-
1
-
-
33747605320
-
Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
-
DOI 10.1038/nrn1971, PII NRN1971
-
Pasinelli P, Brown RH (2006) Molecular biology of amyotrophic lateral sclerosis: Insights from genetics. Nat Rev Neurosci 7:710-723. (Pubitemid 44267495)
-
(2006)
Nature Reviews Neuroscience
, vol.7
, Issue.9
, pp. 710-723
-
-
Pasinelli, P.1
Brown, R.H.2
-
2
-
-
22244479388
-
Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
-
DOI 10.1146/annurev.biochem.72.121801.161647
-
Valentine JS, Doucette PA, Potter SZ (2005) Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem 74:563-593. (Pubitemid 40995518)
-
(2005)
Annual Review of Biochemistry
, vol.74
, pp. 563-593
-
-
Valentine, J.S.1
Doucette, P.A.2
Potter, S.Z.3
-
3
-
-
0028284779
-
Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation
-
Gurney ME, et al. (1994) Motor neuron degeneration in mice that express a human Cu,Zn superoxide-dismutase mutation. Science 264:1772-1775. (Pubitemid 24227760)
-
(1994)
Science
, vol.264
, Issue.5166
, pp. 1772-1775
-
-
Gurney, M.E.1
Pu, H.2
Chiu, A.Y.3
Dal Canto, M.C.4
Polchow, C.Y.5
Alexander, D.D.6
Caliendo, J.7
Hentati, A.8
Kwon, Y.W.9
Deng, H.-X.10
Chen, W.11
Zhai, P.12
Sufit, R.L.13
Siddique, T.14
-
4
-
-
0032544674
-
Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
-
Bruijn LI, et al. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281:1851-1854.
-
(1998)
Science
, vol.281
, pp. 1851-1854
-
-
Bruijn, L.I.1
-
5
-
-
0033749379
-
Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
-
Johnston JA, Dalton MJ, Gurney ME, Kopito RR (2000) Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 97:12571-12576.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 12571-12576
-
-
Johnston, J.A.1
Dalton, M.J.2
Gurney, M.E.3
Kopito, R.R.4
-
6
-
-
0347358915
-
Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis
-
Jonsson PA, et al. (2004) Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis. Brain 127:73-88.
-
(2004)
Brain
, vol.127
, pp. 73-88
-
-
Jonsson, P.A.1
-
7
-
-
34547640096
-
Common molecular signature in SOD1 for both sporadic and familial amyotrophic lateral sclerosis
-
DOI 10.1073/pnas.0705044104
-
Gruzman A, et al. (2007) Common molecular signature in SOD1 for both sporadic and familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 104:12524-12529. (Pubitemid 47206171)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.30
, pp. 12524-12529
-
-
Gruzman, A.1
Wood, W.L.2
Alpert, E.3
Prasad, M.D.4
Miller, R.G.5
Rothstein, J.D.6
Bowser, R.7
Hamilton, R.8
Wood, T.D.9
Cleveland, D.W.10
Lingappa, V.R.11
Liu, J.12
-
8
-
-
66049156169
-
Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
-
Karch CM, Prudencio M, Winkler DD, Hart PJ, Borchelt DR (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc Natl Acad Sci USA 106:7774-7779.
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 7774-7779
-
-
Karch, C.M.1
Prudencio, M.2
Winkler, D.D.3
Hart, P.J.4
Borchelt, D.R.5
-
9
-
-
57749098600
-
Amyloid formation by globular proteins under native conditions
-
Chiti F, Dobson CM (2009) Amyloid formation by globular proteins under native conditions. Nat Chem Biol 5:15-22.
-
(2009)
Nat Chem Biol
, vol.5
, pp. 15-22
-
-
Chiti, F.1
Dobson, C.M.2
-
10
-
-
33751212177
-
Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis
-
DOI 10.1016/j.bbadis.2006.05.004, PII S0925443906000846
-
Rakhit R, Chakrabartty A (2006) Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. Biochim Biophys Acta 1762:1025-1037. (Pubitemid 44781177)
-
(2006)
Biochimica et Biophysica Acta - Molecular Basis of Disease
, vol.1762
, Issue.11-12
, pp. 1025-1037
-
-
Rakhit, R.1
Chakrabartty, A.2
-
11
-
-
53049109088
-
Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
-
Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N (2008) Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. J Biol Chem 283:24167-24176.
-
(2008)
J Biol Chem
, vol.283
, pp. 24167-24176
-
-
Furukawa, Y.1
Kaneko, K.2
Yamanaka, K.3
O'Halloran, T.V.4
Nukina, N.5
-
12
-
-
2442624720
-
Monomeric Cu,Zn-superoxide Dismutase Is a Common Misfolding Intermediate in the Oxidation Models of Sporadic and Familial Amyotrophic Lateral Sclerosis
-
DOI 10.1074/jbc.M313295200
-
Rakhit R, et al. (2004) Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. J Biol Chem 279:15499-15504. (Pubitemid 38618950)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.15
, pp. 15499-15504
-
-
Rakhit, R.1
Crow, J.P.2
Lepock, J.R.3
Kondejewski, L.H.4
Cashman, N.R.5
Chakrabartty, A.6
-
13
-
-
6344277909
-
The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis
-
DOI 10.1073/pnas.0406650101
-
Khare SD, Caplow M, Dokholyan NV (2004) The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 101:15094-15099. (Pubitemid 39391724)
-
(2004)
Proceedings of the National Academy of Sciences of the United States of America
, vol.101
, Issue.42
, pp. 15094-15099
-
-
Khare, S.D.1
Caplow, M.2
Dokholyan, N.V.3
-
14
-
-
22244489417
-
Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
-
DOI 10.1073/pnas.0501957102
-
Lindberg MJ, Byström R, Boknäs N, Andersen PM, Oliveberg M (2005) Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants. Proc Natl Acad Sci USA 102:9754-9759. (Pubitemid 40993641)
-
(2005)
Proceedings of the National Academy of Sciences of the United States of America
, vol.102
, Issue.28
, pp. 9754-9759
-
-
Lindberg, M.J.1
Bystrom, R.2
Boknas, N.3
Andersen, P.M.4
Oliveberg, M.5
-
15
-
-
34547415429
-
Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS
-
DOI 10.1073/pnas.0704307104
-
Banci L, et al. (2007) Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS. Proc Natl Acad Sci USA 104:11263-11267. (Pubitemid 47175129)
-
(2007)
Proceedings of the National Academy of Sciences of the United States of America
, vol.104
, Issue.27
, pp. 11263-11267
-
-
Banci, L.1
Bertini, I.2
Durazo, A.3
Girotto, S.4
Gralla, E.B.5
Martinelli, M.6
Valentine, J.S.7
Vieru, M.8
Whitelegge, J.P.9
-
16
-
-
57749100302
-
Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
-
Chattopadhyay M, et al. (2008) Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc Natl Acad Sci USA 105:18663-18668.
-
(2008)
Proc Natl Acad Sci USA
, vol.105
, pp. 18663-18668
-
-
Chattopadhyay, M.1
-
17
-
-
58149402390
-
Dynamical roles of metal ions and the disulfide bond in Cu,Zn superoxide dismutase folding and aggregation
-
Ding F, Dokholyan NV (2008) Dynamical roles of metal ions and the disulfide bond in Cu,Zn superoxide dismutase folding and aggregation. Proc Natl Acad Sci USA 105:19696-19701.
-
(2008)
Proc Natl Acad Sci USA
, vol.105
, pp. 19696-19701
-
-
Ding, F.1
Dokholyan, N.V.2
-
18
-
-
66349087949
-
Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants
-
Banci L, et al. (2009) Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants. Proc Natl Acad Sci USA 106:6980-6985.
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 6980-6985
-
-
Banci, L.1
-
19
-
-
67649852607
-
Functional features cause misfolding of the ALS-provoking enzyme SOD1
-
Nordlund A, et al. (2009) Functional features cause misfolding of the ALS-provoking enzyme SOD1. Proc Natl Acad Sci USA 106:9667-9672.
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 9667-9672
-
-
Nordlund, A.1
-
20
-
-
34249980373
-
An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS
-
DOI 10.1038/nm1559, PII NM1559
-
Rakhit R, et al. (2007) An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS. Nat Med 13:754-759. (Pubitemid 46889748)
-
(2007)
Nature Medicine
, vol.13
, Issue.6
, pp. 754-759
-
-
Rakhit, R.1
Robertson, J.2
Velde, C.V.3
Horne, P.4
Ruth, D.M.5
Griffin, J.6
Cleveland, D.W.7
Cashman, N.R.8
Chakrabartty, A.9
-
21
-
-
33846978054
-
Impaired post-translational folding of familial ALS-linked Cu,Zn superoxide dismutase mutants
-
Bruns CK, Kopito RR (2007) Impaired post-translational folding of familial ALS-linked Cu,Zn superoxide dismutase mutants. EMBO J 26:855-866.
-
(2007)
EMBO J
, vol.26
, pp. 855-866
-
-
Bruns, C.K.1
Kopito, R.R.2
-
22
-
-
9144261759
-
The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
-
DOI 10.1074/jbc.M406021200
-
Arnesano F, et al. (2004) The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem 279:47998-48003. (Pubitemid 39540952)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.46
, pp. 47998-48003
-
-
Arnesano, F.1
Banci, L.2
Bertini, I.3
Martinelli, M.4
Furukawa, Y.5
O'Halloran, T.V.6
-
23
-
-
38149115471
-
Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
-
Cozzolino M, et al. (2007) Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis. J Biol Chem 283:866-874.
-
(2007)
J Biol Chem
, vol.283
, pp. 866-874
-
-
Cozzolino, M.1
-
24
-
-
34948850962
-
Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1
-
DOI 10.1074/jbc.M704465200
-
Niwa J, et al. (2007) Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-liked mutant SOD1. J Biol Chem 282:28087-28095. (Pubitemid 47529492)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.38
, pp. 28087-28095
-
-
Niwa, J.-I.1
Yamada, S.-I.2
Ishigaki, S.3
Sone, J.4
Takahashi, M.5
Katsuno, M.6
Tanaka, F.7
Doyu, M.8
Sobue, G.9
-
25
-
-
0038247520
-
Solution structure of apo Cu,Zn superoxide dismutase: Role of metal ions in protein folding
-
DOI 10.1021/bi034324m
-
Banci L, Bertini I, Cramaro F, Del CR, Viezzoli MS (2003) Solution structure of Apo Cu,Zn superoxide dismutase: Role of metal ions in protein folding. Biochemistry 42:9543-9553. (Pubitemid 37006303)
-
(2003)
Biochemistry
, vol.42
, Issue.32
, pp. 9543-9553
-
-
Banci, L.1
Bertini, I.2
Cramaro, F.3
Del Conte, R.4
Viezzoli, M.S.5
-
26
-
-
0034919305
-
Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
-
Palmer AG, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238.
-
(2001)
Methods Enzymol
, vol.339
, pp. 204-238
-
-
Palmer, A.G.1
Kroenke, C.D.2
Loria, J.P.3
-
27
-
-
33645834303
-
New tools provide new insights in NMR studies of protein dynamics
-
Mittermaier A, Kay LE (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312:224-228.
-
(2006)
Science
, vol.312
, pp. 224-228
-
-
Mittermaier, A.1
Kay, L.E.2
-
28
-
-
34547120448
-
Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins
-
DOI 10.1074/jbc.M700765200
-
Sandelin E, Nordlund A, Andersen PM, Marklund SL, Oliveberg M (2007) Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins. J Biol Chem 282:21230-21236. (Pubitemid 47099916)
-
(2007)
Journal of Biological Chemistry
, vol.282
, Issue.29
, pp. 21230-21236
-
-
Sandelin, E.1
Nordlund, A.2
Andersen, P.M.3
Marklund, S.S.L.4
Oliveberg, M.5
-
29
-
-
0036814981
-
13C chemical shift statistics
-
DOI 10.1023/A:1020997118364
-
Schubert M, Labudde D, Oschkinat H, Schmieder P (2002) A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on C-13 chemical shift statistics. J Biomol NMR 24:149-154. (Pubitemid 35414678)
-
(2002)
Journal of Biomolecular NMR
, vol.24
, Issue.2
, pp. 149-154
-
-
Schubert, M.1
Labudde, D.2
Oschkinat, H.3
Schmieder, P.4
-
30
-
-
0037184476
-
Investigation of the neighboring residue effects on protein chemical shifts
-
DOI 10.1021/ja026811f
-
Wang Y, Jardetzky O (2002) Investigation of the neighboring residue effects on protein chemical shifts. J Am Chem Soc 124:14075-14084. (Pubitemid 35386860)
-
(2002)
Journal of the American Chemical Society
, vol.124
, Issue.47
, pp. 14075-14084
-
-
Wang, Y.1
Jardetzky, O.2
-
31
-
-
33846561471
-
1H transverse paramagnetic relaxation enhancement measurements on macromolecules
-
DOI 10.1016/j.jmr.2006.10.003, PII S109078070600334X
-
Iwahara J, Tang C, Clore GM (2007) Practical aspects of H-1 transverse paramagnetic relaxation enhancement measurements on macromolecules. J Magn Reson 184:185-195. (Pubitemid 46177665)
-
(2007)
Journal of Magnetic Resonance
, vol.184
, Issue.2
, pp. 185-195
-
-
Iwahara, J.1
Tang, C.2
Marius Clore, G.3
-
33
-
-
23044431627
-
Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis
-
Rodriguez JA, et al. (2005) Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proc Natl Acad Sci USA 102:10516-10521.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 10516-10521
-
-
Rodriguez, J.A.1
-
34
-
-
23444450909
-
Coupling of local folding to site-specific binding of proteins to DNA
-
Spolar RS, Record MT (1994) Coupling of local folding to site-specific binding of proteins to DNA. Science 263:777-784.
-
(1994)
Science
, vol.263
, pp. 777-784
-
-
Spolar, R.S.1
Record, M.T.2
-
35
-
-
0037427449
-
The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
-
Strange RW, et al. (2003) The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. J Mol Biol 328:877-891.
-
(2003)
J Mol Biol
, vol.328
, pp. 877-891
-
-
Strange, R.W.1
-
36
-
-
0038442784
-
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
-
Elam JS, et al. (2003) Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat Struct Biol 10:461-467.
-
(2003)
Nat Struct Biol
, vol.10
, pp. 461-467
-
-
Elam, J.S.1
-
38
-
-
0037022563
-
Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
-
Richardson JS, Richardson DC (2002) Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 99:2754-2759.
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 2754-2759
-
-
Richardson, J.S.1
Richardson, D.C.2
-
39
-
-
33144467755
-
Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
-
Jahn TR, Parker MJ, Homans SW, Radford SE (2006) Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol 13:195-201.
-
(2006)
Nat Struct Mol Biol
, vol.13
, pp. 195-201
-
-
Jahn, T.R.1
Parker, M.J.2
Homans, S.W.3
Radford, S.E.4
-
40
-
-
37249017468
-
Systematic in vivo analysis of the intrinsic determinants of amyloid b pathogeneicity
-
Luheshi LM, et al. (2007) Systematic in vivo analysis of the intrinsic determinants of amyloid b pathogeneicity. PLOS Biol 5:2493-2500.
-
(2007)
PLOS Biol
, vol.5
, pp. 2493-2500
-
-
Luheshi, L.M.1
-
41
-
-
45949083132
-
SOD1 and amyotrophic lateral sclerosis: Mutations and oligomerization
-
DOI 10.1371/journal.pone.0001677
-
Banci L, et al. (2008) SOD1 and amyotrophic lateral sclerosis: Mutations and oligomerzation. PLoS One 3:e1677. (Pubitemid 351891080)
-
(2008)
PLoS ONE
, vol.3
, Issue.2
-
-
Banci, L.1
Bertini, I.2
Boca, M.3
Girotto, S.4
Martinelli, M.5
Valentine, J.S.6
Vieru, M.7
-
42
-
-
33745889333
-
Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease
-
DOI 10.1073/pnas.0601696103
-
Nordlund A, Oliveberg M (2006) Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease. Proc Natl Acad Sci USA 103:10218-10223. (Pubitemid 44051147)
-
(2006)
Proceedings of the National Academy of Sciences of the United States of America
, vol.103
, Issue.27
, pp. 10218-10223
-
-
Nordlund, A.1
Oliveberg, M.2
-
43
-
-
3242880292
-
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
-
Korzhnev DM, et al. (2004) Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature 430:586-590.
-
(2004)
Nature
, vol.430
, pp. 586-590
-
-
Korzhnev, D.M.1
-
44
-
-
33646466296
-
Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
-
Deng H-X, et al. (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc Natl Acad Sci USA 103:7142-7147.
-
(2006)
Proc Natl Acad Sci USA
, vol.103
, pp. 7142-7147
-
-
Deng, H.-X.1
-
45
-
-
0003489517
-
-
Academic, San Diego, CA
-
Cavanagh J, Fairbrother WJ, Palmer AG, Skelton NJ (1995) Protein NMR Spectroscopy: Principles and Practice (Academic, San Diego, CA), p 587.
-
(1995)
Protein NMR Spectroscopy: Principles and Practice
, pp. 587
-
-
Cavanagh, J.1
Fairbrother, W.J.2
Palmer, A.G.3
Skelton, N.J.4
-
46
-
-
0033577288
-
A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy [13]
-
DOI 10.1021/ja983961a
-
Loria JP, Rance M, Palmer AG (1999) A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J Am Chem Soc 121:2331-2332. (Pubitemid 29152458)
-
(1999)
Journal of the American Chemical Society
, vol.121
, Issue.10
, pp. 2331-2332
-
-
Loria, J.P.1
Rance, M.2
Palmer III, A.G.3
-
47
-
-
0035819455
-
15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
-
DOI 10.1021/ja003447g
-
Mulder FAA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE (2001) Measurement of slow (microseconds-milliseconds) time scale dynamics in protein side chains by 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J Am Chem Soc 123:967-975. (Pubitemid 32151376)
-
(2001)
Journal of the American Chemical Society
, vol.123
, Issue.5
, pp. 967-975
-
-
Mulder, F.A.A.1
Skrynnikov, N.R.2
Hon, B.3
Dahlquist, F.W.4
Kay, L.E.5
-
48
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delaglio F, et al. (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
-
50
-
-
0035930026
-
Slow dynamics in folded and unfolded states of an SH3 domain
-
DOI 10.1021/ja011300z
-
Tollinger M, Skrynnikov NR, Mulder FAA, Forman-Kay JD, Kay LE (2001) Slow dynamics in folded and unfolded states of an SH3 domain. J Am Chem Soc 123:11341-11352. (Pubitemid 33070591)
-
(2001)
Journal of the American Chemical Society
, vol.123
, Issue.46
, pp. 11341-11352
-
-
Tollinger, M.1
Skrynnikov, N.R.2
Mulder, F.A.A.3
Forman-Kay, J.D.4
Kay, L.E.5
-
51
-
-
0028941877
-
Backbone dynamics of Eschericia coli ribonuclease HI: Correlations with structure and function in an active enzyme
-
Mandel AM, Akke M, Palmer AG (1995) Backbone dynamics of Eschericia coli ribonuclease HI: Correlations with structure and function in an active enzyme. J Mol Biol 246:144-163.
-
(1995)
J Mol Biol
, vol.246
, pp. 144-163
-
-
Mandel, A.M.1
Akke, M.2
Palmer, A.G.3
|