-
1
-
-
0024537756
-
Fluorescence microscopy in three dimensions
-
doi:10.1016/S0091-679X(08)60986-3
-
Agard, D.A., Y. Hiraoka, P. Shaw, and J.W. Sedat. 1989. Fluorescence microscopy in three dimensions. Methods Cell Biol. 30:353-377. doi:10.1016/S0091-679X(08)60986-3
-
(1989)
Methods Cell Biol.
, vol.30
, pp. 353-377
-
-
Agard, D.A.1
Hiraoka, Y.2
Shaw, P.3
Sedat, J.W.4
-
2
-
-
11144322815
-
On-chip single-cell observation assay for propagation dynamics of yeast Sup35 prionlike proteins
-
doi:10.1143/JJAP.43.L1429
-
Ayano, S., S. Noma, M. Yoshida, H. Taguchi, and K. Yasuda. 2004. On-chip single-cell observation assay for propagation dynamics of yeast Sup35 prionlike proteins. Jpn. J. Appl. Phys. 43:L1429-L1432. doi:10.1143/JJAP.43.L1429
-
(2004)
Jpn. J. Appl. Phys.
, vol.43
-
-
Ayano, S.1
Noma, S.2
Yoshida, M.3
Taguchi, H.4
Yasuda, K.5
-
3
-
-
48749104090
-
Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition
-
doi:10.1091/mbc.E08-01-0078
-
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. doi: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
-
4
-
-
0042660351
-
Fluorescence correlation spectroscopy of enzymatic DNA polymerization
-
doi:10.1021/bi980694c
-
Björling, S., M. Kinjo, Z. Földes-Papp, E. Hagman, P. Thyberg, and R. Rigler. 1998. Fluorescence correlation spectroscopy of enzymatic DNA polymerization. Biochemistry. 37:12971-12978. doi:10.1021/bi980694c
-
(1998)
Biochemistry
, vol.37
, pp. 12971-12978
-
-
Björling, S.1
Kinjo, M.2
Földes-Papp, Z.3
Hagman, E.4
Thyberg, P.5
Rigler, R.6
-
5
-
-
0029052468
-
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
-
doi:10.1126/science.7754373
-
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. doi: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
-
6
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
doi:10.1146/annurev.biochem.75.101304.123901
-
Chiti, F., and C.M. Dobson. 2006. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75:333-366. doi:10.1146/annurev.biochem. 75.101304.123901
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
7
-
-
84966138908
-
[PSI], a cytoplasmic suppressor of supersuppression in yeast
-
doi:10.1038/hdy.1965.65
-
Cox, B.S. 1965. [PSI], a cytoplasmic suppressor of supersuppression in yeast. Heredity. 20:505-521. doi:10.1038/hdy.1965.65
-
(1965)
Heredity
, vol.20
, pp. 505-521
-
-
Cox, B.S.1
-
8
-
-
58149181486
-
Hsp104 and ClpB: Protein disaggregating machines
-
doi:10.1016/j.tibs.2008.09.010
-
Doyle, S.M., and S. Wickner. 2009. Hsp104 and ClpB: protein disaggregating machines. Trends Biochem. Sci. 34:40-48. doi:10.1016/j.tibs.2008. 09.010
-
(2009)
Trends Biochem Sci
, vol.34
, pp. 40-48
-
-
Doyle, S.M.1
Wickner, S.2
-
9
-
-
30644474711
-
Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast
-
doi:10.1128/MCB.26.2.617-629.2006
-
Ganusova, E.E., L.N. Ozolins, S. Bhagat, G.P. Newnam, R.D. Wegrzyn, M.Y. Sherman, and Y.O. Chernoff. 2006. Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. Mol. Cell. Biol. 26:617-629. doi:10.1128/MCB.26.2.617-629.2006
-
(2006)
Mol. Cell. Biol.
, vol.26
, pp. 617-629
-
-
Ganusova, E.E.1
Ozolins, L.N.2
Bhagat, S.3
Newnam, G.P.4
Wegrzyn, R.D.5
Sherman, M.Y.6
Chernoff, Y.O.7
-
10
-
-
0030712145
-
Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
-
doi:10.1016/S0092-8674(00)80264-0
-
Glover, J.R., A.S. Kowal, E.C. Schirmer, M.M. Patino, J.J. Liu, and S. Lindquist. 1997. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell. 89:811-819. doi:10.1016/S0092-8674(00)80264-0
-
(1997)
Cell
, vol.89
, pp. 811-819
-
-
Glover, J.R.1
Kowal, A.S.2
Schirmer, E.C.3
Patino, M.M.4
Liu, J.J.5
Lindquist, S.6
-
11
-
-
50249107835
-
Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly
-
doi:10.1242/jcs.033597
-
Haraguchi, T., T. Kojidani, T. Koujin, T. Shimi, H. Osakada, C. Mori, A. Yamamoto, and Y. Hiraoka. 2008. Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly. J. Cell Sci. 121:2540-2554. doi:10.1242/jcs.033597
-
(2008)
J. Cell Sci.
, vol.121
, pp. 2540-2554
-
-
Haraguchi, T.1
Kojidani, T.2
Koujin, T.3
Shimi, T.4
Osakada, H.5
Mori, C.6
Yamamoto, A.7
Hiraoka, Y.8
-
12
-
-
0141989819
-
On-chip culture system for observation of isolated individual cells
-
doi:10.1039/b103931h
-
Inoue, I., Y. Wakamoto, H. Moriguchi, K. Okano, and K. Yasuda. 2001. On-chip culture system for observation of isolated individual cells. Lab Chip. 1:50-55. doi:10.1039/b103931h
-
(2001)
Lab Chip.
, vol.1
, pp. 50-55
-
-
Inoue, I.1
Wakamoto, Y.2
Moriguchi, H.3
Okano, K.4
Yasuda, K.5
-
13
-
-
10044227566
-
Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it
-
doi:10.1074/jbc.M408159200
-
Inoue, Y., H. Taguchi, A. Kishimoto, and M. Yoshida. 2004. Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it. J. Biol. Chem. 279:52319-52323. doi:10.1074/jbc.M408159200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 52319-52323
-
-
Inoue, Y.1
Taguchi, H.2
Kishimoto, A.3
Yoshida, M.4
-
14
-
-
33747470607
-
Dynamics of yeast prion aggregates in single living cells
-
DOI 10.1111/j.1365-2443.2006.01004.x
-
Kawai-Noma, S., S. Ayano, C.G. Pack, M. Kinjo, M. Yoshida, K. Yasuda, and H. Taguchi. 2006. Dynamics of yeast prion aggregates in single living cells. Genes Cells. 11:1085-1096. doi:10.1111/j.1365-2443.2006.01004.x (Pubitemid 44256386)
-
(2006)
Genes to Cells
, vol.11
, Issue.9
, pp. 1085-1096
-
-
Kawai-noma, S.1
Ayano, S.2
Pack, C.-G.3
Kinjo, M.4
Yoshida, M.5
Yasuda, K.6
Taguchi, H.7
-
15
-
-
69849100344
-
Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells
-
doi:10.1111/j.1365-2443.2009.01333.x
-
Kawai-Noma, S., C.G. Pack, T. Tsuji, M. Kinjo, and H. Taguchi. 2009. Single mother-daughter pair analysis to clarify the diffusion properties of yeast prion Sup35 in guanidine-HCl-treated [PSI] cells. Genes Cells. 14:1045-1054. doi:10.1111/j.1365-2443.2009.01333.x
-
(2009)
Genes Cells
, vol.14
, pp. 1045-1054
-
-
Kawai-Noma, S.1
Pack, C.G.2
Tsuji, T.3
Kinjo, M.4
Taguchi, H.5
-
16
-
-
0041825135
-
Analysis of yeast prion aggregates with amyloid-staining compound in vivo
-
doi:10.1247/csf.28.187
-
Kimura, Y., S. Koitabashi, and T. Fujita. 2003. Analysis of yeast prion aggregates with amyloid-staining compound in vivo. Cell Struct. Funct. 28:187-193. doi:10.1247/csf.28.187
-
(2003)
Cell Struct. Funct.
, vol.28
, pp. 187-193
-
-
Kimura, Y.1
Koitabashi, S.2
Fujita, T.3
-
17
-
-
1242340413
-
Beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers
-
doi:10.1016/j.bbrc.2004.01.117
-
Kishimoto, A., K. Hasegawa, H. Suzuki, H. Taguchi, K. Namba, and M. Yoshida. 2004. beta-Helix is a likely core structure of yeast prion Sup35 amyloid fibers. Biochem. Biophys. Res. Commun. 315:739-745. doi:10.1016/j.bbrc. 2004.01.117
-
(2004)
Biochem. Biophys. Res. Commun.
, vol.315
, pp. 739-745
-
-
Kishimoto, A.1
Hasegawa, K.2
Suzuki, H.3
Taguchi, H.4
Namba, K.5
Yoshida, M.6
-
18
-
-
0024352110
-
Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
-
Klunk, W.E., J.W. Pettegrew, and D.J. Abraham. 1989. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 37:1273-1281.
-
(1989)
J. Histochem. Cytochem.
, vol.37
, pp. 1273-1281
-
-
Klunk, W.E.1
Pettegrew, J.W.2
Abraham, D.J.3
-
19
-
-
1542782213
-
Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104
-
doi:10.1074/jbc.M307996200
-
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. doi: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
-
20
-
-
33644555537
-
Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
-
DOI 10.1038/sj.emboj.7600985, PII 7600985
-
Krzewska, J., and R. Melki. 2006. Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J. 25:822-833. doi:10.1038/sj. emboj.7600985 (Pubitemid 43292443)
-
(2006)
EMBO Journal
, vol.25
, Issue.4
, pp. 822-833
-
-
Krzewska, J.1
Melki, R.2
-
22
-
-
0024509805
-
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1
-
doi:10.1016/0003-2697(89)90046-8
-
Naiki, H., K. Higuchi, M. Hosokawa, and T. Takeda. 1989. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1. Anal. Biochem. 177:244-249. doi:10.1016/0003-2697(89)90046-8
-
(1989)
Anal. Biochem.
, vol.177
, pp. 244-249
-
-
Naiki, H.1
Higuchi, K.2
Hosokawa, M.3
Takeda, T.4
-
23
-
-
0033168398
-
Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy
-
doi:10.1002/(SICI)1097-0320(19990701)36:3〈247::AID-CYTO15〉3.0. CO;2-#
-
Pack, C.G., G. Nishimura, M. Tamura, K. Aoki, H. Taguchi, M. Yoshida, and M. Kinjo. 1999. Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy. Cytometry. 36: 247-253. doi:10.1002/(SICI)1097-0320(19990701)36:3〈247::AID-CYTO15〉3.0.CO;2-#
-
(1999)
Cytometry
, vol.36
, pp. 247-253
-
-
Pack, C.G.1
Nishimura, G.2
Tamura, M.3
Aoki, K.4
Taguchi, H.5
Yoshida, M.6
Kinjo, M.7
-
24
-
-
33751229633
-
Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs
-
DOI 10.1529/biophysj.105.079467
-
Pack, C., K. Saito, M. Tamura, and M. Kinjo. 2006. Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys. J. 91:3921-3936. doi:10.1529/biophysj.105.079467 (Pubitemid 44788334)
-
(2006)
Biophysical Journal
, vol.91
, Issue.10
, pp. 3921-3936
-
-
Pack, C.1
Saito, K.2
Tamura, M.3
Kinjo, M.4
-
25
-
-
0029780647
-
Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
-
doi:10.1126/science.273.5275.622
-
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. doi: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
-
26
-
-
52649114611
-
The use of lead citrate at high pH as an electron-opaque stain in electron microscopy
-
doi:10.1083/jcb.17.1.208
-
Reynolds, E.S. 1963. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J. Cell Biol. 17:208-212. doi:10.1083/jcb.17.1.208
-
(1963)
J. Cell Biol.
, vol.17
, pp. 208-212
-
-
Reynolds, E.S.1
-
27
-
-
24644467295
-
Prion protein remodelling confers an immediate phenotypic switch
-
DOI 10.1038/nature03981
-
Satpute-Krishnan, P., and T.R. Serio. 2005. Prion protein remodelling confers an immediate phenotypic switch. Nature. 437:262-265. doi:10.1038/nature03981 (Pubitemid 41294489)
-
(2005)
Nature
, vol.437
, Issue.7056
, pp. 262-265
-
-
Satpute-Krishnan, P.1
Serio, T.R.2
-
28
-
-
0036275447
-
Getting started with yeast
-
doi:10.1016/S0076-6879(02)50954-X
-
Sherman, F. 2002. Getting started with yeast. Methods Enzymol. 350:3-41. doi:10.1016/S0076-6879(02)50954-X
-
(2002)
Methods Enzymol.
, vol.350
, pp. 3-41
-
-
Sherman, F.1
-
29
-
-
2942722444
-
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
-
DOI 10.1126/science.1098007
-
Shorter, J., and S. Lindquist. 2004. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science. 304:1793-1797. doi:10.1126/science.1098007 (Pubitemid 38787894)
-
(2004)
Science
, vol.304
, Issue.5678
, pp. 1793-1797
-
-
Shorter, J.1
Lindquist, S.2
-
30
-
-
13844313010
-
Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication
-
doi:10.1128/EC.4.2.289-297.2005
-
Song, Y., Y.X. Wu, G. Jung, Y. Tutar, E. Eisenberg, L.E. Greene, and D.C. Masison. 2005. Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot. Cell. 4:289-297. doi:10.1128/EC.4.2.289-297.2005
-
(2005)
Eukaryot. Cell.
, vol.4
, pp. 289-297
-
-
Song, Y.1
Wu, Y.X.2
Jung, G.3
Tutar, Y.4
Eisenberg, E.5
Greene, L.E.6
Masison, D.C.7
-
31
-
-
0035844884
-
Prion filament networks in [Ure3] cells of Saccharomyces cerevisiae
-
doi:10.1083/jcb.153.6.1327
-
Speransky, V.V., K.L. Taylor, H.K. Edskes, R.B. Wickner, and A.C. Steven. 2001. Prion filament networks in [Ure3] cells of Saccharomyces cerevisiae. J. Cell Biol. 153:1327-1336. doi:10.1083/jcb.153.6.1327
-
(2001)
J. Cell Biol.
, vol.153
, pp. 1327-1336
-
-
Speransky, V.V.1
Taylor, K.L.2
Edskes, H.K.3
Wickner, R.B.4
Steven, A.C.5
-
32
-
-
77749315510
-
Amyloid oligomers: Diffuse oligomer-based transmission of yeast prions
-
doi:10.1111/j.1742-4658.2010.07569.x
-
Taguchi, H., and S. Kawai-Noma. 2010. Amyloid oligomers: diffuse oligomer-based transmission of yeast prions. FEBS J. 277:1359-1368. doi:10.1111/j.1742-4658.2010.07569.x
-
(2010)
FEBS J.
, vol.277
, pp. 1359-1368
-
-
Taguchi, H.1
Kawai-Noma, S.2
-
33
-
-
1642633056
-
Conformational variations in an infectious protein determine prion strain differences
-
DOI 10.1038/nature02392
-
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. doi:10.1038/nature02392 (Pubitemid 38418803)
-
(2004)
Nature
, vol.428
, Issue.6980
, pp. 323-328
-
-
Tanaka, M.1
Chien, P.2
Naber, N.3
Cooke, R.4
Weissman, J.S.5
-
34
-
-
0242636317
-
Propagation of yeast prions
-
doi:10.1038/nrm1247
-
Tuite, M.F., and B.S. Cox. 2003. Propagation of yeast prions. Nat. Rev. Mol. Cell Biol. 4:878-890. doi:10.1038/nrm1247
-
(2003)
Nat. Rev. Mol. Cell Biol.
, vol.4
, pp. 878-890
-
-
Tuite, M.F.1
Cox, B.S.2
-
35
-
-
0019604156
-
Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae
-
Tuite, M.F., C.R. Mundy, and B.S. Cox. 1981. Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics. 98:691-711.
-
(1981)
Genetics
, vol.98
, pp. 691-711
-
-
Tuite, M.F.1
Mundy, C.R.2
Cox, B.S.3
-
36
-
-
0038239944
-
On-chip singlecell microcultivation assay for monitoring environmental effects on isolated cells
-
doi:10.1016/S0006-291X(03)00794-0
-
Umehara, S., Y. Wakamoto, I. Inoue, and K. Yasuda. 2003. On-chip singlecell microcultivation assay for monitoring environmental effects on isolated cells. Biochem. Biophys. Res. Commun. 305:534-540. doi:10.1016/S0006- 291X(03)00794-0
-
(2003)
Biochem. Biophys. Res. Commun.
, vol.305
, pp. 534-540
-
-
Umehara, S.1
Wakamoto, Y.2
Inoue, I.3
Yasuda, K.4
-
37
-
-
0035179616
-
The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]
-
doi:10.1046/j.1365-2958.2001.02224.x
-
Zhou, P., I.L. Derkatch, and S.W. Liebman. 2001. The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]. Mol. Microbiol. 39:37-46. doi:10.1046/j.1365-2958.2001.02224.x
-
(2001)
Mol. Microbiol.
, vol.39
, pp. 37-46
-
-
Zhou, P.1
Derkatch, I.L.2
Liebman, S.W.3
|