-
1
-
-
33645521792
-
Protein aggregation and its consequences for human disease
-
C.M. Dobson Protein aggregation and its consequences for human disease Protein Pept. Lett. 13 2006 219 227
-
(2006)
Protein Pept. Lett.
, vol.13
, pp. 219-227
-
-
Dobson, C.M.1
-
2
-
-
7944233158
-
Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
-
DOI 10.1038/ncb1104-1054
-
D.J. Selkoe Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases Nat. Cell Biol. 6 2004 1054 1061 (Pubitemid 39468006)
-
(2004)
Nature Cell Biology
, vol.6
, Issue.11
, pp. 1054-1061
-
-
Selkoe, D.J.1
-
3
-
-
84869887960
-
Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits
-
M. Stefani Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits Prog. Neurobiol. 99 2012 226 245
-
(2012)
Prog. Neurobiol.
, vol.99
, pp. 226-245
-
-
Stefani, M.1
-
5
-
-
33846023647
-
Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways
-
DOI 10.1016/j.jmb.2006.10.101, PII S0022283606015294
-
A.L. Gharibyan, V. Zamotin, K. Yanamandra, O.S. Moskaleva, B.A. Margulis, I.A. Kostanyan, and L.A. Morozova-Roche Lysozyme amyloid oligomers and fibrils induce cellular death via different apoptotic/necrotic pathways J. Mol. Biol. 365 2007 1337 1349 (Pubitemid 46048842)
-
(2007)
Journal of Molecular Biology
, vol.365
, Issue.5
, pp. 1337-1349
-
-
Gharibyan, A.L.1
Zamotin, V.2
Yanamandra, K.3
Moskaleva, O.S.4
Margulis, B.A.5
Kostanyan, I.A.6
Morozova-Roche, L.A.7
-
6
-
-
0037271080
-
Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein
-
H.-J. Kim, S.-C. Chae, D.-K. Lee, B. Chromy, S.C. Lee, Y.-C. Park, W.L. Klein, G.A. Krafft, and S.-T. Hong Selective neuronal degeneration induced by soluble oligomeric amyloid beta protein FASEB J. 17 2003 118 120
-
(2003)
FASEB J.
, vol.17
, pp. 118-120
-
-
Kim, H.-J.1
Chae, S.-C.2
Lee, D.-K.3
Chromy, B.4
Lee, S.C.5
Park, Y.-C.6
Klein, W.L.7
Krafft, G.A.8
Hong, S.-T.9
-
7
-
-
0242668337
-
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
-
DOI 10.1126/science.1079469
-
R. Kayed, E. Head, J.L. Thompson, T.M. McIntire, S.C. Milton, C.W. Cotman, and C.G. Glabe Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300 2003 486 489 (Pubitemid 36444329)
-
(2003)
Science
, vol.300
, Issue.5618
, pp. 486-489
-
-
Kayed, R.1
Head, E.2
Thompson, J.L.3
McIntire, T.M.4
Milton, S.C.5
Cotman, C.W.6
Glabel, C.G.7
-
8
-
-
84655162704
-
Soluble Abeta oligomer production and toxicity
-
M.E. Larson, and S.E. Lesne Soluble Abeta oligomer production and toxicity J. Neurochem. 120 Suppl. 1 2012 125 139
-
(2012)
J. Neurochem.
, vol.120
, Issue.SUPPL. 1
, pp. 125-139
-
-
Larson, M.E.1
Lesne, S.E.2
-
9
-
-
80054761710
-
Modes of A beta toxicity in Alzheimer's disease
-
J. Gotz, A. Eckert, M. Matamales, L.M. Ittner, and X. Liu Modes of A beta toxicity in Alzheimer's disease Cell. Mol. Life Sci. 68 2011 3359 3375
-
(2011)
Cell. Mol. Life Sci.
, vol.68
, pp. 3359-3375
-
-
Gotz, J.1
Eckert, A.2
Matamales, M.3
Ittner, L.M.4
Liu, X.5
-
10
-
-
84355161488
-
Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin
-
H.A. Davies, J. Madine, and D.A. Middleton Solid-state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic amyloid polypeptide medin J. Pept. Sci. 18 2012 65 72
-
(2012)
J. Pept. Sci.
, vol.18
, pp. 65-72
-
-
Davies, H.A.1
Madine, J.2
Middleton, D.A.3
-
11
-
-
65249169320
-
Cross-β spine architecture of fibrils formed by the amyloidogenic segment NFGSVQFV of medin from solid-state NMR and X-ray fiber diffraction measurements
-
J. Madine, A. Copland, L.C. Serpell, and D.A. Middleton Cross-β spine architecture of fibrils formed by the amyloidogenic segment NFGSVQFV of medin from solid-state NMR and X-ray fiber diffraction measurements Biochemistry 48 2009 3089 3099
-
(2009)
Biochemistry
, vol.48
, pp. 3089-3099
-
-
Madine, J.1
Copland, A.2
Serpell, L.C.3
Middleton, D.A.4
-
12
-
-
45749101292
-
Design of an N-methylated peptide inhibitor of α-synuclein aggregation guided by solid-state NMR
-
DOI 10.1021/ja075356q
-
J. Madine, A.J. Doig, and D.A. Middleton Design of an N-methylated peptide inhibitor of α-synuclein aggregation guided by solid-state NMR J. Am. Chem. Soc. 130 2008 7873 7881 (Pubitemid 351875062)
-
(2008)
Journal of the American Chemical Society
, vol.130
, Issue.25
, pp. 7873-7881
-
-
Madine, J.1
Doig, A.J.2
Middleton, D.A.3
-
14
-
-
0038340980
-
Applications of solid state NMR to the structural characterization of amyloid fibrils: Methods and results
-
R. Tycko Applications of solid state NMR to the structural characterization of amyloid fibrils: methods and results Prog. Nucl. Magn. Reson. Spectrosc. 42 2003 53 68
-
(2003)
Prog. Nucl. Magn. Reson. Spectrosc.
, vol.42
, pp. 53-68
-
-
Tycko, R.1
-
15
-
-
33749509894
-
Characterization of Amyloid Structures at the Molecular Level by Solid State Nuclear Magnetic Resonance Spectroscopy
-
DOI 10.1016/S0076-6879(06)13006-2, PII S0076687906130062, Amyloid, Prions, and Other Protein Aggregates, Part C
-
R. Tycko Characterization of amyloid structures at the molecular level by solid state nuclear magnetic resonance spectroscopy Methods Enzymol. 413 2006 103 122 (Pubitemid 44528687)
-
(2006)
Methods in Enzymology
, vol.413
, pp. 103-122
-
-
Tycko, R.1
-
16
-
-
38849108169
-
Solid-state NMR spectroscopy of amyloid proteins
-
DOI 10.1002/cbic.200700630
-
H. Heise Solid-state NMR spectroscopy of amyloid proteins Chembiochem 9 2008 179 189 (Pubitemid 351196782)
-
(2008)
ChemBioChem
, vol.9
, Issue.2
, pp. 179-189
-
-
Heise, H.1
-
17
-
-
80053610643
-
Localized amyloids important in diseases outside the brain - Lessons from the islets of Langerhans and the thoracic aorta
-
G.T. Westermark, and P. Westermark Localized amyloids important in diseases outside the brain - lessons from the islets of Langerhans and the thoracic aorta FEBS J. 278 2011 3918 3929
-
(2011)
FEBS J.
, vol.278
, pp. 3918-3929
-
-
Westermark, G.T.1
Westermark, P.2
-
18
-
-
36248940276
-
Role of aggregated medin in the pathogenesis of thoracic aortic aneurysm and dissection
-
DOI 10.1038/labinvest.3700679, PII 3700679
-
S. Peng, A. Larsson, E. Wassberg, P. Gerwins, S. Thelin, X. Fu, and P. Westermark Role of aggregated medin in the pathogenesis of thoracic aortic aneurysm and dissection Lab. Invest. 87 2007 1195 1205 (Pubitemid 350126704)
-
(2007)
Laboratory Investigation
, vol.87
, Issue.12
, pp. 1195-1205
-
-
Peng, S.1
Larsson, A.2
Wassberg, E.3
Gerwins, P.4
Thelin, S.5
Fu, X.6
Westermark, P.7
-
19
-
-
0033587677
-
Medin: An integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid
-
DOI 10.1073/pnas.96.15.8669
-
B. Häggqvist, J. Näslund, K. Sletten, G.T. Westermark, G. Mucchiano, L.O. Tjernberg, C. Nordstedt, U. Engström, and P. Westermark Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid Proc. Natl. Acad. Sci. 96 1999 8669 8674 (Pubitemid 29354849)
-
(1999)
Proceedings of the National Academy of Sciences of the United States of America
, vol.96
, Issue.15
, pp. 8669-8674
-
-
Haggqvist, B.O.1
Naslund, J.2
Sletten, K.3
Westermark, G.T.4
Mucchiano, G.5
Tjernberg, L.O.6
Nordstedt, C.7
Engstrom, U.8
Westermark, P.9
-
20
-
-
34547897456
-
Unwinding fibril formation of medin, the peptide of the most common form of human amyloid
-
DOI 10.1016/j.bbrc.2007.06.187, PII S0006291X07014167
-
A. Larsson, L. Söderberg, G.T. Westermark, K. Sletten, U. Engström, L.O. Tjernberg, J. Näslund, and P. Westermark Unwinding fibril formation of medin, the peptide of the most common form of human amyloid Biochem. Biophys. Res. Commun. 361 2007 822 828 (Pubitemid 47259013)
-
(2007)
Biochemical and Biophysical Research Communications
, vol.361
, Issue.4
, pp. 822-828
-
-
Larsson, A.1
Soderberg, L.2
Westermark, G.T.3
Sletten, K.4
Engstrom, U.5
Tjernberg, L.O.6
Naslund, J.7
Westermark, P.8
-
21
-
-
79958768615
-
Production of recombinant peptides as fusions with SUMO
-
M. Satakarni, and R. Curtis Production of recombinant peptides as fusions with SUMO Protein Expr. Purif. 78 2011 113 119
-
(2011)
Protein Expr. Purif.
, vol.78
, pp. 113-119
-
-
Satakarni, M.1
Curtis, R.2
-
22
-
-
34247846396
-
A versatile ligation-independent cloning method suitable for high-throughput expression screening applications
-
N.S. Berrow, D. Alderton, S. Sainsbury, J. Nettleship, R. Assenberg, N. Rahman, D.I. Stuart, and R.J. Owens A versatile ligation-independent cloning method suitable for high-throughput expression screening applications Nucleic Acids Res. 35 2007
-
(2007)
Nucleic Acids Res.
, vol.35
-
-
Berrow, N.S.1
Alderton, D.2
Sainsbury, S.3
Nettleship, J.4
Assenberg, R.5
Rahman, N.6
Stuart, D.I.7
Owens, R.J.8
-
23
-
-
0014949207
-
Cleavage of structural proteins during the assembly of the head of bacteriophage T4
-
U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
-
(1970)
Nature
, vol.227
, pp. 680-685
-
-
Laemmli, U.K.1
-
24
-
-
0023472472
-
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
-
DOI 10.1016/0003-2697(87)90587-2
-
H. Schägger, and G. von Jagow Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379 (Pubitemid 18004907)
-
(1987)
Analytical Biochemistry
, vol.166
, Issue.2
, pp. 368-379
-
-
Schagger, H.1
Von Jagow, G.2
-
25
-
-
79956193503
-
Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation
-
M. Zhao, D. Cascio, M.R. Sawaya, and D. Eisenberg Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation Protein Sci. 20 2011 996 1004
-
(2011)
Protein Sci.
, vol.20
, pp. 996-1004
-
-
Zhao, M.1
Cascio, D.2
Sawaya, M.R.3
Eisenberg, D.4
-
26
-
-
33845967502
-
Aβ produced as a fusion to maltose binding protein can be readily purified and stably associates with copper and zinc
-
DOI 10.2174/092986607779117263
-
J. Caine, I. Volitakis, R. Cherny, J. Varghese, and I. Macreadie A beta produced as a fusion to maltose binding protein can be readily purified and stably associates with copper and zinc Protein Pept. Lett. 14 2007 83 86 (Pubitemid 46046956)
-
(2007)
Protein and Peptide Letters
, vol.14
, Issue.1
, pp. 83-86
-
-
Caine, J.1
Volitakis, I.2
Cherny, R.3
Varghese, J.4
Macreadie, I.5
-
27
-
-
67650022868
-
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
-
J.J.W. Wiltzius, S.A. Sievers, M.R. Sawaya, and D. Eisenberg Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process Protein Sci. 18 2009 1521 1530
-
(2009)
Protein Sci.
, vol.18
, pp. 1521-1530
-
-
Wiltzius, J.J.W.1
Sievers, S.A.2
Sawaya, M.R.3
Eisenberg, D.4
-
28
-
-
74649086711
-
The recombinant amyloid-beta peptide A beta 1-42 aggregates faster and is more neurotoxic than synthetic A beta 1-42
-
V.H. Finder, I. Vodopivec, R.M. Nitsch, and R. Glockshuber The recombinant amyloid-beta peptide A beta 1-42 aggregates faster and is more neurotoxic than synthetic A beta 1-42 J. Mol. Biol. 396 2010 9 18
-
(2010)
J. Mol. Biol.
, vol.396
, pp. 9-18
-
-
Finder, V.H.1
Vodopivec, I.2
Nitsch, R.M.3
Glockshuber, R.4
-
29
-
-
4544301224
-
Amyloidogenic hexapeptide fragment of medin: Homology to functional islet amyloid polypeptide fragments
-
DOI 10.1080/13506120412331272287
-
M. Reches, and E. Gazit Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments Amyloid 11 2004 81 89 (Pubitemid 39222404)
-
(2004)
Amyloid
, vol.11
, Issue.2
, pp. 81-89
-
-
Reches, M.1
Gazit, E.2
-
30
-
-
0031592945
-
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
-
DOI 10.1006/jmbi.1997.1348
-
M. Sunde, L.C. Serpell, M. Bartlam, P.E. Fraser, M.B. Pepys, and C.C.F. Blake Common core structure of amyloid fibrils by synchrotron X-ray diffraction J. Mol. Biol. 273 1997 729 739 (Pubitemid 27488813)
-
(1997)
Journal of Molecular Biology
, vol.273
, Issue.3
, pp. 729-739
-
-
Sunde, M.1
Serpell, L.C.2
Bartlam, M.3
Fraser, P.E.4
Pepys, M.B.5
Blake, C.C.F.6
-
31
-
-
84871953993
-
Site-specific identification of an Aβ fibril-heparin interaction site by using solid-state NMR spectroscopy
-
J. Madine, M.J. Pandya, M.R. Hicks, A. Rodger, E.A. Yates, S.E. Radford, and D.A. Middleton Site-specific identification of an Aβ fibril-heparin interaction site by using solid-state NMR spectroscopy Angew. Chem. 51 2012 13140 13143
-
(2012)
Angew. Chem.
, vol.51
, pp. 13140-13143
-
-
Madine, J.1
Pandya, M.J.2
Hicks, M.R.3
Rodger, A.4
Yates, E.A.5
Radford, S.E.6
Middleton, D.A.7
-
32
-
-
0037168655
-
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
-
DOI 10.1073/pnas.262663499
-
A.T. Petkova, Y. Ishii, J.J. Balbach, O.N. Antzutkin, R.D. Leapman, F. Delaglio, and R. Tycko A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR Proc. Natl. Acad. Sci. U.S.A. 99 2002 16742 16747 (Pubitemid 36034043)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.26
, pp. 16742-16747
-
-
Petkova, A.T.1
Ishii, Y.2
Balbach, J.J.3
Antzutkin, O.N.4
Leapman, R.D.5
Delaglio, F.6
Tycko, R.7
-
33
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
-
DOI 10.1126/science.1105850
-
A.T. Petkova, R.D. Leapman, Z.H. Guo, W.M. Yau, M.P. Mattson, and R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils Science 307 2005 262 265 (Pubitemid 40116242)
-
(2005)
Science
, vol.307
, Issue.5707
, pp. 262-265
-
-
Petkova, A.T.1
Leapman, R.D.2
Guo, Z.3
Yau, W.-M.4
Mattson, M.P.5
Tycko, R.6
-
34
-
-
66149140617
-
Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
-
A.K. Paravastu, I. Qahwash, R.D. Leapman, S.C. Meredith, and R. Tycko Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure Proc. Natl. Acad. Sci. U.S.A. 106 2009 7443 7448
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 7443-7448
-
-
Paravastu, A.K.1
Qahwash, I.2
Leapman, R.D.3
Meredith, S.C.4
Tycko, R.5
-
35
-
-
80051673221
-
SHIFTX2: Significantly improved protein chemical shift prediction
-
B. Han, Y. Liu, S. Ginzinger, and D. Wishart SHIFTX2: significantly improved protein chemical shift prediction J. Biomol. NMR 50 2011 43 57
-
(2011)
J. Biomol. NMR
, vol.50
, pp. 43-57
-
-
Han, B.1
Liu, Y.2
Ginzinger, S.3
Wishart, D.4
-
36
-
-
0036129107
-
Probability-based protein secondary structure identification using combined NMR chemical-shift data
-
DOI 10.1110/ps.3180102
-
Y. Wang, and O. Jardetzky Probability-based protein secondary structure identification using combined NMR chemical-shift data Protein Sci. 11 2002 852 861 (Pubitemid 34241293)
-
(2002)
Protein Science
, vol.11
, Issue.4
, pp. 852-861
-
-
Wang, Y.1
Jardetzky, O.2
|