-
1
-
-
70350336829
-
Characterization of different water pools in solid-state NMR protein samples
-
Böckmann A, Gardiennet C, Verel R, Hunkeler A, Loquet A, Pintacuda G, Emsley L, Meier BH, Lesage A (2009) Characterization of different water pools in solid-state NMR protein samples. J Biomol NMR 45(3):319–327
-
(2009)
J Biomol NMR
, vol.45
, Issue.3
, pp. 319-327
-
-
Böckmann, A.1
Gardiennet, C.2
Verel, R.3
Hunkeler, A.4
Loquet, A.5
Pintacuda, G.6
Emsley, L.7
Meier, B.H.8
Lesage, A.9
-
2
-
-
0037022186
-
Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro
-
Cohlberg JA, Li J, Uversky VN, Fink AL (2002) Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro. Biochemistry 41(5):1502–1511
-
(2002)
Biochemistry
, vol.41
, Issue.5
, pp. 1502-1511
-
-
Cohlberg, J.A.1
Li, J.2
Uversky, V.N.3
Fink, A.L.4
-
3
-
-
80051672851
-
Structured regions of α-synuclein fibrils include the early-onset Parkinsons disease mutation sites
-
Comellas G, Lemkau LR, Nieuwkoop AJ, Kloepper KD, Ladror DT, Ebisu R, Woods WS, Lipton AS, George JM, Rienstra CM (2011) Structured regions of α-synuclein fibrils include the early-onset Parkinsons disease mutation sites. J Mol Biol 411(4):881–895
-
(2011)
J Mol Biol
, vol.411
, Issue.4
, pp. 881-895
-
-
Comellas, G.1
Lemkau, L.R.2
Nieuwkoop, A.J.3
Kloepper, K.D.4
Ladror, D.T.5
Ebisu, R.6
Woods, W.S.7
Lipton, A.S.8
George, J.M.9
Rienstra, C.M.10
-
4
-
-
84858277813
-
Solid-state NMR sequential assignments of α-synuclein
-
Gath J, Habenstein B, Bousset L, Melki R, Meier BH, Böckmann A (2012) Solid-state NMR sequential assignments of α-synuclein. Biomol NMR Assign 6(1):51–55
-
(2012)
Biomol NMR Assign
, vol.6
, Issue.1
, pp. 51-55
-
-
Gath, J.1
Habenstein, B.2
Bousset, L.3
Melki, R.4
Meier, B.H.5
Böckmann, A.6
-
5
-
-
80755128107
-
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
-
Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A (2011) Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion. J Biomol NMR 51(3):235–243
-
(2011)
J Biomol NMR
, vol.51
, Issue.3
, pp. 235-243
-
-
Habenstein, B.1
Wasmer, C.2
Bousset, L.3
Sourigues, Y.4
Schütz, A.5
Loquet, A.6
Meier, B.H.7
Melki, R.8
Böckmann, A.9
-
6
-
-
79551519276
-
α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells
-
Hansen C, Angot E, Bergström A-L, Steiner JA, Pieri L, Paul G, Outeiro TF, Melki R, Kallunki P, Fog K, Li J-Y, Brundin P (2011) α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells. J Clin Invest 121(2):715–725
-
(2011)
J Clin Invest
, vol.121
, Issue.2
, pp. 715-725
-
-
Hansen, C.1
Angot, E.2
Bergström, A.-L.3
Steiner, J.A.4
Pieri, L.5
Paul, G.6
Outeiro, T.F.7
Melki, R.8
Kallunki, P.9
Fog, K.10
Li, J.-Y.11
Brundin, P.12
-
7
-
-
27644518721
-
Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
-
Heise H, Hoyer W, Becker S, Andronesi O, Riedel D, Baldus M (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 102(44):15871–15876
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, Issue.44
, pp. 15871-15876
-
-
Heise, H.1
Hoyer, W.2
Becker, S.3
Andronesi, O.4
Riedel, D.5
Baldus, M.6
-
8
-
-
72249104472
-
Structural properties of pore-forming oligomers of α-synuclein
-
Kim H-Y, Cho M-K, Kumar A, Maier E, Siebenhaar C, Becker S, Fernández CO, Lashuel HA, Benz R, Lange A, Zweckstetter M (2009) Structural properties of pore-forming oligomers of α-synuclein. J Am Chem Soc 131(47):17482–17489
-
(2009)
J Am Chem Soc
, vol.131
, Issue.47
, pp. 17482-17489
-
-
Kim, H.-Y.1
Cho, M.-K.2
Kumar, A.3
Maier, E.4
Siebenhaar, C.5
Becker, S.6
Fernández, C.O.7
Lashuel, H.A.8
Benz, R.9
Lange, A.10
Zweckstetter, M.11
-
9
-
-
84861822461
-
Structural comparison of mouse and human α-synuclein amyloid fibrils by solid-state NMR
-
Lv G, Kumar A, Giller K, Orcellet ML, Riedel D, Fernandez CO, Becker S, Lange A (2012) Structural comparison of mouse and human α-synuclein amyloid fibrils by solid-state NMR. J Mol Biol 420(1–2):99–111
-
(2012)
J Mol Biol
, vol.420
, Issue.1-2
, pp. 99-111
-
-
Lv, G.1
Kumar, A.2
Giller, K.3
Orcellet, M.L.4
Riedel, D.5
Fernandez, C.O.6
Becker, S.7
Lange, A.8
-
10
-
-
77955123982
-
Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227)
-
Schuetz A, Wasmer C, Habenstein B, Verel R, Greenwald J, Riek R, Böckmann A, Meier BH (2010) Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227). ChemBioChem 11(11):1543–1551
-
(2010)
ChemBioChem
, vol.11
, Issue.11
, pp. 1543-1551
-
-
Schuetz, A.1
Wasmer, C.2
Habenstein, B.3
Verel, R.4
Greenwald, J.5
Riek, R.6
Böckmann, A.7
Meier, B.H.8
-
11
-
-
84855281379
-
A software framework for analysing solid-state MAS NMR data
-
Stevens TJ, Fogh RH, Boucher W, Higman VA, Eisenmenger F, Bardiaux B, van Rossum B-J, Oschkinat H, Laue ED (2011) A software framework for analysing solid-state MAS NMR data. J Biomol NMR 51(4):437–447
-
(2011)
J Biomol NMR
, vol.51
, Issue.4
, pp. 437-447
-
-
Stevens, T.J.1
Fogh, R.H.2
Boucher, W.3
Higman, V.A.4
Eisenmenger, F.5
Bardiaux, B.6
van Rossum, B.-J.7
Oschkinat, H.8
Laue, E.D.9
-
12
-
-
19444382397
-
The CCPN data model for NMR spectroscopy: development of a software pipeline
-
Vranken W, Boucher W, Stevens T, Fogh R, Pajon A, Llinas P, Ulrich E, Markley J, Ionides J, Laue E (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59(4):687–696
-
(2005)
Proteins
, vol.59
, Issue.4
, pp. 687-696
-
-
Vranken, W.1
Boucher, W.2
Stevens, T.3
Fogh, R.4
Pajon, A.5
Llinas, P.6
Ulrich, E.7
Markley, J.8
Ionides, J.9
Laue, E.10
-
13
-
-
0028393784
-
The 13C Chemical-Shift Index: a simple method for the identification of protein secondary structure using 13C chemical-shift data
-
Wishart DS, Sykes BD (1994) The 13C Chemical-Shift Index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4(2):171–180
-
(1994)
J Biomol NMR
, vol.4
, Issue.2
, pp. 171-180
-
-
Wishart, D.S.1
Sykes, B.D.2
|