiquitin and the SH3 domains involved in immune signaling Biochim Biophys Acta 1784 1335 1341 18539162 1:CAS:528:DC%2BD1cXhtVShs73I
-
(2008)
Biochim Biophys Acta
, vol.1784
, pp. 1335-1341
-
-
Kang, J.1
-
24
-
-
0036385914
-
Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
-
12217702 10.1016/S0022-2836(02)00745-3 1:CAS:528:DC%2BD38Xms1Wru7o%3D
-
BW Koenig, et al. 2002 Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings J Mol Biol 322 441 461 12217702 10.1016/S0022-2836(02)00745-3 1:CAS:528:DC%2BD38Xms1Wru7o%3D
-
(2002)
J Mol Biol
, vol.322
, pp. 441-461
-
-
Koenig, B.W.1
-
25
-
-
59149097809
-
Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy
-
19111555 10.1016/j.jmb.2008.11.055 1:CAS:528:DC%2BD1MXhs1arsrY%3D
-
DM Korzhnev, et al. 2009 Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy J Mol Biol 386 391 405 19111555 10.1016/j.jmb.2008.11.055 1:CAS:528:DC%2BD1MXhs1arsrY%3D
-
(2009)
J Mol Biol
, vol.386
, pp. 391-405
-
-
Korzhnev, D.M.1
-
26
-
-
45849131354
-
Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
-
DOI 10.1126/science.1157092
-
OF Lange, et al. 2008 Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution Science 320 1471 1475 18556554 10.1126/science.1157092 1:CAS:528:DC%2BD1cXntVWqs70%3D (Pubitemid 351929422)
-
(2008)
Science
, vol.320
, Issue.5882
, pp. 1471-1475
-
-
Lange, O.F.1
Lakomek, N.-A.2
Fares, C.3
Schroder, G.F.4
Walter, K.F.A.5
Becker, S.6
Meiler, J.7
Grubmuller, H.8
Griesinger, C.9
De Groot, B.L.10
-
27
-
-
78650907948
-
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin
-
10.1021/bi101594a
-
A Lange, et al. 2010 NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin Biochemistry 50 48 62 10.1021/bi101594a
-
(2010)
Biochemistry
, vol.50
, pp. 48-62
-
-
Lange, A.1
-
28
-
-
77956361185
-
Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping
-
20589905 10.1002/pro.447 1:CAS:528:DC%2BC3cXhtV2gsLrO
-
H Lee, et al. 2010 Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping Protein Sci 19 1673 1685 20589905 10.1002/pro.447 1:CAS:528:DC%2BC3cXhtV2gsLrO
-
(2010)
Protein Sci
, vol.19
, pp. 1673-1685
-
-
Lee, H.1
-
29
-
-
3042691762
-
Residual dipolar couplings in NMR structure analysis
-
DOI 10.1146/annurev.biophys.33.110502.140306
-
RS Lipsitz N Tjandra 2004 Residual dipolar couplings in NMR structure analysis Annu Rev Biophys Biomol Struct 33 387 413 15139819 10.1146/annurev. biophys.33.110502.140306 1:CAS:528:DC%2BD2cXltlKkt7g%3D (Pubitemid 38829965)
-
(2004)
Annual Review of Biophysics and Biomolecular Structure
, vol.33
, pp. 387-413
-
-
Lipsitz, R.S.1
Tjandra, N.2
-
30
-
-
70450237199
-
Toward a unified representation of protein structural dynamics in solution
-
19919148 10.1021/ja907476w 1:CAS:528:DC%2BD1MXhtlGjtrzF
-
PRL Markwick, et al. 2009 Toward a unified representation of protein structural dynamics in solution J Am Chem Soc 131 16968 16975 19919148 10.1021/ja907476w 1:CAS:528:DC%2BD1MXhtlGjtrzF
-
(2009)
J Am Chem Soc
, vol.131
, pp. 16968-16975
-
-
Markwick, P.R.L.1
-
32
-
-
71749087100
-
Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings
-
19908838 10.1021/ja9069024 1:CAS:528:DC%2BD1MXhsVSmu7zK
-
G Nodet L Salmon V Ozenne S Meier MR Jensen M Blackledge 2009 Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings J Am Chem Soc 131 17908 17918 19908838 10.1021/ja9069024 1:CAS:528:DC%2BD1MXhsVSmu7zK
-
(2009)
J Am Chem Soc
, vol.131
, pp. 17908-17918
-
-
Nodet, G.1
Salmon, L.2
Ozenne, V.3
Meier, S.4
Jensen, M.R.5
Blackledge, M.6
-
33
-
-
73249139292
-
The structural analysis of protein-protein interactions by NMR spectroscopy
-
19834907 10.1002/pmic.200900303
-
MR O'Connell R Gamsjaeger JP Mackay 2009 The structural analysis of protein-protein interactions by NMR spectroscopy Proteomics 9 5224 5232 19834907 10.1002/pmic.200900303
-
(2009)
Proteomics
, vol.9
, pp. 5224-5232
-
-
O'Connell, M.R.1
Gamsjaeger, R.2
MacKay, J.P.3
-
34
-
-
35848962243
-
The high resolution NMR structure of the third SH3 domain of CD2AP
-
DOI 10.1007/s10858-007-9201-7
-
JL Ortega Roldan, et al. 2007 The high resolution NMR structure of the third SH3 domain of CD2AP J Biomol NMR 39 331 336 17922258 10.1007/s10858-007- 9201-7 1:CAS:528:DC%2BD2sXht1Grs7zN (Pubitemid 350055755)
-
(2007)
Journal of Biomolecular NMR
, vol.39
, Issue.4
, pp. 331-336
-
-
Ortega Roldan, J.L.1
Romero Romero, M.L.2
Ora, A.3
Ab, E.4
Lopez Mayorga, O.5
Azuaga, A.I.6
Nuland, N.A.J.7
-
35
-
-
66249142325
-
Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: Application to the CD2AP SH3-C:ubiquitin complex
-
19359362 10.1093/nar/gkp211
-
JL Ortega Roldan, et al. 2009 Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex Nucleic Acids Res 37 e70 19359362 10.1093/nar/gkp211
-
(2009)
Nucleic Acids Res
, vol.37
, pp. 70
-
-
Ortega Roldan, J.L.1
-
36
-
-
80051688323
-
Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
-
Ortega Roldan JL, Blackledge M, van Nuland NAJ, Azuaga AI (2011) Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP. J Biomol NMR 50:103-117
-
(2011)
J Biomol NMR
, vol.50
, pp. 103-117
-
-
Ortega Roldan, J.L.1
Blackledge, M.2
Van Nuland Naj3
Azuaga, A.I.4
-
37
-
-
0034480326
-
NMR structures of biomolecules using field oriented media and residual dipolar couplings
-
DOI 10.1017/S0033583500003656
-
JH Prestegard HM al-Hashimi JR Tolman 2000 NMR structures of biomolecules using field oriented media and residual dipolar couplings Q Rev Biophys 33 371 424 11233409 10.1017/S0033583500003656 1:CAS:528:DC%2BD3MXntFGmurg%3D (Pubitemid 32151707)
-
(2000)
Quarterly Reviews of Biophysics
, vol.33
, Issue.4
, pp. 371-424
-
-
Prestegard, J.H.1
Al-Hashimi, H.M.2
Tolman, J.R.3
-
38
-
-
0037551646
-
Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
-
10.1021/ja001068h
-
M Rückert G Otting 2000 Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments J Am Chem Soc 122 7793 7797 10.1021/ja001068h
-
(2000)
J Am Chem Soc
, vol.122
, pp. 7793-7797
-
-
Rückert, M.1
Otting, G.2
-
39
-
-
70349784868
-
Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin
-
10.1002/anie.200900476 1:CAS:528:DC%2BD1MXmsVSit74%3D
-
L Salmon, et al. 2009 Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin Angew Chem 48 4154 4157 10.1002/anie.200900476 1:CAS:528:DC%2BD1MXmsVSit74%3D
-
(2009)
Angew Chem
, vol.48
, pp. 4154-4157
-
-
Salmon, L.1
-
40
-
-
77953627413
-
NMR characterization of long-range order in intrinsically disordered proteins
-
20499903 10.1021/ja101645g 1:CAS:528:DC%2BC3cXmsFOks74%3D
-
L Salmon, et al. 2010 NMR characterization of long-range order in intrinsically disordered proteins J Am Chem Soc 132 8407 8418 20499903 10.1021/ja101645g 1:CAS:528:DC%2BC3cXmsFOks74%3D
-
(2010)
J Am Chem Soc
, vol.132
, pp. 8407-8418
-
-
Salmon, L.1
-
41
-
-
79953699641
-
Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions
-
10.1002/anie.201100310 1:CAS:528:DC%2BC3MXkt12jur4%3D
-
L Salmon, et al. 2011 Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions Angew Chem 50 3755 3759 10.1002/anie.201100310 1:CAS:528: DC%2BC3MXkt12jur4%3D
-
(2011)
Angew Chem
, vol.50
, pp. 3755-3759
-
-
Salmon, L.1
-
42
-
-
79953718077
-
Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales
-
21388216 10.1021/bi200177v 1:CAS:528:DC%2BC3MXjsVygt7g%3D
-
L Salmon G Bouvignies P Markwick M Blackledge 2011 Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales Biochemistry 50 2735 2747 21388216 10.1021/bi200177v 1:CAS:528:DC%2BC3MXjsVygt7g%3D
-
(2011)
Biochemistry
, vol.50
, pp. 2735-2747
-
-
Salmon, L.1
Bouvignies, G.2
Markwick, P.3
Blackledge, M.4
-
43
-
-
0034501042
-
Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes
-
DOI 10.1023/A:1026703605147
-
HJ Sass, et al. 2000 Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes J Biomol NMR 18 303 309 11200524 10.1023/A:1026703605147 1:CAS:528:DC%2BD3MXns1KisQ%3D%3D (Pubitemid 32065084)
-
(2000)
Journal of Biomolecular NMR
, vol.18
, Issue.4
, pp. 303-309
-
-
Sass, H.-J.1
Musco, G.2
J. Stahl, S.3
T. Wingfield, P.4
Grzesiek, S.5
-
44
-
-
79551681222
-
Protein binding specificity versus promiscuity
-
21071205 10.1016/j.sbi.2010.10.002 1:CAS:528:DC%2BC3MXhvFKhur0%3D
-
G Schreiber AE Keating 2011 Protein binding specificity versus promiscuity Curr Opin Struct Biol 21 50 61 21071205 10.1016/j.sbi.2010.10.002 1:CAS:528:DC%2BC3MXhvFKhur0%3D
-
(2011)
Curr Opin Struct Biol
, vol.21
, pp. 50-61
-
-
Schreiber, G.1
Keating, A.E.2
-
45
-
-
33846212272
-
Ubiquitin Binds to and Regulates a Subset of SH3 Domains
-
DOI 10.1016/j.molcel.2006.12.016, PII S1097276506008847
-
SD Stamenova, et al. 2007 Ubiquitin binds to and regulates a subset of SH3 domains Mol Cell 25 273 284 17244534 10.1016/j.molcel.2006.12.016 1:CAS:528:DC%2BD2sXhslKju7w%3D (Pubitemid 46109609)
-
(2007)
Molecular Cell
, vol.25
, Issue.2
, pp. 273-284
-
-
Stamenova, S.D.1
French, M.E.2
He, Y.3
Francis, S.A.4
Kramer, Z.B.5
Hicke, L.6
-
46
-
-
32344445231
-
NMR studies of protein interactions
-
DOI 10.1016/j.sbi.2006.01.006, PII S0959440X0600011X
-
K Takeuchi G Wagner 2006 NMR studies of protein interactions Curr Opin Struct Biol 16 109 117 16427776 10.1016/j.sbi.2006.01.006 1:CAS:528: DC%2BD28XhsFOjsrg%3D (Pubitemid 43221879)
-
(2006)
Current Opinion in Structural Biology
, vol.16
, Issue.1
, pp. 109-117
-
-
Takeuchi, K.1
Wagner, G.2
-
47
-
-
0030722243
-
Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
-
DOI 10.1126/science.278.5340.1111
-
N Tjandra A Bax 1997 Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science 278 1111 1114 9353189 10.1126/science.278.5340.1111 1:CAS:528:DyaK2sXnt1aju7c%3D (Pubitemid 27517889)
-
(1997)
Science
, vol.278
, Issue.5340
, pp. 1111-1114
-
-
Tjandra, N.1
Bax, A.2
-
48
-
-
0037048594
-
A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy
-
12358549 10.1021/ja0261123 1:CAS:528:DC%2BD38XmvFWlt7k%3D
-
JR Tolman 2002 A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy J Am Chem Soc 124 12020 12030 12358549 10.1021/ja0261123 1:CAS:528:DC%2BD38XmvFWlt7k%3D
-
(2002)
J Am Chem Soc
, vol.124
, pp. 12020-12030
-
-
Tolman, J.R.1
-
49
-
-
0029050883
-
Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
-
7568117 10.1073/pnas.92.20.9279 1:CAS:528:DyaK2MXosVWltLg%3D
-
JR Tolman, et al. 1995 Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution Proc Natl Acad Sci USA 92 9279 9283 7568117 10.1073/pnas.92.20.9279 1:CAS:528:DyaK2MXosVWltLg%3D
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 9279-9283
-
-
Tolman, J.R.1
-
50
-
-
70349910448
-
One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements
-
19764746 10.1021/ja904766g 1:CAS:528:DC%2BD1MXhtFCqtbrM
-
M Tonelli, et al. 2009 One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements J Am Chem Soc 131 14138 14139 19764746 10.1021/ja904766g 1:CAS:528:DC%2BD1MXhtFCqtbrM
-
(2009)
J Am Chem Soc
, vol.131
, pp. 14138-14139
-
-
Tonelli, M.1
-
51
-
-
0018640809
-
Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field
-
J Torbet G Maret 1979 Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field J Mol Biol 134 843 845 537078 10.1016/0022-2836(79)90489-3 1:CAS:528:DyaL3cXlsV2ktQ%3D%3D (Pubitemid 10133193)
-
(1979)
Journal of Molecular Biology
, vol.134
, Issue.4
, pp. 843-845
-
-
Torbet, J.1
Maret, G.2
-
52
-
-
0034721465
-
Alignment of biopolymers in strained gels: A new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR
-
10.1021/ja002133q 1:CAS:528:DC%2BD3cXmt1Kisb8%3D
-
R Tycko FJ Blanco Y Ishii 2000 Alignment of biopolymers in strained gels: a new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR J Am Chem Soc 122 9340 9341 10.1021/ja002133q 1:CAS:528:DC%2BD3cXmt1Kisb8%3D
-
(2000)
J Am Chem Soc
, vol.122
, pp. 9340-9341
-
-
Tycko, R.1
Blanco, F.J.2
Ishii, Y.3
-
53
-
-
29544446689
-
Weak protein-protein interactions as probed by NMR spectroscopy
-
DOI 10.1016/j.tibtech.2005.09.006, PII S0167779905002532
-
J Vaynberg J Qin 2006 Weak protein-protein interactions as probed by NMR spectroscopy Trends Biotech 24 22 27 10.1016/j.tibtech.2005.09.006 1:CAS:528:DC%2BD28XitFCrsQ%3D%3D (Pubitemid 43017747)
-
(2006)
Trends in Biotechnology
, vol.24
, Issue.1
, pp. 22-27
-
-
Vaynberg, J.1
Qin, J.2
-
55
-
-
77955787224
-
Shifting the equilibrium between the encounter state and the specific form of a protein complex by interfacial point mutations
-
20672804 10.1021/ja100867c 1:CAS:528:DC%2BC3cXpsV2lsr0%3D
-
AN Volkov Q Bashir, et al. 2010 Shifting the equilibrium between the encounter state and the specific form of a protein complex by interfacial point mutations J Am Chem Soc 132 11487 11495 20672804 10.1021/ja100867c 1:CAS:528:DC%2BC3cXpsV2lsr0%3D
-
(2010)
J Am Chem Soc
, vol.132
, pp. 11487-11495
-
-
Volkov, A.N.1
Bashir, Q.2
-
56
-
-
78651327177
-
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
-
21049303 10.1007/s10858-010-9452-6 1:CAS:528:DC%2BC3cXhsVeku7vE
-
AN Volkov M Ubbink NAJ van Nuland 2010 Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy J Biomol NMR 48 225 236 21049303 10.1007/s10858-010-9452-6 1:CAS:528:DC%2BC3cXhsVeku7vE
-
(2010)
J Biomol NMR
, vol.48
, pp. 225-236
-
-
Volkov, A.N.1
Ubbink, M.2
Van Nuland, N.A.J.3
-
57
-
-
0037039335
-
Mapping protein-protein interactions in solution by NMR spectroscopy
-
DOI 10.1021/bi011870b
-
ERP Zuiderweg 2002 Mapping protein-protein interactions in solution by NMR spectroscopy Biochemistry 41 1 7 11771996 10.1021/bi011870b 1:CAS:528:DC%2BD3MXoslygsr8%3D (Pubitemid 34049375)
-
(2002)
Biochemistry
, vol.41
, Issue.1
, pp. 1-7
-
-
Zuiderweg, E.R.P.1
|