-
1
-
-
18844420024
-
Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy
-
10.1002/anie.200461794
-
Bermel W, Bertini I, Duma L, Emsley L, Felli IC, Pierattelli R, Vasos PR (2005) Complete assignment of heteronuclear protein resonances by protonless NMR spectroscopy. Angew Chem Int Ed 44:3089-3092
-
(2005)
Angew Chem Int Ed
, vol.44
, pp. 3089-3092
-
-
Bermel, W.1
Bertini, I.2
Duma, L.3
Emsley, L.4
Felli, I.C.5
Pierattelli, R.6
Vasos, P.R.7
-
2
-
-
67349216108
-
H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins
-
2009JMagR.198.275B 10.1016/j.jmr.2009.02.012
-
Bermel W, Bertini I, Csizmok V, Felli IC, Pierattelli R, Tompa P (2009a) H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins. J Magn Reson 198:275-281
-
(2009)
J Magn Reson
, vol.198
, pp. 275-281
-
-
Bermel, W.1
Bertini, I.2
Csizmok, V.3
Felli, I.C.4
Pierattelli, R.5
Tompa, P.6
-
4
-
-
84865108267
-
Speeding up sequence specific assignment of IDPs
-
10.1007/s10858-012-9639-0
-
Bermel W, Bertini I, Felli IC, Gonnelli L, Kozminski W, Piai A, Pierattelli R, Stanek J (2012a) Speeding up sequence specific assignment of IDPs. J Biomol NMR 53:293-301
-
(2012)
J Biomol NMR
, vol.53
, pp. 293-301
-
-
Bermel, W.1
Bertini, I.2
Felli, I.C.3
Gonnelli, L.4
Kozminski, W.5
Piai, A.6
Pierattelli, R.7
Stanek, J.8
-
5
-
-
84868115572
-
Exclusively heteronuclear 13C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDP)
-
Bermel W, Bertini I, Chill J, Felli IC, Haba N, Kumar V, Pieratelli R (2012b) Exclusively heteronuclear 13C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDP). Chem Biochem 13:2425-2432
-
(2012)
Chem Biochem
, vol.13
, pp. 2425-2432
-
-
Bermel, W.1
Bertini, I.2
Chill, J.3
Felli, I.C.4
Haba, N.5
Kumar, V.6
Pieratelli, R.7
-
7
-
-
33745042221
-
Alanine check points in HNN and HN(C)N spectra
-
2006JMagR.181.21C 10.1016/j.jmr.2006.03.009
-
Chatterjee A, Kumar A, Hosur RV (2006) Alanine check points in HNN and HN(C)N spectra. J Magn Reson 181:21-28
-
(2006)
J Magn Reson
, vol.181
, pp. 21-28
-
-
Chatterjee, A.1
Kumar, A.2
Hosur, R.V.3
-
8
-
-
38349049191
-
Tuning the HNN experiment: Generation of serine-threonine check points
-
10.1007/s10858-007-9217-z
-
Chugh J, Kumar D, Hosur RV (2008) Tuning the HNN experiment: generation of serine-threonine check points. J Biomol NMR 40:145-152
-
(2008)
J Biomol NMR
, vol.40
, pp. 145-152
-
-
Chugh, J.1
Kumar, D.2
Hosur, R.V.3
-
9
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
10.1007/BF00197809
-
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293
-
(1995)
J Biomol NMR
, vol.6
, pp. 277-293
-
-
Delaglio, F.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
11
-
-
0034912536
-
Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states
-
10.1016/S0076-6879(01)39317-5
-
Dyson HJ, Wright PE (2001) Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol 339:258-270
-
(2001)
Methods Enzymol
, vol.339
, pp. 258-270
-
-
Dyson, H.J.1
Wright, P.E.2
-
12
-
-
4344707281
-
Unfolded proteins and protein folding studied by NMR
-
10.1021/cr030403s
-
Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104:3607-3622
-
(2004)
Chem Rev
, vol.104
, pp. 3607-3622
-
-
Dyson, H.J.1
Wright, P.E.2
-
13
-
-
60349087841
-
Biophysical characterization of intrinsically disordered proteins
-
10.1016/j.sbi.2008.12.004
-
Eliezer D (2009) Biophysical characterization of intrinsically disordered proteins. Curr Opin Struct Biol 19:23-30
-
(2009)
Curr Opin Struct Biol
, vol.19
, pp. 23-30
-
-
Eliezer, D.1
-
14
-
-
13844255387
-
Natively unfolded proteins
-
10.1016/j.sbi.2005.01.002
-
Fink AL (2005) Natively unfolded proteins. Curr Opin Struct Biol 15:35-41
-
(2005)
Curr Opin Struct Biol
, vol.15
, pp. 35-41
-
-
Fink, A.L.1
-
15
-
-
0000061511
-
15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides
-
10.1021/ja00063a068
-
15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides. J Am Chem Soc 115:4369-4370
-
(1993)
J Am Chem Soc
, vol.115
, pp. 4369-4370
-
-
Grzesiek, S.1
Anglister, J.2
Ren, J.H.3
Bax, A.4
-
16
-
-
34249765651
-
NMR view: A computer program for the visualization and analysis of NMR data
-
10.1007/BF00404272
-
Johnson BA, Blevins RA (1994) NMR view: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603-614
-
(1994)
J Biomol NMR
, vol.4
, pp. 603-614
-
-
Johnson, B.A.1
Blevins, R.A.2
-
18
-
-
77954762400
-
HA-detected experiments for the backbone assignment of intrinsically disordered proteins
-
10.1007/s10858-010-9421-0
-
Mäntylahti S, Aito O, Hellman M, Permi P (2010) HA-detected experiments for the backbone assignment of intrinsically disordered proteins. J Biomol NMR 47:171-181
-
(2010)
J Biomol NMR
, vol.47
, pp. 171-181
-
-
Mäntylahti, S.1
Aito, O.2
Hellman, M.3
Permi, P.4
-
19
-
-
79954431523
-
Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins
-
10.1007/s10858-011-9470-z
-
Mäntylahti S, Hellman M, Permi P (2011) Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins. J Biomol NMR 49:99-109
-
(2011)
J Biomol NMR
, vol.49
, pp. 99-109
-
-
Mäntylahti, S.1
Hellman, M.2
Permi, P.3
-
20
-
-
78149414561
-
Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution enhanced 5D experiments
-
10.1007/s10858-010-9447-3
-
Motácková V, Novácek J, Zawadzka-Kazimierczuk A, Kazimierczuk K, Žídek L, Sanderová H, Krásny L, Kozminski W, Sklenár V (2010) Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution enhanced 5D experiments. J Biomol NMR 48:169-177
-
(2010)
J Biomol NMR
, vol.48
, pp. 169-177
-
-
Motácková, V.1
Novácek, J.2
Zawadzka-Kazimierczuk, A.3
Kazimierczuk, K.4
Žídek, L.5
Sanderová, H.6
Krásny, L.7
Kozminski, W.8
Sklenár, V.9
-
21
-
-
79952696284
-
13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion
-
10.1007/s10858-011-9496-2
-
13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion. J Biomol NMR 50:1-11
-
(2011)
J Biomol NMR
, vol.50
, pp. 1-11
-
-
Novácek, J.1
Zawadzka-Kazimierczuk, A.2
Papousková, V.3
Žídek, L.4
Sandervá, H.5
Krásny, L.6
Kozminski, W.7
Sklenár, V.8
-
22
-
-
84865187352
-
4D Non-uniformly sampled HCBCACON and 1 J(NCα)-selective-HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
-
10.1007/s10858-012-9631-8
-
Novácek J, Haba NY, Chill JH, Žídek L, Sklenár V (2012) 4D Non-uniformly sampled HCBCACON and 1 J(NCα)-selective-HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. J Biomol NMR 53:139-148
-
(2012)
J Biomol NMR
, vol.53
, pp. 139-148
-
-
Novácek, J.1
Haba, N.Y.2
Chill, J.H.3
Žídek, L.4
Sklenár, V.5
-
23
-
-
0034919873
-
15N) labeled proteins: Application to unfolded proteins
-
10.1023/A:1011239023422
-
15N) labeled proteins: application to unfolded proteins. J Biomol NMR 20:135-147
-
(2001)
J Biomol NMR
, vol.20
, pp. 135-147
-
-
Panchal, S.C.1
Bavesh, N.S.2
Hosur, R.V.3
-
24
-
-
71049140420
-
Aliasing in reduced dimensionality spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH as examples
-
10.1007/s10858-009-9383-2
-
Pantoja-Uceda D, Santoro J (2009) Aliasing in reduced dimensionality spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH as examples. J Biomol NMR 45:351-356
-
(2009)
J Biomol NMR
, vol.45
, pp. 351-356
-
-
Pantoja-Uceda, D.1
Santoro, J.2
-
26
-
-
0347722841
-
Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
-
10.1016/S0079-6565(98)00025-9
-
Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Magn Reson Spectrosc 34:93-158
-
(1999)
Prog Nucl Magn Reson Spectrosc
, vol.34
, pp. 93-158
-
-
Sattler, M.1
Schleucher, J.2
Griesinger, C.3
-
28
-
-
0036803243
-
Intrinsically unstructured proteins
-
10.1016/S0968-0004(02)02169-2
-
Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533
-
(2002)
Trends Biochem Sci
, vol.27
, pp. 527-533
-
-
Tompa, P.1
-
29
-
-
79958044914
-
Unstructural biology coming of age
-
10.1016/j.sbi.2011.03.012
-
Tompa P (2011) Unstructural biology coming of age. Curr Opin Struct Biol 21:419-425
-
(2011)
Curr Opin Struct Biol
, vol.21
, pp. 419-425
-
-
Tompa, P.1
-
30
-
-
84870057622
-
Intrinsically disordered proteins: A 10-year recap
-
10.1016/j.tibs.2012.08.004
-
Tompa P (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 37:509-516
-
(2012)
Trends Biochem Sci
, vol.37
, pp. 509-516
-
-
Tompa, P.1
-
31
-
-
0031451750
-
Chemical shift dispersion and secondary structure prediction in unfolded and partially folded proteins
-
10.1016/S0014-5793(97)01474-9
-
Yao J, Dyson HJ, Wright PE (1997) Chemical shift dispersion and secondary structure prediction in unfolded and partially folded proteins. FEBS Lett 419:285-289
-
(1997)
FEBS Lett
, vol.419
, pp. 285-289
-
-
Yao, J.1
Dyson, H.J.2
Wright, P.E.3
-
32
-
-
0031064317
-
Triple-resonance NOESY-based experiments with improved spectral resolution: Applications to structural characterization of unfolded, partially folded and folded proteins
-
10.1023/A:1018658305040
-
Zhang O, Forman-Kay JD, Shortle D, Kay LE (1997) Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins. J Biomol NMR 9:181-200
-
(1997)
J Biomol NMR
, vol.9
, pp. 181-200
-
-
Zhang, O.1
Forman-Kay, J.D.2
Shortle, D.3
Kay, L.E.4
|