-
1
-
-
10944273371
-
Specificity of prion assembly in vivo [PSI+] and [PIN+] form separate structures in yeast
-
Bagriantsev, S., and S.W. Liebman. 2004. Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast. J. Biol. Chem. 279:51042-51048. http://dx.doi.org/10.1074/jbc. M410611200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 51042-51048
-
-
Bagriantsev, S.1
Liebman, S.W.2
-
2
-
-
48749104090
-
Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition
-
Bagriantsev, S.N., E.O. Gracheva, J.E. Richmond, and S.W. Liebman. 2008. Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol. Biol. Cell. 19:2433-2443. http://dx.doi.org/10.1091/mbc. E08-01-0078
-
(2008)
Mol. Biol. Cell.
, vol.19
, pp. 2433-2443
-
-
Bagriantsev, S.N.1
Gracheva, E.O.2
Richmond, J.E.3
Liebman, S.W.4
-
3
-
-
0037551741
-
Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
-
Caughey, B., and P.T. Lansbury. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-298. http://dx.doi.org/10.1146/annurev.neuro.26.010302.081142
-
(2003)
Annu. Rev. Neurosci.
, vol.26
, pp. 267-298
-
-
Caughey, B.1
Lansbury, P.T.2
-
4
-
-
0029052468
-
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
-
Chernoff, Y.O., S.L. Lindquist, B. Ono, S.G. Inge-Vechtomov, and S.W. Liebman. 1995. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science. 268:880-884. http://dx.doi.org/10.1126/science.7754373
-
(1995)
Science
, vol.268
, pp. 880-884
-
-
Chernoff, Y.O.1
Lindquist, S.L.2
Ono, B.3
Inge-Vechtomov, S.G.4
Liebman, S.W.5
-
5
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
Chiti, F., and C.M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366. http://dx.doi.org/10.1146/annurev.biochem.75.101304.123901
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
6
-
-
0031787871
-
Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease
-
Conway, K.A., J.D. Harper, and P.T. Lansbury. 1998. Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat. Med. 4:1318-1320. http://dx.doi.org/10.1038/3311
-
(1998)
Nat. Med.
, vol.4
, pp. 1318-1320
-
-
Conway, K.A.1
Harper, J.D.2
Lansbury, P.T.3
-
7
-
-
0030482356
-
Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae
-
Derkatch, I.L., Y.O. Chernoff, V.V. Kushnirov, S.G. Inge-Vechtomov, and S.W. Liebman. 1996. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics. 144:1375-1386.
-
(1996)
Genetics
, vol.144
, pp. 1375-1386
-
-
Derkatch, I.L.1
Chernoff, Y.O.2
Kushnirov, V.V.3
Inge-Vechtomov, S.G.4
Liebman, S.W.5
-
8
-
-
0032503968
-
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
-
Glover, J.R., and S. Lindquist. 1998. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 94:73-82. http://dx.doi.org/10.1016/S0092-8674(00)81223-4
-
(1998)
Cell
, vol.94
, pp. 73-82
-
-
Glover, J.R.1
Lindquist, S.2
-
9
-
-
67650162529
-
Remodeling of protein aggregates by Hsp104
-
Glover, J.R., and R. Lum. 2009. Remodeling of protein aggregates by Hsp104. Protein Pept. Lett. 16:587-597. http://dx.doi.org/10.2174/092986609788490087
-
(2009)
Protein Pept. Lett.
, vol.16
, pp. 587-597
-
-
Glover, J.R.1
Lum, R.2
-
10
-
-
33847662852
-
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide
-
Haass, C., and D.J. Selkoe. 2007. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 8:101-112. http://dx.doi.org/10.1038/nrm2101
-
(2007)
Nat. Rev. Mol. Cell Biol.
, vol.8
, pp. 101-112
-
-
Haass, C.1
Selkoe, D.J.2
-
11
-
-
0036708168
-
Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies
-
Kirkitadze, M.D., G. Bitan, and D.B. Teplow. 2002. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69:567-577. http://dx.doi.org/10.1002/jnr.10328
-
(2002)
J. Neurosci. Res.
, vol.69
, pp. 567-577
-
-
Kirkitadze, M.D.1
Bitan, G.2
Teplow, D.B.3
-
12
-
-
21044453723
-
Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo
-
Klyubin, I., D.M. Walsh, C.A. Lemere, W.K. Cullen, G.M. Shankar, V. Betts, E.T. Spooner, L. Jiang, R. Anwyl, D.J. Selkoe, and M.J. Rowan. 2005. Amyloid beta protein immunotherapy neutralizes Abeta oligomers that disrupt synaptic plasticity in vivo. Nat. Med. 11:556-561. http://dx.doi.org/10.1038/nm1234
-
(2005)
Nat. Med.
, vol.11
, pp. 556-561
-
-
Klyubin, I.1
Walsh, D.M.2
Lemere, C.A.3
Cullen, W.K.4
Shankar, G.M.5
Betts, V.6
Spooner, E.T.7
Jiang, L.8
Anwyl, R.9
Selkoe, D.J.10
Rowan, M.J.11
-
13
-
-
1542782213
-
Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
-
Kryndushkin, D.S., I.M. Alexandrov, M.D. Ter-Avanesyan, and V.V. Kushnirov. 2003. Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J. Biol. Chem. 278:49636-49643. http://dx.doi.org/10.1074/jbc. M307996200
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 49636-49643
-
-
Kryndushkin, D.S.1
Alexandrov, I.M.2
Ter-Avanesyan, M.D.3
Kushnirov, V.V.4
-
14
-
-
0344030333
-
Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein
-
Lasmézas, C.I., J.P. Deslys, O. Robain, A. Jaegly, V. Beringue, J.M. Peyrin, J.G. Fournier, J.J. Hauw, J. Rossier, and D. Dormont. 1997. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science. 275:402-405. http://dx.doi.org/10.1126/science.275.5298.402
-
(1997)
Science
, vol.275
, pp. 402-405
-
-
Lasmézas, C.I.1
Deslys, J.P.2
Robain, O.3
Jaegly, A.4
Beringue, V.5
Peyrin, J.M.6
Fournier, J.G.7
Hauw, J.J.8
Rossier, J.9
Dormont, D.10
-
15
-
-
33645038471
-
A specific amyloid-beta protein assembly in the brain impairs memory
-
Lesné, S., M.T. Koh, L. Kotilinek, R. Kayed, C.G. Glabe, A. Yang, M. Gallagher, and K.H. Ashe. 2006. A specific amyloid-beta protein assembly in the brain impairs memory. Nature. 440:352-357. http://dx.doi.org/10.1038/nature04533
-
(2006)
Nature
, vol.440
, pp. 352-357
-
-
Lesné, S.1
Koh, M.T.2
Kotilinek, L.3
Kayed, R.4
Glabe, C.G.5
Yang, A.6
Gallagher, M.7
Ashe, K.H.8
-
16
-
-
0033555530
-
The yeast [PSI+] prion: making sense of nonsense
-
Liebman, S.W., and I.L. Derkatch. 1999. The yeast [PSI+] prion: making sense of nonsense. J. Biol. Chem. 274:1181-1184. http://dx.doi.org/10.1074/jbc.274.3.1181
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 1181-1184
-
-
Liebman, S.W.1
Derkatch, I.L.2
-
17
-
-
3142657524
-
Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
-
Lum, R., J.M. Tkach, E. Vierling, and J.R. Glover. 2004. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279:29139-29146. http://dx.doi.org/10.1074/jbc. M403777200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 29139-29146
-
-
Lum, R.1
Tkach, J.M.2
Vierling, E.3
Glover, J.R.4
-
18
-
-
0036310663
-
Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast
-
Ness, F., P. Ferreira, B.S. Cox, and M.F. Tuite. 2002. Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast. Mol. Cell. Biol. 22:5593-5605. http://dx.doi.org/10.1128/MCB.22.15.5593-5605.2002
-
(2002)
Mol. Cell. Biol.
, vol.22
, pp. 5593-5605
-
-
Ness, F.1
Ferreira, P.2
Cox, B.S.3
Tuite, M.F.4
-
19
-
-
77249124926
-
Differences in prion strain conformations result from non-native interactions in a nucleus
-
Ohhashi, Y., K. Ito, B.H. Toyama, J.S. Weissman, and M. Tanaka. 2010. Differences in prion strain conformations result from non-native interactions in a nucleus. Nat. Chem. Biol. 6:225-230. http://dx.doi.org/10.1038/nchembio.306
-
(2010)
Nat. Chem. Biol.
, vol.6
, pp. 225-230
-
-
Ohhashi, Y.1
Ito, K.2
Toyama, B.H.3
Weissman, J.S.4
Tanaka, M.5
-
20
-
-
0029780647
-
Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
-
Patino, M.M., J.J. Liu, J.R. Glover, and S. Lindquist. 1996. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science. 273:622-626. http://dx.doi.org/10.1126/science.273.5275.622
-
(1996)
Science
, vol.273
, pp. 622-626
-
-
Patino, M.M.1
Liu, J.J.2
Glover, J.R.3
Lindquist, S.4
-
21
-
-
0029888121
-
Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
-
Paushkin, S.V., V.V. Kushnirov, V.N. Smirnov, and M.D. Ter-Avanesyan. 1996. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 15:3127-3134.
-
(1996)
EMBO J
, vol.15
, pp. 3127-3134
-
-
Paushkin, S.V.1
Kushnirov, V.V.2
Smirnov, V.N.3
Ter-Avanesyan, M.D.4
-
22
-
-
84861209811
-
PK- sensitive PrP is infectious and shares basic structural features with PK-resistant PrP
-
Sajnani, G., C.J. Silva, A. Ramos, M.A. Pastrana, B.C. Onisko, M.L. Erickson, E.M. Antaki, I. Dynin, E. Vázquez-Fernández, C.J. Sigurdson, et al. 2012. PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrP. PLoS Pathog. 8:e1002547. http://dx.doi.org/10.1371/journal.ppat.1002547
-
(2012)
PLoS Pathog
, vol.8
-
-
Sajnani, G.1
Silva, C.J.2
Ramos, A.3
Pastrana, M.A.4
Onisko, B.C.5
Erickson, M.L.6
Antaki, E.M.7
Dynin, I.8
Vázquez-Fernández, E.9
Sigurdson, C.J.10
-
23
-
-
0037461730
-
Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
-
Sánchez, I., C. Mahlke, and J. Yuan. 2003. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature. 421:373-379. http://dx.doi.org/10.1038/nature01301
-
(2003)
Nature
, vol.421
, pp. 373-379
-
-
Sánchez, I.1
Mahlke, C.2
Yuan, J.3
-
24
-
-
24644467295
-
Prion protein remodelling confers an immediate phenotypic switch
-
Satpute-Krishnan, P., and T.R. Serio. 2005. Prion protein remodelling confers an immediate phenotypic switch. Nature. 437:262-265. http://dx.doi.org/10.1038/nature03981
-
(2005)
Nature
, vol.437
, pp. 262-265
-
-
Satpute-Krishnan, P.1
Serio, T.R.2
-
25
-
-
33846973006
-
Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance
-
Satpute-Krishnan, P., S.X. Langseth, and T.R. Serio. 2007. Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol. 5:e24. http://dx.doi.org/10.1371/journal.pbio.0050024
-
(2007)
PLoS Biol
, vol.5
-
-
Satpute-Krishnan, P.1
Langseth, S.X.2
Serio, T.R.3
-
26
-
-
0034714351
-
Nucleated conformational conversion and the replication of conformational information by a prion determinant
-
Serio, T.R., A.G. Cashikar, A.S. Kowal, G.J. Sawicki, J.J. Moslehi, L. Serpell, M.F. Arnsdorf, and S.L. Lindquist. 2000. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science. 289:1317-1321. http://dx.doi.org/10.1126/science.289.5483.1317
-
(2000)
Science
, vol.289
, pp. 1317-1321
-
-
Serio, T.R.1
Cashikar, A.G.2
Kowal, A.S.3
Sawicki, G.J.4
Moslehi, J.J.5
Serpell, L.6
Arnsdorf, M.F.7
Lindquist, S.L.8
-
27
-
-
2942722444
-
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
-
Shorter, J., and S. Lindquist. 2004. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science. 304:1793-1797. http://dx.doi.org/10.1126/science.1098007
-
(2004)
Science
, vol.304
, pp. 1793-1797
-
-
Shorter, J.1
Lindquist, S.2
-
28
-
-
33746405081
-
Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
-
Shorter, J., and S. Lindquist. 2006. Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol. Cell. 23:425-438. http://dx.doi.org/10.1016/j.molcel.2006.05.042
-
(2006)
Mol. Cell.
, vol.23
, pp. 425-438
-
-
Shorter, J.1
Lindquist, S.2
-
29
-
-
24644448839
-
The most infectious prion protein particles
-
Silveira, J.R., G.J. Raymond, A.G. Hughson, R.E. Race, V.L. Sim, S.F. Hayes, and B. Caughey. 2005. The most infectious prion protein particles. Nature. 437:257-261. http://dx.doi.org/10.1038/nature03989
-
(2005)
Nature
, vol.437
, pp. 257-261
-
-
Silveira, J.R.1
Raymond, G.J.2
Hughson, A.G.3
Race, R.E.4
Sim, V.L.5
Hayes, S.F.6
Caughey, B.7
-
30
-
-
77749315510
-
Amyloid oligomers: diffuse oligomerbased transmission of yeast prions
-
Taguchi, H., and S. Kawai-Noma. 2010. Amyloid oligomers: diffuse oligomerbased transmission of yeast prions. FEBS J. 277:1359-1368. http://dx.doi.org/10.1111/j.1742-4658.2010.07569.x
-
(2010)
FEBS J
, vol.277
, pp. 1359-1368
-
-
Taguchi, H.1
Kawai-Noma, S.2
-
31
-
-
1642633056
-
Conformational variations in an infectious protein determine prion strain differences
-
Tanaka, M., P. Chien, N. Naber, R. Cooke, and J.S. Weissman. 2004. Conformational variations in an infectious protein determine prion strain differences. Nature. 428:323-328. http://dx.doi.org/10.1038/nature02392
-
(2004)
Nature
, vol.428
, pp. 323-328
-
-
Tanaka, M.1
Chien, P.2
Naber, N.3
Cooke, R.4
Weissman, J.S.5
-
32
-
-
34250866206
-
A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast
-
Taneja, V., M.L. Maddelein, N. Talarek, S.J. Saupe, and S.W. Liebman. 2007. A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast. Mol. Cell. 27:67-77. http://dx.doi.org/10.1016/j.molcel.2007.05.027
-
(2007)
Mol. Cell.
, vol.27
, pp. 67-77
-
-
Taneja, V.1
Maddelein, M.L.2
Talarek, N.3
Saupe, S.J.4
Liebman, S.W.5
-
33
-
-
40649098449
-
Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
-
Tessarz, P., A. Mogk, and B. Bukau. 2008. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol. Microbiol. 68:87-97. http://dx.doi.org/10.1111/j.1365-2958.2008.06135.x
-
(2008)
Mol. Microbiol.
, vol.68
, pp. 87-97
-
-
Tessarz, P.1
Mogk, A.2
Bukau, B.3
-
34
-
-
55949109442
-
In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
-
Tipton, K.A., K.J. Verges, and J.S. Weissman. 2008. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol. Cell. 32:584-591. http://dx.doi.org/10.1016/j.molcel.2008.11.003
-
(2008)
Mol. Cell.
, vol.32
, pp. 584-591
-
-
Tipton, K.A.1
Verges, K.J.2
Weissman, J.S.3
-
35
-
-
4143115896
-
Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation
-
Tkach, J.M., and J.R. Glover. 2004. Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J. Biol. Chem. 279:35692-35701. http://dx.doi.org/10.1074/jbc. M400782200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 35692-35701
-
-
Tkach, J.M.1
Glover, J.R.2
-
36
-
-
0037159185
-
Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes
-
Tzaban, S., G. Friedlander, O. Schonberger, L. Horonchik, Y. Yedidia, G. Shaked, R. Gabizon, and A. Taraboulos. 2002. Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes. Biochemistry. 41: 12868-12875. http://dx.doi.org/10.1021/bi025958g
-
(2002)
Biochemistry
, vol.41
, pp. 12868-12875
-
-
Tzaban, S.1
Friedlander, G.2
Schonberger, O.3
Horonchik, L.4
Yedidia, Y.5
Shaked, G.6
Gabizon, R.7
Taraboulos, A.8
-
37
-
-
70350147706
-
Sequestration of essential proteins causes prion associated toxicity in yeast
-
Vishveshwara, N., M.E. Bradley, and S.W. Liebman. 2009. Sequestration of essential proteins causes prion associated toxicity in yeast. Mol. Microbiol. 73:1101-1114. http://dx.doi.org/10.1111/j.1365-2958.2009.06836.x
-
(2009)
Mol. Microbiol.
, vol.73
, pp. 1101-1114
-
-
Vishveshwara, N.1
Bradley, M.E.2
Liebman, S.W.3
|