-
1
-
-
0033389470
-
MTCP1 studied by NMR relaxation
-
doi:10.1023/A:1008336418418
-
MTCP1 studied by NMR relaxation. J Biomol NMR 15:271-288. doi:10.1023/A:1008336418418
-
(1999)
J Biomol NMR
, vol.15
, pp. 271-288
-
-
Barthe, P.1
Chiche, L.2
Declerck, N.3
Delsuc, M.4
Lefèvre, J.5
Malliavin, T.6
Mispelter, J.7
Stern, M.8
Lhoste, J.9
Roumestand, C.10
-
2
-
-
0035824545
-
Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein
-
Bussell R, Eliezer D (2001) Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein. J Biol Chem 276(49):45,996-46,003
-
(2001)
J Biol Chem
, vol.276
, Issue.49
, pp. 45996-46003
-
-
Bussell, R.1
Eliezer, D.2
-
3
-
-
0346733333
-
Helix formation and the unfolded state of a 52-residue helical protein
-
DOI 10.1110/ps.03383004
-
Cao W, Bracken C, Kallenbach NR, Lu M (2004) Helix formation and the unfolded state of a 52-residue helical protein. Protein Sci 13:177-189. doi:10.1110/ps.03383004 (Pubitemid 38021152)
-
(2004)
Protein Science
, vol.13
, Issue.1
, pp. 177-189
-
-
Cao, W.1
Bracken, C.2
Kallenbach, N.R.3
Lu, M.4
-
4
-
-
38349077155
-
Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces
-
doi:10.1007/s10858-007-9214-2
-
d'Auvergne EJ, Gooley PR (2008) Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. J Biomol NMR 40:107-119. doi:10.1007/s10858-007- 9214-2
-
(2008)
J Biomol NMR
, vol.40
, pp. 107-119
-
-
D'Auvergne, E.J.1
Gooley, P.R.2
-
5
-
-
38349050193
-
Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor
-
doi:10.1007/s10858-007-9213-3
-
d'Auvergne EJ, Gooley PR (2008) Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. J Biomol NMR 40:121-133. doi:10.1007/s10858-007-9213-3
-
(2008)
J Biomol NMR
, vol.40
, pp. 121-133
-
-
D'Auvergne, E.J.1
Gooley, P.R.2
-
6
-
-
0029400480
-
NMRPipe - A multidimensional spectral processing system based on UNIX pipes
-
doi:10.1007/BF00197809
-
Delaglio F, Grzesiek S, Vuister G, Zhu G, Pfeifer J, Bax A (1995) NMRPipe - a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293. doi:10.1007/BF00197809
-
(1995)
J Biomol NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
Grzesiek, S.2
Vuister, G.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
7
-
-
0029087264
-
Structural-analysis of the Bacillus-subtilis delta-factor - A protein polyanion which displaces RNA from RNA-polymerase
-
DeSaro F, Woody A, Helmann J (1995) Structural-analysis of the Bacillus-subtilis delta-factor - a protein polyanion which displaces RNA from RNA-polymerase. J Mol Biol 252(2):189-202
-
(1995)
J Mol Biol
, vol.252
, Issue.2
, pp. 189-202
-
-
DeSaro, F.1
Woody, A.2
Helmann, J.3
-
8
-
-
4344707281
-
Unfolded proteins and protein folding studied by NMR
-
Dyson H, Wright P (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104(8):3607-3622
-
(2004)
Chem Rev
, vol.104
, Issue.8
, pp. 3607-3622
-
-
Dyson, H.1
Wright, P.2
-
9
-
-
33747768414
-
Characterizing residual structure in disordered protein states using nuclear magnetic resonance
-
Eliezer D (2007) Characterizing residual structure in disordered protein states using nuclear magnetic resonance. Methods Mol Biol 350:49-67
-
(2007)
Methods Mol Biol
, vol.350
, pp. 49-67
-
-
Eliezer, D.1
-
10
-
-
60349087841
-
Biophysical characterization of intrinsically disordered proteins
-
Eliezer D (2009) Biophysical characterization of intrinsically disordered proteins. Curr Opin Struct Biol 19(1):23-30
-
(2009)
Curr Opin Struct Biol
, vol.19
, Issue.1
, pp. 23-30
-
-
Eliezer, D.1
-
12
-
-
0031027137
-
Characterization of the backbone dynamics of folded and denatured states of an SH3 domain
-
DOI 10.1021/bi962548h
-
Farrow NA, Zhang OW, FormanKay JD, Kay LE (1997) Characterization of the backbone dynamics of folded and denatured states of an SH3 domain. Biochemistry 36:2390-2402. doi:10.1021/bi962548h (Pubitemid 27106631)
-
(1997)
Biochemistry
, vol.36
, Issue.9
, pp. 2390-2402
-
-
Farrow, N.A.1
Zhang, O.2
Forman-Kay, J.D.3
Kay, L.E.4
-
13
-
-
70149102207
-
1H nuclear Overhauser effect measurements in the presence of cross-correlated relaxation
-
doi:10.1021/ja809526q
-
1H nuclear Overhauser effect measurements in the presence of cross-correlated relaxation. J Am Chem Soc 131(17):6048+. doi:10.1021/ja809526q
-
(2009)
J Am Chem Soc
, vol.131
, Issue.17
, pp. 6048
-
-
Ferrage, F.1
Cowburn, D.2
Ghose, R.3
-
14
-
-
0242299094
-
1H-coupled HSQC spectra
-
doi:10.1002/mrc.1253
-
1H-coupled HSQC spectra. Magn Reson Chem 41:837-842. doi:10.1002/mrc.1253
-
(2003)
Magn Reson Chem
, vol.41
, pp. 837-842
-
-
Hall, J.1
Fushman, D.2
-
15
-
-
0037649010
-
15N CSA/dipolar relaxation interference from coupled HSQC spectra
-
doi:10.1023/A:1023546107553
-
15N CSA/dipolar relaxation interference from coupled HSQC spectra. J Biomol NMR 26:181-186. doi:10.1023/A:1023546107553
-
(2003)
J Biomol NMR
, vol.26
, pp. 181-186
-
-
Hall, J.1
Dayie, K.2
Fushman, D.3
-
16
-
-
0000503877
-
Protein hydration from water oxygen-17 magnetic-relaxation
-
doi:10.1021/ja00393a004
-
Halle B, Andersson T, Forsén S, Lindman B (1981) Protein hydration from water oxygen-17 magnetic-relaxation. J Am Chem Soc 103:500-508. doi:10.1021/ja00393a004
-
(1981)
J Am Chem Soc
, vol.103
, pp. 500-508
-
-
Halle, B.1
Andersson, T.2
Forsén, S.3
Lindman, B.4
-
17
-
-
0028938022
-
Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei
-
doi:10.1021/bi00010a005
-
Ishima R, Nagayama K (1995) protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei. Biochemistry 34:3162-3171. doi:10.1021/bi00010a005
-
(1995)
Biochemistry
, vol.34
, pp. 3162-3171
-
-
Ishima, R.1
Nagayama, K.2
-
18
-
-
0003075383
-
Quasi-spectral-density function analysis for nitrogen-15 nuclei in proteins
-
doi:10.1006/jmrb.1995.1104
-
Ishima R, Nagayama K (1995) Quasi-spectral-density function analysis for nitrogen-15 nuclei in proteins. J Magn Reson Ser B 108:73-76. doi:10.1006/jmrb.1995.1104
-
(1995)
J Magn Reson Ser B
, vol.108
, pp. 73-76
-
-
Ishima, R.1
Nagayama, K.2
-
19
-
-
84877924088
-
15N relaxation measurements in intrinsically disordered proteins
-
doi:10.1007/s10858-013-9706-1
-
15N relaxation measurements in intrinsically disordered proteins. J Biomol NMR 55:249-256. doi:10.1007/s10858-013-9706-1
-
(2013)
J Biomol NMR
, vol.55
, pp. 249-256
-
-
Kim, S.1
Wu, K.P.2
Baum, J.3
-
20
-
-
0035917992
-
NMR studies of Brownian tumbling and internal motions in proteins
-
DOI 10.1016/S0079-6565(00)00028-5
-
Korzhnev D, Billeter M, Arseniev A, Orekhov V (2001) NMR studies of Brownian tumbling and internal motions in proteins. Prog Nucl Magn Reson Spectrosc 38:197-266. doi:10.1016/S0079-6565(00)00028-5 (Pubitemid 32263164)
-
(2001)
Progress in nuclear magnetic resonance spectroscopy
, vol.38
, Issue.3
, pp. 197-266
-
-
Korzhnev, D.M.1
Billeter, M.2
Arseniev, A.S.3
Orekhov, V.Y.4
-
21
-
-
10744221921
-
Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2-sec-butyl-4,5-dihydrothiazole
-
doi:10.1023/B:JNMR.0000015404.61574.65
-
Křížová H, Žídek L, Stone M, Novotný M, Sklenář V (2004) Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2-sec-butyl-4,5-dihydrothiazole. J Biomol NMR 28:369-384. doi:10.1023/B:JNMR.0000015404.61574.65
-
(2004)
J Biomol NMR
, vol.28
, pp. 369-384
-
-
Křížová, H.1
Žídek, L.2
Stone, M.3
Novotný, M.4
Sklenář, V.5
-
22
-
-
0029872895
-
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
-
doi:10.1021/bi9526802
-
Lefèvre J, Dayie K, Peng J, Wagner G (1996) Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions. Biochemistry 35:2674-2686. doi:10.1021/bi9526802
-
(1996)
Biochemistry
, vol.35
, pp. 2674-2686
-
-
Lefèvre, J.1
Dayie, K.2
Peng, J.3
Wagner, G.4
-
23
-
-
33646719091
-
Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity
-
doi:10.1021/ja00381a009
-
Lipari G, Szabo A (1982) Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559. doi:10.1021/ja00381a009
-
(1982)
J Am Chem Soc
, vol.104
, pp. 4546-4559
-
-
Lipari, G.1
Szabo, A.2
-
24
-
-
33845553743
-
Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results
-
doi:10.1021/ja00381a010
-
Lipari G, Szabo A (1982) Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results. J Am Chem Soc 104:4559-4570. doi:10.1021/ja00381a010
-
(1982)
J Am Chem Soc
, vol.104
, pp. 4559-4570
-
-
Lipari, G.1
Szabo, A.2
-
25
-
-
39749145723
-
Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment
-
DOI 10.1021/ja710477h
-
Long D, Liu M, Yang D (2008) Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment. J Am Chem Soc 130(8):2432-2433. doi:10.1021/ja710477h (Pubitemid 351304747)
-
(2008)
Journal of the American Chemical Society
, vol.130
, Issue.8
, pp. 2432-2433
-
-
Long, D.1
Liu, M.2
Yang, D.3
-
26
-
-
78149414561
-
Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced experiments
-
doi:10.1007/s10858-010-9447-3
-
Motáčková V, Nováček J, Zawadzka-Kazimierczuk A, Kazimierczuk K, Žídek L, Šanderová H, Krásný L, Koźmiński W, Sklenář V (2010) Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced experiments. J Biomol NMR 48(3):169-177. doi:10.1007/s10858-010-9447-3
-
(2010)
J Biomol NMR
, vol.48
, Issue.3
, pp. 169-177
-
-
Motáčková, V.1
Nováček, J.2
Zawadzka-Kazimierczuk, A.3
Kazimierczuk, K.4
Žídek, L.5
Šanderová, H.6
Krásný, L.7
Koźmiński, W.8
Sklenář, V.9
-
27
-
-
77951211788
-
Solution structure of the N-terminal domain of Bacillus subtilis δ subunit of RNA polymerase and its classification based on structural homologs
-
doi:10.1002/prot.22708
-
Motáčková V, Šanderová H, Žídek L, Nováček J, Padrta P, Švenková A, Korelusová J, Jonák J, Krásný L, Sklenář V (2010) Solution structure of the N-terminal domain of Bacillus subtilis δ subunit of RNA polymerase and its classification based on structural homologs. Proteins 78(7):1807-1810. doi:10.1002/prot.22708
-
(2010)
Proteins
, vol.78
, Issue.7
, pp. 1807-1810
-
-
Motáčková, V.1
Šanderová, H.2
Žídek, L.3
Nováček, J.4
Padrta, P.5
Švenková, A.6
Korelusová, J.7
Jonák, J.8
Krásný, L.9
Sklenář, V.10
-
29
-
-
84884703854
-
Structural study of the partially disordered full-length δ subunit of RNA polymerase from Bacillus subtilis
-
doi:10.1002/cbic.201300226
-
Papoušková V, Kadeřávek P, Otrusinová O, Rabatinová A, Šanderová H, Nováček J, Krásný L, Sklenář V, Žídek L (2013) Structural study of the partially disordered full-length δ subunit of RNA polymerase from Bacillus subtilis. ChemBioChem 14:1772-1779. doi:10.1002/cbic.201300226
-
(2013)
ChemBioChem
, vol.14
, pp. 1772-1779
-
-
Papoušková, V.1
Kadeřávek, P.2
Otrusinová, O.3
Rabatinová, A.4
Šanderová, H.5
Nováček, J.6
Krásný, L.7
Sklenář, V.8
Žídek, L.9
-
30
-
-
0037812457
-
Symmetrical reconversion: Measuring cross-correlation rates with enhanced accuracy
-
doi:10.1016/S1090-7807(02)00190-8
-
Pelupessy P, Espallargas GM, Bodenhausen G (2003) Symmetrical reconversion: measuring cross-correlation rates with enhanced accuracy. J Magn Res 161:258-264. doi:10.1016/S1090-7807(02)00190-8
-
(2003)
J Magn Res
, vol.161
, pp. 258-264
-
-
Pelupessy, P.1
Espallargas, G.M.2
Bodenhausen, G.3
-
31
-
-
34047246826
-
Accurate measurement of longitudinal cross-relaxation rates in nuclear magnetic resonance
-
doi:10.1063/1.2715583
-
Pelupessy P, Ferrage F, Bodenhausen G (2007) Accurate measurement of longitudinal cross-relaxation rates in nuclear magnetic resonance. J Chem Phys 126. doi:10.1063/1.2715583
-
(2007)
J Chem Phys
, pp. 126
-
-
Pelupessy, P.1
Ferrage, F.2
Bodenhausen, G.3
-
32
-
-
0000660936
-
Mapping of spectral density-functions using heteronuclear NMR relaxation measurements
-
doi:10.1016/0022-2364(92)90135-T
-
Peng J, Wagner G (1992) Mapping of spectral density-functions using heteronuclear NMR relaxation measurements. J Magn Reson 98:308-332. doi:10.1016/0022-2364(92)90135-T
-
(1992)
J Magn Reson
, vol.98
, pp. 308-332
-
-
Peng, J.1
Wagner, G.2
-
33
-
-
0026784152
-
Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments
-
doi:10.1021/bi00151a027
-
Peng J, Wagner G (1992) Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 31:8571-8586. doi:10.1021/bi00151a027
-
(1992)
Biochemistry
, vol.31
, pp. 8571-8586
-
-
Peng, J.1
Wagner, G.2
-
34
-
-
0016683641
-
Highly asymmetric transcription by rna-polymerase containing phage-Sp01-induced polypeptides and a new host protein
-
doi:10.1073/pnas.72.4.1589
-
Pero J, Nelson J, Fox TD (1975) Highly asymmetric transcription by rna-polymerase containing phage-Sp01-induced polypeptides and a new host protein. Proc Natl Acad Sci USA 72:1589-1593. doi:10.1073/pnas.72.4.1589
-
(1975)
Proc Natl Acad Sci USA
, vol.72
, pp. 1589-1593
-
-
Pero, J.1
Nelson, J.2
Fox, T.D.3
-
35
-
-
84877965282
-
The delta subunit of RNA polymerase is required for rapid changes in gene expression and competitive fitness of the cell
-
doi:10.1128/JB.00188-13
-
Rabatinová A, Šanderová H, Jirát Matějčková J, Korelusová J, Sojka L, Barvík I, Papoušková V, Sklenář V, Žídek L, Krásný L (2013) The delta subunit of RNA polymerase is required for rapid changes in gene expression and competitive fitness of the cell. J Bacteriol 195:2603-2611. doi:10.1128/JB.00188-13
-
(2013)
J Bacteriol
, vol.195
, pp. 2603-2611
-
-
Rabatinová, A.1
Šanderová, H.2
Jirát Matějčková, J.3
Korelusová, J.4
Sojka, L.5
Barvík, I.6
Papoušková, V.7
Sklenář, V.8
Žídek, L.9
Krásný, L.10
-
36
-
-
85022461682
-
The theory of relaxation processes
-
Redfield A (1965) The theory of relaxation processes. Adv Magn Reson 1:1-32
-
(1965)
Adv Magn Reson
, vol.1
, pp. 1-32
-
-
Redfield, A.1
-
37
-
-
0030253418
-
15N NMR relaxation measurements at two magnetic fields
-
doi:10.1007/BF00410326
-
15N NMR relaxation measurements at two magnetic fields. J Biomol NMR 8:273-284. doi:10.1007/BF00410326
-
(1996)
J Biomol NMR
, vol.8
, pp. 273-284
-
-
Tjandra, N.1
Wingfield, P.2
Stahl, S.3
Bax, A.4
-
38
-
-
84870057622
-
Intrinsically disordered proteins: A 10-year recap
-
doi:10.1016/j.tibs.2012.08.004
-
Tompa P (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 37:509-516. doi:10.1016/j.tibs.2012.08.004
-
(2012)
Trends Biochem Sci
, vol.37
, pp. 509-516
-
-
Tompa, P.1
-
39
-
-
84876281768
-
Unusual biophysics of intrinsically disordered proteins
-
doi:10.1016/j.bbapap.2012.12.008
-
Uversky VN (2013) Unusual biophysics of intrinsically disordered proteins. Biochim Biophys Acta 1834:932-951. doi:10.1016/j.bbapap.2012.12.008
-
(2013)
Biochim Biophys Acta
, vol.1834
, pp. 932-951
-
-
Uversky, V.N.1
-
40
-
-
36149011974
-
The dynamical theory of nuclear induction
-
doi:10.1103/PhysRev.89.728
-
Wangsness R, Bloch F (1953) The dynamical theory of nuclear induction. Phys Rev Lett 89(4):728-739. doi:10.1103/PhysRev.89.728
-
(1953)
Phys Rev Lett
, vol.89
, Issue.4
, pp. 728-739
-
-
Wangsness, R.1
Bloch, F.2
-
41
-
-
0035957221
-
NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
-
DOI 10.1021/bi002776i
-
Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ (2001) NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry 40:3561-3571. doi:10.1021/bi002776i (Pubitemid 32242813)
-
(2001)
Biochemistry
, vol.40
, Issue.12
, pp. 3561-3571
-
-
Yao, J.1
Chung, J.2
Eliezer, D.3
Wright, P.E.4
Dyson, H.J.5
-
42
-
-
77950270413
-
15N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements
-
doi:10.1021/ja910186u
-
15N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements. J Am Chem Soc 132:4295-4309. doi:10.1021/ja910186u
-
(2010)
J Am Chem Soc
, vol.132
, pp. 4295-4309
-
-
Yao, L.1
Grishaev, A.2
Cornilescu, G.3
Bax, A.4
-
43
-
-
20144365610
-
Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding
-
doi:10.1021/bi0501939
-
Zhang XC, Xu YQ, Zhang JH, Wu JH, Shi YY (2005) Structural and dynamic characterization of the acid-unfolded state of hUBF HMG box 1 provides clues for the early events in protein folding. Biochemistry 44:8117-8125. doi:10.1021/bi0501939
-
(2005)
Biochemistry
, vol.44
, pp. 8117-8125
-
-
Zhang, X.C.1
Xu, Y.Q.2
Zhang, J.H.3
Wu, J.H.4
Shi, Y.Y.5
|