-
1
-
-
33646093028
-
Polymorphysm and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy
-
Anderson M., Bocharova O.V., Makarava N., Breydo L., Salnikov V.V., Baskakov I.V. Polymorphysm and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. J. Mol. Biol. 2006, 358:580-596.
-
(2006)
J. Mol. Biol.
, vol.358
, pp. 580-596
-
-
Anderson, M.1
Bocharova, O.V.2
Makarava, N.3
Breydo, L.4
Salnikov, V.V.5
Baskakov, I.V.6
-
2
-
-
34547638271
-
Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein
-
Atarashi R., Moore R.A., Sim V.L., Hughson A.G., Dorward D.W., Onwubiko H.A., Priola S.A., Caughey B. Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein. Nat. Methods 2007, 4:645-650.
-
(2007)
Nat. Methods
, vol.4
, pp. 645-650
-
-
Atarashi, R.1
Moore, R.A.2
Sim, V.L.3
Hughson, A.G.4
Dorward, D.W.5
Onwubiko, H.A.6
Priola, S.A.7
Caughey, B.8
-
3
-
-
50849113452
-
A C-terminal protease-resistant prion fragment distinguishes ovine "CH1641-like" scrapie from bovine classical and L-type BSE in ovine transgenic mice
-
Baron T., Bencsik A., Vulin J., Biacabe A.G., Morignat E., Verchere J., Betemps D. A C-terminal protease-resistant prion fragment distinguishes ovine "CH1641-like" scrapie from bovine classical and L-type BSE in ovine transgenic mice. PLOS Pathog. 2008, 4:e1000137.
-
(2008)
PLOS Pathog.
, vol.4
, pp. e1000137
-
-
Baron, T.1
Bencsik, A.2
Vulin, J.3
Biacabe, A.G.4
Morignat, E.5
Verchere, J.6
Betemps, D.7
-
4
-
-
0037077234
-
Pathway complexity of prion protein assembly into amyloid
-
Baskakov I.V., Legname G., Baldwin M.A., Prusiner S.B., Cohen F.E. Pathway complexity of prion protein assembly into amyloid. J. Biol. Chem. 2002, 277:21140-21148.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 21140-21148
-
-
Baskakov, I.V.1
Legname, G.2
Baldwin, M.A.3
Prusiner, S.B.4
Cohen, F.E.5
-
5
-
-
1342331870
-
The peculiar nature of unfolding of human prion protein
-
Baskakov I.V., Legname G., Gryczynski Z., Prusiner S.B. The peculiar nature of unfolding of human prion protein. Protein Sci. 2004, 13:586-595.
-
(2004)
Protein Sci.
, vol.13
, pp. 586-595
-
-
Baskakov, I.V.1
Legname, G.2
Gryczynski, Z.3
Prusiner, S.B.4
-
6
-
-
0022476747
-
Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
-
Basler K., Oesch B., Scott M., Westaway D., Wälchli M., Groth D.F., McKinley M.P., Prusiner S.B., Weissmann C. Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 1986, 46:417-428.
-
(1986)
Cell
, vol.46
, pp. 417-428
-
-
Basler, K.1
Oesch, B.2
Scott, M.3
Westaway, D.4
Wälchli, M.5
Groth, D.F.6
McKinley, M.P.7
Prusiner, S.B.8
Weissmann, C.9
-
7
-
-
34948908239
-
H-type bovine spongiform encephalopathy: complex molecular features and similarities with human prion diseases
-
Biacabe A.G., Jacobs J.G., Bencsik A., Langeveld J.P., Baron T.G. H-type bovine spongiform encephalopathy: complex molecular features and similarities with human prion diseases. Prion 2007, 1:61-68.
-
(2007)
Prion
, vol.1
, pp. 61-68
-
-
Biacabe, A.G.1
Jacobs, J.G.2
Bencsik, A.3
Langeveld, J.P.4
Baron, T.G.5
-
8
-
-
12544257523
-
In vitro conversion of full length mammalian prion protein produces amyloid form with physical property of PrPSc
-
Bocharova O.V., Breydo L., Parfenov A.S., Salnikov V.V., Baskakov I.V. In vitro conversion of full length mammalian prion protein produces amyloid form with physical property of PrPSc. J. Mol. Biol. 2005, 346:645-659.
-
(2005)
J. Mol. Biol.
, vol.346
, pp. 645-659
-
-
Bocharova, O.V.1
Breydo, L.2
Parfenov, A.S.3
Salnikov, V.V.4
Baskakov, I.V.5
-
9
-
-
17744379376
-
Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease
-
Bocharova O.V., Breydo L., Salnikov V.V., Gill A.C., Baskakov I.V. Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob Disease. Protein Science 2005, 14:1222-1232.
-
(2005)
Protein Science
, vol.14
, pp. 1222-1232
-
-
Bocharova, O.V.1
Breydo, L.2
Salnikov, V.V.3
Gill, A.C.4
Baskakov, I.V.5
-
10
-
-
33644858238
-
Annealing PrP amyloid firbils at high temperature results in extension of a proteinase K resistant core
-
Bocharova O.V., Makarava N., Breydo L., Anderson M., Salnikov V.V., Baskakov I.V. Annealing PrP amyloid firbils at high temperature results in extension of a proteinase K resistant core. J. Biol. Chem. 2006, 281:2373-2379.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 2373-2379
-
-
Bocharova, O.V.1
Makarava, N.2
Breydo, L.3
Anderson, M.4
Salnikov, V.V.5
Baskakov, I.V.6
-
11
-
-
0033610870
-
Strain-dependent differences in á-sheet conformations of abnormal prion protein
-
Caughey B., Raymond G.J., Bessen R.A. Strain-dependent differences in á-sheet conformations of abnormal prion protein. J. Biol. Chem. 1998, 273:32230-32235.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 32230-32235
-
-
Caughey, B.1
Raymond, G.J.2
Bessen, R.A.3
-
12
-
-
20344394154
-
Anchorless prion protein result in infectious amyloid disease without clinical scrapie
-
Chesebro B., Trifilo M., Race M., Meade-White K., Teng C., LaCasse R., Raymond L., Favara C., Baron G., Priola S., Caughey B., Masliah E., Oldstone M. Anchorless prion protein result in infectious amyloid disease without clinical scrapie. Science 2005, 308:1435-1439.
-
(2005)
Science
, vol.308
, pp. 1435-1439
-
-
Chesebro, B.1
Trifilo, M.2
Race, M.3
Meade-White, K.4
Teng, C.5
LaCasse, R.6
Raymond, L.7
Favara, C.8
Baron, G.9
Priola, S.10
Caughey, B.11
Masliah, E.12
Oldstone, M.13
-
13
-
-
37649000487
-
Molecular architecture of human prion protein amyloid: a parallel, in-register b-structure
-
Cobb N.J., Sonnichsen F.D., McHaourab H., Surewicz W. Molecular architecture of human prion protein amyloid: a parallel, in-register b-structure. Proc. Acad. Natl. Sci. U. S. A. 2007, 104:18946-18951.
-
(2007)
Proc. Acad. Natl. Sci. U. S. A.
, vol.104
, pp. 18946-18951
-
-
Cobb, N.J.1
Sonnichsen, F.D.2
McHaourab, H.3
Surewicz, W.4
-
14
-
-
73949160065
-
Design and construction of diverse mammalian prion strains
-
Colby D.W., Giles K., Legname G., Wille H., Baskakov I.V., DeArmond S.J., Prusiner S.B. Design and construction of diverse mammalian prion strains. Proc. Acad. Natl. Sci. U. S. A. 2009, 106:20417-20422.
-
(2009)
Proc. Acad. Natl. Sci. U. S. A.
, vol.106
, pp. 20417-20422
-
-
Colby, D.W.1
Giles, K.2
Legname, G.3
Wille, H.4
Baskakov, I.V.5
DeArmond, S.J.6
Prusiner, S.B.7
-
15
-
-
38049170554
-
Prion detection by an amyloid seeding assay
-
Colby D.W., Zhang Q., Wang S., Groth D., Legname G., Riesner D., Prusiner S.B. Prion detection by an amyloid seeding assay. Proc. Acad. Natl. Sci. U. S. A. 2007, 104:20914-20919.
-
(2007)
Proc. Acad. Natl. Sci. U. S. A.
, vol.104
, pp. 20914-20919
-
-
Colby, D.W.1
Zhang, Q.2
Wang, S.3
Groth, D.4
Legname, G.5
Riesner, D.6
Prusiner, S.B.7
-
16
-
-
1442330474
-
From conversion to aggregation: protofibrils formation of the prion protein
-
DeMarco M.L., Daggett V. From conversion to aggregation: protofibrils formation of the prion protein. Proc. Acad. Natl. Sci. U. S. A. 2004, 101:2293-2298.
-
(2004)
Proc. Acad. Natl. Sci. U. S. A.
, vol.101
, pp. 2293-2298
-
-
DeMarco, M.L.1
Daggett, V.2
-
17
-
-
79958024318
-
Probing structural differences between PrPC and PrPSc by surface nitration and acetylation: evidence of conformational change in the C-terminus
-
Gong B., Ramos A., Vazquez-Fernandez E., Silva C.J., Alonso J., Liu Z., Requena J. Probing structural differences between PrPC and PrPSc by surface nitration and acetylation: evidence of conformational change in the C-terminus. Biochemistry 2011, 50:4963-4972.
-
(2011)
Biochemistry
, vol.50
, pp. 4963-4972
-
-
Gong, B.1
Ramos, A.2
Vazquez-Fernandez, E.3
Silva, C.J.4
Alonso, J.5
Liu, Z.6
Requena, J.7
-
18
-
-
84864009032
-
Assessment of strain-specific PrPSc elongation rates revealed a transformation of PrPSc properties during protein misfolding cyclic amplification
-
Gonzalez-Montalban N., Baskakov I.V. Assessment of strain-specific PrPSc elongation rates revealed a transformation of PrPSc properties during protein misfolding cyclic amplification. PLoS ONE 2012, 7:0041210.
-
(2012)
PLoS ONE
, vol.7
, pp. 0041210
-
-
Gonzalez-Montalban, N.1
Baskakov, I.V.2
-
19
-
-
79952213492
-
Highly efficient protein misfolding cyclic amplification
-
Gonzalez-Montalban N., Makarava N., Ostapchenko V.G., Savtchenko R., Alexeeva I., Rohwer R.G., Baskakov I.V. Highly efficient protein misfolding cyclic amplification. PLoS Pathog. 2011, 7:e1001277.
-
(2011)
PLoS Pathog.
, vol.7
, pp. e1001277
-
-
Gonzalez-Montalban, N.1
Makarava, N.2
Ostapchenko, V.G.3
Savtchenko, R.4
Alexeeva, I.5
Rohwer, R.G.6
Baskakov, I.V.7
-
20
-
-
80052702962
-
Relationship between conformational stability and amplification efficiency of prions
-
Gonzalez-Montalban N., Makarava N., Savtchenko R., Baskakov I.V. Relationship between conformational stability and amplification efficiency of prions. Biochemistry 2011, 50:7933-7940.
-
(2011)
Biochemistry
, vol.50
, pp. 7933-7940
-
-
Gonzalez-Montalban, N.1
Makarava, N.2
Savtchenko, R.3
Baskakov, I.V.4
-
21
-
-
2942616602
-
Evidance for assembly of prions with left-handed b-helices into trimers
-
Govaerts C., Wille H., Prusiner S.B., Cohen F.E. Evidance for assembly of prions with left-handed b-helices into trimers. Proc. Acad. Natl. Sci. U. S. A. 2004, 101:8342-8347.
-
(2004)
Proc. Acad. Natl. Sci. U. S. A.
, vol.101
, pp. 8342-8347
-
-
Govaerts, C.1
Wille, H.2
Prusiner, S.B.3
Cohen, F.E.4
-
22
-
-
84896033164
-
Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongoform encephalopathies
-
Jeffrey M., McGovern G., Makarava N., Gonzalez L., Kim Y.S., Rohwer R.G., Baskakov I.V. Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongoform encephalopathies. Neuropathol. Appl. Neurobiol. 2014, 40:296-310.
-
(2014)
Neuropathol. Appl. Neurobiol.
, vol.40
, pp. 296-310
-
-
Jeffrey, M.1
McGovern, G.2
Makarava, N.3
Gonzalez, L.4
Kim, Y.S.5
Rohwer, R.G.6
Baskakov, I.V.7
-
23
-
-
84883688262
-
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
-
Jucker M., Walker L.C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 2013, 501:45-51.
-
(2013)
Nature
, vol.501
, pp. 45-51
-
-
Jucker, M.1
Walker, L.C.2
-
24
-
-
0029819057
-
Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain
-
Kocisko D.A., Lansbury J.P.T., Caughey B. Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain. Biochemistry 1996, 35:13434-13442.
-
(1996)
Biochemistry
, vol.35
, pp. 13434-13442
-
-
Kocisko, D.A.1
Lansbury, J.P.T.2
Caughey, B.3
-
25
-
-
84886679165
-
Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles
-
Kovacs G.G., Makarava N., Savtchenko R., Baskakov I.V. Atypical and classical forms of the disease-associated state of the prion protein exhibit distinct neuronal tropism, deposition patterns, and lesion profiles. Am. J. Pathol. 2013, 183:1539-1547.
-
(2013)
Am. J. Pathol.
, vol.183
, pp. 1539-1547
-
-
Kovacs, G.G.1
Makarava, N.2
Savtchenko, R.3
Baskakov, I.V.4
-
26
-
-
33745620145
-
Two-rung model of a left-handed b-helix for prions explains species barrier and strain variation in transmissible spongiform encephalopathies
-
Langedijk J.P.M., Fuentes G., Boshuizen R., Bonvin A.M.J.J. Two-rung model of a left-handed b-helix for prions explains species barrier and strain variation in transmissible spongiform encephalopathies. J. Mol. Biol. 2006, 360:907-920.
-
(2006)
J. Mol. Biol.
, vol.360
, pp. 907-920
-
-
Langedijk, J.P.M.1
Fuentes, G.2
Boshuizen, R.3
Bonvin, A.M.J.J.4
-
27
-
-
1842791529
-
Flexible N-terminal region of prion protein influences conformation of protease resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro
-
Lawson V.A., Priola S.A., Meade-White K., Lawton M., Chesebro B. Flexible N-terminal region of prion protein influences conformation of protease resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro. J. Biol. Chem. 2004, 279:13689-13695.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 13689-13695
-
-
Lawson, V.A.1
Priola, S.A.2
Meade-White, K.3
Lawton, M.4
Chesebro, B.5
-
28
-
-
47049117171
-
The same primary structure of the prion protein yields two distinct self-propagating states
-
Makarava N., Baskakov I.V. The same primary structure of the prion protein yields two distinct self-propagating states. J. Biol. Chem. 2008, 283:15988-15996.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 15988-15996
-
-
Makarava, N.1
Baskakov, I.V.2
-
29
-
-
84864633028
-
Purification and fibrillation of full-length recombinant PrP
-
Makarava N., Baskakov I.V. Purification and fibrillation of full-length recombinant PrP. Methods Mol. Biol. 2012, 849:33-52.
-
(2012)
Methods Mol. Biol.
, vol.849
, pp. 33-52
-
-
Makarava, N.1
Baskakov, I.V.2
-
30
-
-
84892874469
-
The evolution of transmissible prions: the role of deformed templating
-
Makarava N., Baskakov I.V. The evolution of transmissible prions: the role of deformed templating. PLOS Pathog. 2013, 9:e1003759.
-
(2013)
PLOS Pathog.
, vol.9
, pp. e1003759
-
-
Makarava, N.1
Baskakov, I.V.2
-
31
-
-
77449142074
-
Recombinant prion protein induces a new transmissible prion disease in wild type animals
-
Makarava N., Kovacs G.G., Bocharova O.V., Savtchenko R., Alexeeva I., Budka H., Rohwer R.G., Baskakov I.V. Recombinant prion protein induces a new transmissible prion disease in wild type animals. Acta Neuropathol. 2010, 119:177-187.
-
(2010)
Acta Neuropathol.
, vol.119
, pp. 177-187
-
-
Makarava, N.1
Kovacs, G.G.2
Bocharova, O.V.3
Savtchenko, R.4
Alexeeva, I.5
Budka, H.6
Rohwer, R.G.7
Baskakov, I.V.8
-
32
-
-
84855290517
-
Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease
-
Makarava N., Kovacs G.G., Savtchenko R., Alexeeva I., Budka H., Rohwer R.G., Baskakov I.V. Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease. PLoS Pathog. 2011, 7:e1002419.
-
(2011)
PLoS Pathog.
, vol.7
, pp. e1002419
-
-
Makarava, N.1
Kovacs, G.G.2
Savtchenko, R.3
Alexeeva, I.4
Budka, H.5
Rohwer, R.G.6
Baskakov, I.V.7
-
33
-
-
84865740820
-
Stabilization of a prion strain of synthetic origin requires multiple serial passages
-
Makarava N., Kovacs G.G., Savtchenko R., Alexeeva I., Budka H., Rohwer R.G., Baskakov I.V. Stabilization of a prion strain of synthetic origin requires multiple serial passages. J. Biol. Chem. 2012, 287:30205-30214.
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 30205-30214
-
-
Makarava, N.1
Kovacs, G.G.2
Savtchenko, R.3
Alexeeva, I.4
Budka, H.5
Rohwer, R.G.6
Baskakov, I.V.7
-
34
-
-
84861309020
-
A new mechanism for transmissible prion diseases
-
Makarava N., Kovacs G.G., Savtchenko R., Alexeeva I., Ostapchenko V.G., Budka H., Rohwer R.G., Baskakov I.V. A new mechanism for transmissible prion diseases. J. Neurosci. 2012, 32:7345-7355.
-
(2012)
J. Neurosci.
, vol.32
, pp. 7345-7355
-
-
Makarava, N.1
Kovacs, G.G.2
Savtchenko, R.3
Alexeeva, I.4
Ostapchenko, V.G.5
Budka, H.6
Rohwer, R.G.7
Baskakov, I.V.8
-
35
-
-
67649807925
-
Conformational switching within individual amyloid fibrils
-
Makarava N., Ostapchenko V.G., Savtchenko R., Baskakov I.V. Conformational switching within individual amyloid fibrils. J. Biol. Chem. 2009, 284:14386-14395.
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 14386-14395
-
-
Makarava, N.1
Ostapchenko, V.G.2
Savtchenko, R.3
Baskakov, I.V.4
-
36
-
-
84859193614
-
Fast and ultrasensitive method for quantitating prion infectivity titer
-
Makarava N., Savtchenko R., Alexeeva I., Rohwer R.G., Baskakov I.V. Fast and ultrasensitive method for quantitating prion infectivity titer. Nat. Commun. 2012, 3:741.
-
(2012)
Nat. Commun.
, vol.3
, pp. 741
-
-
Makarava, N.1
Savtchenko, R.2
Alexeeva, I.3
Rohwer, R.G.4
Baskakov, I.V.5
-
37
-
-
84872088301
-
Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification
-
Makarava N., Savtchenko R., Baskakov I.V. Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification. J. Biol. Chem. 2013, 288:33-41.
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 33-41
-
-
Makarava, N.1
Savtchenko, R.2
Baskakov, I.V.3
-
38
-
-
79960934693
-
Dissociation of infectivity from seeding ability in prions with alternate docking mechanism
-
Miller M.B., Geoghegan J.C., Supattapone S. Dissociation of infectivity from seeding ability in prions with alternate docking mechanism. PLoS Pathog. 2011, 7:e1002128.
-
(2011)
PLoS Pathog.
, vol.7
, pp. e1002128
-
-
Miller, M.B.1
Geoghegan, J.C.2
Supattapone, S.3
-
39
-
-
33751572491
-
The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro
-
Nishina K., Deleault N.R., Mahal S., Baskakov I., Luhrs T., Riek R., Supattapone S. The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. Biochemistry 2006, 45:14129-14139.
-
(2006)
Biochemistry
, vol.45
, pp. 14129-14139
-
-
Nishina, K.1
Deleault, N.R.2
Mahal, S.3
Baskakov, I.4
Luhrs, T.5
Riek, R.6
Supattapone, S.7
-
40
-
-
1942533390
-
Effects of different experimental conditions on the PrPSc core generated by protease digestion
-
Notari S., Capellari S., Giese A., Westner I., Baruzzi A., Ghetti B., Gambetti P., Kretzschmar H.A., Parchi P. Effects of different experimental conditions on the PrPSc core generated by protease digestion. J. Biol. Chem. 2004, 279:16797-16804.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 16797-16804
-
-
Notari, S.1
Capellari, S.2
Giese, A.3
Westner, I.4
Baruzzi, A.5
Ghetti, B.6
Gambetti, P.7
Kretzschmar, H.A.8
Parchi, P.9
-
41
-
-
33744954409
-
Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay
-
Novitskaya V., Makarava N., Bellon A., Bocharova O.V., Bronstein I.B., Williamson R.A., Baskakov I.V. Probing the conformation of the prion protein within a single amyloid fibril using a novel immunoconformational assay. J. Biol. Chem. 2006, 281:15536-15545.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 15536-15545
-
-
Novitskaya, V.1
Makarava, N.2
Bellon, A.3
Bocharova, O.V.4
Bronstein, I.B.5
Williamson, R.A.6
Baskakov, I.V.7
-
42
-
-
0022005315
-
A cellular gene encodes scrapie PrP 27-30 protein
-
Oesch B., Westaway D., Wälchli M., McKinley M.P., Kent S.B.H., Aebersold R., Barry R.A., Tempst P., Teplow D.B., Hood L.E., Prusiner S.B., Weissmann C. A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985, 40:735-746.
-
(1985)
Cell
, vol.40
, pp. 735-746
-
-
Oesch, B.1
Westaway, D.2
Wälchli, M.3
McKinley, M.P.4
Kent, S.B.H.5
Aebersold, R.6
Barry, R.A.7
Tempst, P.8
Teplow, D.B.9
Hood, L.E.10
Prusiner, S.B.11
Weissmann, C.12
-
43
-
-
77954382827
-
Two amyloid states of the prion protein display significantly different folding patterns
-
Ostapchenko V.G., Sawaya M.R., Makarava N., Savtchenko R., Nilsson K.P., Eisenberg D., Baskakov I.V. Two amyloid states of the prion protein display significantly different folding patterns. J. Mol. Biol. 2010, 400:908-921.
-
(2010)
J. Mol. Biol.
, vol.400
, pp. 908-921
-
-
Ostapchenko, V.G.1
Sawaya, M.R.2
Makarava, N.3
Savtchenko, R.4
Nilsson, K.P.5
Eisenberg, D.6
Baskakov, I.V.7
-
44
-
-
12944253111
-
Genetic Influence on the structural variations of the abnormal prion protein
-
Parchi P., Zou W., Wang W., Brown P., Capellari S., Ghetti B., Kopp N., Schulz-Schaeffer W.J., Kretzschmar H.A., Head M.W., Ironside J.W., Gambetti P., Chen S.G. Genetic Influence on the structural variations of the abnormal prion protein. Proc. Acad. Natl. Sci. U. S. A. 2000, 97:10168-10172.
-
(2000)
Proc. Acad. Natl. Sci. U. S. A.
, vol.97
, pp. 10168-10172
-
-
Parchi, P.1
Zou, W.2
Wang, W.3
Brown, P.4
Capellari, S.5
Ghetti, B.6
Kopp, N.7
Schulz-Schaeffer, W.J.8
Kretzschmar, H.A.9
Head, M.W.10
Ironside, J.W.11
Gambetti, P.12
Chen, S.G.13
-
45
-
-
34248396416
-
Accumulation of prion protein in the brain that is not associated with transmissible disease
-
Piccardo P., Manson J.C., King D., Ghetti B., Barron R.M. Accumulation of prion protein in the brain that is not associated with transmissible disease. Proc. Acad. Natl. Sci. U. S. A. 2007, 104:4712-4717.
-
(2007)
Proc. Acad. Natl. Sci. U. S. A.
, vol.104
, pp. 4712-4717
-
-
Piccardo, P.1
Manson, J.C.2
King, D.3
Ghetti, B.4
Barron, R.M.5
-
46
-
-
0020321767
-
Novel proteinaceous infectious particles cause scrapie
-
Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216:136-144.
-
(1982)
Science
, vol.216
, pp. 136-144
-
-
Prusiner, S.B.1
-
47
-
-
84896908507
-
The structure of the infectious prion protein: experimental data and molecular models
-
Requena J.R., Wille H. The structure of the infectious prion protein: experimental data and molecular models. Prion 2014, 8:60-66.
-
(2014)
Prion
, vol.8
, pp. 60-66
-
-
Requena, J.R.1
Wille, H.2
-
48
-
-
49349117873
-
Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry
-
Sajnani G., Pastrana M.A., Dynin I., Onisko B., Requena J.R. Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry. J. Mol. Biol. 2008, 382:88-98.
-
(2008)
J. Mol. Biol.
, vol.382
, pp. 88-98
-
-
Sajnani, G.1
Pastrana, M.A.2
Dynin, I.3
Onisko, B.4
Requena, J.R.5
-
49
-
-
0141841804
-
Association of an 11-12kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt-Jakob disease and other prion diseases
-
Satoh K., Muramoto T., Tanaka T., Kitamoto N., Ironside J.W., Nagashima K., Yamada M., Sato T., Mohri S., Kitamoto T. Association of an 11-12kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt-Jakob disease and other prion diseases. J. Gen. Virol. 2003, 84:2885-2893.
-
(2003)
J. Gen. Virol.
, vol.84
, pp. 2885-2893
-
-
Satoh, K.1
Muramoto, T.2
Tanaka, T.3
Kitamoto, N.4
Ironside, J.W.5
Nagashima, K.6
Yamada, M.7
Sato, T.8
Mohri, S.9
Kitamoto, T.10
-
50
-
-
84898431660
-
Evaluating prion models based on comprehensive mutation data of mouse PrP
-
Shirai T., Saito M., Kobayashi A., Asano M., Hizume M., Ikeda S., Teruya K., Morita M., Kitamoto T. Evaluating prion models based on comprehensive mutation data of mouse PrP. Structure 2014, 8:560-571.
-
(2014)
Structure
, vol.8
, pp. 560-571
-
-
Shirai, T.1
Saito, M.2
Kobayashi, A.3
Asano, M.4
Hizume, M.5
Ikeda, S.6
Teruya, K.7
Morita, M.8
Kitamoto, T.9
-
51
-
-
22144432561
-
Molecular dynamics simulations indicate a possible role of parallel b-helices in seeded aggregation of poly-gln
-
Stork M., Giese A., Kretzchmar H.A., Tavan P. Molecular dynamics simulations indicate a possible role of parallel b-helices in seeded aggregation of poly-gln. Biophys. J. 2005, 88:2442-2451.
-
(2005)
Biophys. J.
, vol.88
, pp. 2442-2451
-
-
Stork, M.1
Giese, A.2
Kretzchmar, H.A.3
Tavan, P.4
-
52
-
-
34247856087
-
Site-specific conformational studies of PrP amyloid fibrils revealed two cooperative folding domain within amyloid structure
-
Sun Y., Breydo L., Makarava N., Yang Q., Bocharova O.V., Baskakov I.V. Site-specific conformational studies of PrP amyloid fibrils revealed two cooperative folding domain within amyloid structure. J. Biol. Chem. 2007, 282:9090-9097.
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 9090-9097
-
-
Sun, Y.1
Breydo, L.2
Makarava, N.3
Yang, Q.4
Bocharova, O.V.5
Baskakov, I.V.6
-
53
-
-
39049119728
-
Conformational stability of PrP amyloid firbils controls their smallest possible fragment size
-
Sun Y., Makarava N., Lee C.I., Laksanalamai P., Robb F.T., Baskakov I.V. Conformational stability of PrP amyloid firbils controls their smallest possible fragment size. J. Mol. Biol. 2008, 376:1155-1167.
-
(2008)
J. Mol. Biol.
, vol.376
, pp. 1155-1167
-
-
Sun, Y.1
Makarava, N.2
Lee, C.I.3
Laksanalamai, P.4
Robb, F.T.5
Baskakov, I.V.6
-
54
-
-
33644941607
-
Elongated oligomers assemble into mammalian PrP amyloid fibrils
-
Tattum M.H., Cohen-Krausz S., Thumanu K., Wharton C.W., Khalili-Shirazi A., Jackson G.S., Orlova E.V., Collinge J., Clarke A.R., Saibil H.R. Elongated oligomers assemble into mammalian PrP amyloid fibrils. J. Mol. Biol. 2006, 357:975-985.
-
(2006)
J. Mol. Biol.
, vol.357
, pp. 975-985
-
-
Tattum, M.H.1
Cohen-Krausz, S.2
Thumanu, K.3
Wharton, C.W.4
Khalili-Shirazi, A.5
Jackson, G.S.6
Orlova, E.V.7
Collinge, J.8
Clarke, A.R.9
Saibil, H.R.10
-
55
-
-
4043137988
-
Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein
-
Thomzig A., Spassov S., Friedrich M., Naumann D., Beekes M. Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein. J. Biol. Chem. 2004, 279:33854.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 33854
-
-
Thomzig, A.1
Spassov, S.2
Friedrich, M.3
Naumann, D.4
Beekes, M.5
-
56
-
-
78149307698
-
The a-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel á-sheet structure in prp fibrils: evidence from solid state nuclear magnetic resonance
-
Tycko R., Savtchenko R., Ostapchenko V.G., Makarava N., Baskakov I.V. The a-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel á-sheet structure in prp fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry 2010, 49:9488-9497.
-
(2010)
Biochemistry
, vol.49
, pp. 9488-9497
-
-
Tycko, R.1
Savtchenko, R.2
Ostapchenko, V.G.3
Makarava, N.4
Baskakov, I.V.5
-
57
-
-
84869785863
-
Structural organization of mammalian prions as probed by limited proteolysis
-
Vazquez-Fernandez E., Alonso J., Pastrana M.A., Ramos A., Stitz L., Vidal E., Dynin I., Petsch B., Silva C.J., Requena J.R. Structural organization of mammalian prions as probed by limited proteolysis. PLOS ONE 2012, 7:e50111.
-
(2012)
PLOS ONE
, vol.7
, pp. e50111
-
-
Vazquez-Fernandez, E.1
Alonso, J.2
Pastrana, M.A.3
Ramos, A.4
Stitz, L.5
Vidal, E.6
Dynin, I.7
Petsch, B.8
Silva, C.J.9
Requena, J.R.10
-
58
-
-
70350134002
-
Natural and synthetic prion structure from X-ray fiber diffraction
-
Wille H., Bian W., McDonald M., Kendall A., Colby D.W., Bloch L., Ollesh J., Borovinskiy A.L., Cohen F.E., Prusiner S.B., Stubbs G. Natural and synthetic prion structure from X-ray fiber diffraction. Proc. Acad. Natl. Sci. U. S. A. 2009, 106:16990-16995.
-
(2009)
Proc. Acad. Natl. Sci. U. S. A.
, vol.106
, pp. 16990-16995
-
-
Wille, H.1
Bian, W.2
McDonald, M.3
Kendall, A.4
Colby, D.W.5
Bloch, L.6
Ollesh, J.7
Borovinskiy, A.L.8
Cohen, F.E.9
Prusiner, S.B.10
Stubbs, G.11
-
59
-
-
0037133587
-
Structural studies of the scrapie prion protein by electron crystallography
-
Wille H., Michelitsch M.D., Guenebaut V., Supattapone S., Serban A., Cohen F.E., Agard D.A., Prusiner S.B. Structural studies of the scrapie prion protein by electron crystallography. Proc. Acad. Natl. Sci. U. S. A. 2002, 99:3563-3568.
-
(2002)
Proc. Acad. Natl. Sci. U. S. A.
, vol.99
, pp. 3563-3568
-
-
Wille, H.1
Michelitsch, M.D.2
Guenebaut, V.3
Supattapone, S.4
Serban, A.5
Cohen, F.E.6
Agard, D.A.7
Prusiner, S.B.8
-
60
-
-
23944494699
-
Structure of infectious prions: stabilization by domain swapping
-
Yang S., LeVine H., Onuchic J.N., Cox D.L. Structure of infectious prions: stabilization by domain swapping. FASEB J. 2005, 19:1778-1782.
-
(2005)
FASEB J.
, vol.19
, pp. 1778-1782
-
-
Yang, S.1
LeVine, H.2
Onuchic, J.N.3
Cox, D.L.4
-
61
-
-
84885446994
-
Recombinant human prion protein inhibits prion propagation in vitro
-
Yuan J., Zhan Y.A., Abskharon R., Xiao X., Martinez M.C., Zhou X., Kneale G., Mikol J., Lehmann S., Surewicz W.K., Castilla J., Steyaert J., Zhang S., Kong Q., Petersen R.B., Wohlkonig A., Zou W.Q. Recombinant human prion protein inhibits prion propagation in vitro. Sci. Rep. 2013, 3:2911.
-
(2013)
Sci. Rep.
, vol.3
, pp. 2911
-
-
Yuan, J.1
Zhan, Y.A.2
Abskharon, R.3
Xiao, X.4
Martinez, M.C.5
Zhou, X.6
Kneale, G.7
Mikol, J.8
Lehmann, S.9
Surewicz, W.K.10
Castilla, J.11
Steyaert, J.12
Zhang, S.13
Kong, Q.14
Petersen, R.B.15
Wohlkonig, A.16
Zou, W.Q.17
-
62
-
-
0141577720
-
Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease
-
Zou W.Q., Capellari S., Parchi P., Sy M.S., Gambetti P., Chen S.G. Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J. Biol. Chem. 2003, 278:40429-40436.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 40429-40436
-
-
Zou, W.Q.1
Capellari, S.2
Parchi, P.3
Sy, M.S.4
Gambetti, P.5
Chen, S.G.6
-
63
-
-
77955302607
-
Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein
-
Zou W.Q., Puoti G., Xiao X., Yuan J., Qing L., Cali I., Shimoji M., Langeveld J.P., Castellani R., Notari S., Crain B., Schmidt R.E., Geschwind M., DeArmond S.J., Cairns N.J., Dickson D., Honig L., Torres J.M., Mastrianni J., Capellari S., Giaccone G., Belay E.D., Schonberger L.B., Cohen M., Perry G., Kong Q., Parchi P., Tagliavini F., Gambetti P. Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein. Ann. Neurol. 2010, 68:162-172.
-
(2010)
Ann. Neurol.
, vol.68
, pp. 162-172
-
-
Zou, W.Q.1
Puoti, G.2
Xiao, X.3
Yuan, J.4
Qing, L.5
Cali, I.6
Shimoji, M.7
Langeveld, J.P.8
Castellani, R.9
Notari, S.10
Crain, B.11
Schmidt, R.E.12
Geschwind, M.13
DeArmond, S.J.14
Cairns, N.J.15
Dickson, D.16
Honig, L.17
Torres, J.M.18
Mastrianni, J.19
Capellari, S.20
Giaccone, G.21
Belay, E.D.22
Schonberger, L.B.23
Cohen, M.24
Perry, G.25
Kong, Q.26
Parchi, P.27
Tagliavini, F.28
Gambetti, P.29
more..
|