-
1
-
-
0037059040
-
Chaperoning brain degeneration
-
The author reviews recent evidence from Drosophila models implicating protein surveillance machinery in neurodegenerative diseases
-
Bonini N.M. Chaperoning brain degeneration. Proc. Natl. Acad. Sci. USA. 99(Suppl 4):2002;16407-16411 The author reviews recent evidence from Drosophila models implicating protein surveillance machinery in neurodegenerative diseases.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, Issue.SUPPL. 4
, pp. 16407-16411
-
-
Bonini, N.M.1
-
2
-
-
0035394668
-
Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
-
Cummings C.J., Sun Y., Opal P., Antalffy B., Mestril R., Orr H.T., Dillmann W.H., Zoghbi H.Y. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10:2001;1511-1518.
-
(2001)
Hum. Mol. Genet.
, vol.10
, pp. 1511-1518
-
-
Cummings, C.J.1
Sun, Y.2
Opal, P.3
Antalffy, B.4
Mestril, R.5
Orr, H.T.6
Dillmann, W.H.7
Zoghbi, H.Y.8
-
3
-
-
0036468432
-
Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
-
The authors used a Drosophila model of PD to show that overexpression of the molecular chaperone Hsp70 suppressed α-synuclein neurotoxicity. Conversely, expression of a dominant negative Hsp70 accelerated disease progression and neuronal loss. Additional studies revealed that some Lewy bodies in human PD tissue contain the molecular chaperones Hsp40 and 70
-
Auluck P.K., Chan H.Y., Trojanowski J.Q., Lee V.M., Bonini N.M. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science. 295:2002;865-868 The authors used a Drosophila model of PD to show that overexpression of the molecular chaperone Hsp70 suppressed α-synuclein neurotoxicity. Conversely, expression of a dominant negative Hsp70 accelerated disease progression and neuronal loss. Additional studies revealed that some Lewy bodies in human PD tissue contain the molecular chaperones Hsp40 and 70.
-
(2002)
Science
, vol.295
, pp. 865-868
-
-
Auluck, P.K.1
Chan, H.Y.2
Trojanowski, J.Q.3
Lee, V.M.4
Bonini, N.M.5
-
4
-
-
0034703863
-
Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
-
Chan H.Y., Warrick J.M., Gray-Board G.L., Paulson H.L., Bonini N.M. Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum. Mol. Genet. 9:2000;2811-2820.
-
(2000)
Hum. Mol. Genet.
, vol.9
, pp. 2811-2820
-
-
Chan, H.Y.1
Warrick, J.M.2
Gray-Board, G.L.3
Paulson, H.L.4
Bonini, N.M.5
-
5
-
-
0034754875
-
Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
-
The authors of this paper describe aggresome-like structures in polyglutamine disease. The inclusions colocalize to the microtubule-organizing center, and recruit components of the 26S proteasome, various chaperones and other proteins. Proteasome inhibition enhanced their formation
-
Waelter S., Boeddrich A., Lurz R., Scherzinger E., Lueder G., Lehrach H., Wanker E.E. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell. 12:2001;1393-1407 The authors of this paper describe aggresome-like structures in polyglutamine disease. The inclusions colocalize to the microtubule-organizing center, and recruit components of the 26S proteasome, various chaperones and other proteins. Proteasome inhibition enhanced their formation.
-
(2001)
Mol. Biol. Cell.
, vol.12
, pp. 1393-1407
-
-
Waelter, S.1
Boeddrich, A.2
Lurz, R.3
Scherzinger, E.4
Lueder, G.5
Lehrach, H.6
Wanker, E.E.7
-
6
-
-
0037137702
-
Parkin protects against the toxicity associated with mutant alpha-synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
-
Mutant α-synuclein was shown to inhibit proteasome activity. Inhibition was worsened by knock-down of the E3 ligase parkin. Conversely, overexpression of parkin rescued cells from toxicity associated with mutant α-synuclein. Mutant α-synuclein only affected catecholaminergic neurons, suggesting specificity to synuclein-mediated neurotoxicity
-
Petrucelli L., O'Farrell C., Lockhart P.J., Baptista M., Kehoe K., Vink L., Choi P., Wolozin B., Farrer M., Hardy J.et al. Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron. 36:2002;1007-1019 Mutant α-synuclein was shown to inhibit proteasome activity. Inhibition was worsened by knock-down of the E3 ligase parkin. Conversely, overexpression of parkin rescued cells from toxicity associated with mutant α-synuclein. Mutant α-synuclein only affected catecholaminergic neurons, suggesting specificity to synuclein-mediated neurotoxicity.
-
(2002)
Neuron
, vol.36
, pp. 1007-1019
-
-
Petrucelli, L.1
O'Farrell, C.2
Lockhart, P.J.3
Baptista, M.4
Kehoe, K.5
Vink, L.6
Choi, P.7
Wolozin, B.8
Farrer, M.9
Hardy, J.10
-
7
-
-
0037108725
-
Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
-
Verhoef L.G., Lindsten K., Masucci M.G., Dantuma N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11:2002;2689-2700.
-
(2002)
Hum. Mol. Genet.
, vol.11
, pp. 2689-2700
-
-
Verhoef, L.G.1
Lindsten, K.2
Masucci, M.G.3
Dantuma, N.P.4
-
8
-
-
0034730172
-
Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
-
Lam Y.A., Pickart C.M., Alban A., Landon M., Jamieson C., Ramage R., Mayer R.J., Layfield R. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 97:2000;9902-9906.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 9902-9906
-
-
Lam, Y.A.1
Pickart, C.M.2
Alban, A.3
Landon, M.4
Jamieson, C.5
Ramage, R.6
Mayer, R.J.7
Layfield, R.8
-
9
-
-
0035947372
-
Impairment of the ubiquitin-proteasome system by protein aggregation
-
Using a reporter cell line that expresses GFP modified with a degron (a protein sequence that targets a protein for degradation), the authors observed an increase in GFP fluorescence when the proteasome was pharmacologically inhibited or when two different mutant proteins formed aggregates in the cell. This was the first paper to clearly demonstrate proteasome inhibition in cellular models of neurodegeneration
-
Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1552-1555 Using a reporter cell line that expresses GFP modified with a degron (a protein sequence that targets a protein for degradation), the authors observed an increase in GFP fluorescence when the proteasome was pharmacologically inhibited or when two different mutant proteins formed aggregates in the cell. This was the first paper to clearly demonstrate proteasome inhibition in cellular models of neurodegeneration.
-
(2001)
Science
, vol.292
, pp. 1552-1555
-
-
Bence, N.F.1
Sampat, R.M.2
Kopito, R.R.3
-
10
-
-
0035870881
-
Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
-
The authors show that mutant α-synuclein expression leads to a nontoxic decrease in proteasomal activity, but subsequent treatment with a normally sublethal concentration of proteasome inhibitor caused apoptosis that could be blocked by cyclosporin A. This paper suggests that even mild perturbation of the UPP increases cellular susceptibility to stress
-
Tanaka Y., Engelender S., Igarashi S., Rao R.K., Wanner T., Tanzi R.E., Sawa A., Dawson V.L., Dawson T.M., Ross C.A. Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Hum. Mol. Genet. 10:2001;919-926 The authors show that mutant α-synuclein expression leads to a nontoxic decrease in proteasomal activity, but subsequent treatment with a normally sublethal concentration of proteasome inhibitor caused apoptosis that could be blocked by cyclosporin A. This paper suggests that even mild perturbation of the UPP increases cellular susceptibility to stress.
-
(2001)
Hum. Mol. Genet.
, vol.10
, pp. 919-926
-
-
Tanaka, Y.1
Engelender, S.2
Igarashi, S.3
Rao, R.K.4
Wanner, T.5
Tanzi, R.E.6
Sawa, A.7
Dawson, V.L.8
Dawson, T.M.9
Ross, C.A.10
-
11
-
-
0036083396
-
The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
-
Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82:2002;373-428.
-
(2002)
Physiol. Rev.
, vol.82
, pp. 373-428
-
-
Glickman, M.H.1
Ciechanover, A.2
-
12
-
-
0035292759
-
Themes and variations on ubiquitylation
-
The author of this review eloquently discusses the enzyme complexity involved in ubiquitination
-
Weissman A.M. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell. Biol. 2:2001;169-178 The author of this review eloquently discusses the enzyme complexity involved in ubiquitination.
-
(2001)
Nat. Rev. Mol. Cell. Biol.
, vol.2
, pp. 169-178
-
-
Weissman, A.M.1
-
13
-
-
0033176770
-
The base of the proteasome regulatory particle exhibits chaperone-like activity
-
Braun B.C., Glickman M., Kraft R., Dahlmann B., Kloetzel P.M., Finley D., Schmidt M. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat. Cell. Biol. 1:1999;221-226.
-
(1999)
Nat. Cell. Biol.
, vol.1
, pp. 221-226
-
-
Braun, B.C.1
Glickman, M.2
Kraft, R.3
Dahlmann, B.4
Kloetzel, P.M.5
Finley, D.6
Schmidt, M.7
-
15
-
-
0037179694
-
A cryptic protease couples deubiquitination and degradation by the proteasome
-
•] show that the 19S cap subunit POH1 (Rpn11 in yeast) is responsible for substrate deubiquitination before proteasomal degradation. This deubiquitinating activity is a rate-limiting step in proteasome degradation and loss of this function is lethal in yeast
-
•] show that the 19S cap subunit POH1 (Rpn11 in yeast) is responsible for substrate deubiquitination before proteasomal degradation. This deubiquitinating activity is a rate-limiting step in proteasome degradation and loss of this function is lethal in yeast.
-
(2002)
Nature
, vol.419
, pp. 403-407
-
-
Yao, T.1
Cohen, R.E.2
-
16
-
-
0037195907
-
Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
-
Alberti S., Demand J., Esser C., Emmerich N., Schild H., Hohfeld J. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J. Biol. Chem. 277:2002;45920-45927.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 45920-45927
-
-
Alberti, S.1
Demand, J.2
Esser, C.3
Emmerich, N.4
Schild, H.5
Hohfeld, J.6
-
17
-
-
0039172708
-
The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
-
Luders J., Demand J., Hohfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem. 275:2000;4613-4617.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 4613-4617
-
-
Luders, J.1
Demand, J.2
Hohfeld, J.3
-
18
-
-
0035293622
-
Protein regulation by monoubiquitin
-
An excellent review that discusses the role of monoubiquitination in regulating protein function
-
Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell. Biol. 2:2001;195-201 An excellent review that discusses the role of monoubiquitination in regulating protein function.
-
(2001)
Nat. Rev. Mol. Cell. Biol.
, vol.2
, pp. 195-201
-
-
Hicke, L.1
-
19
-
-
0035979738
-
Regulation of transcriptional activation domain function by ubiquitin
-
This paper highlights a non-traditional role for ubiquitin in activating and subsequently degrading the transcription factor VP16, and implicates the transcriptional activation domain as a critical region for ubiquitin-dependent regulation
-
Salghetti S.E., Caudy A.A., Chenoweth J.G., Tansey W.P. Regulation of transcriptional activation domain function by ubiquitin. Science. 293:2001;1651-1653 This paper highlights a non-traditional role for ubiquitin in activating and subsequently degrading the transcription factor VP16, and implicates the transcriptional activation domain as a critical region for ubiquitin-dependent regulation.
-
(2001)
Science
, vol.293
, pp. 1651-1653
-
-
Salghetti, S.E.1
Caudy, A.A.2
Chenoweth, J.G.3
Tansey, W.P.4
-
20
-
-
0037335034
-
How the ubiquitin-proteasome system controls transcription
-
This review highlights the intriguing relationship between transcriptional regulation and the UPP
-
Muratani M., Tansey W.P. How the ubiquitin-proteasome system controls transcription. Nat. Rev. Mol. Cell. Biol. 4:2003;192-201 This review highlights the intriguing relationship between transcriptional regulation and the UPP.
-
(2003)
Nat. Rev. Mol. Cell. Biol.
, vol.4
, pp. 192-201
-
-
Muratani, M.1
Tansey, W.P.2
-
21
-
-
0036345454
-
CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
-
CHIP was found to interact with the E3 ligase parkin, enhancing ubiquitination of Pael-R by this ligase. CHIP and Hsp70 overexpression, in conjunction with parkin, reduced cellular toxicity as a result of misfolded Pael-R. The greatest reduction in cell death was observed when CHIP, Hsp70 and parkin were coexpressed together
-
Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.I., Takahashi R. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell. 10:2002;55-67 CHIP was found to interact with the E3 ligase parkin, enhancing ubiquitination of Pael-R by this ligase. CHIP and Hsp70 overexpression, in conjunction with parkin, reduced cellular toxicity as a result of misfolded Pael-R. The greatest reduction in cell death was observed when CHIP, Hsp70 and parkin were coexpressed together.
-
(2002)
Mol. Cell.
, vol.10
, pp. 55-67
-
-
Imai, Y.1
Soda, M.2
Hatakeyama, S.3
Akagi, T.4
Hashikawa, T.5
Nakayama, K.I.6
Takahashi, R.7
-
22
-
-
0032846416
-
Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice
-
Saigoh K., Wang Y.L., Suh J.G., Yamanishi T., Sakai Y., Kiyosawa H., Harada T., Ichihara N., Wakana S., Kikuchi T.et al. Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice. Nat. Genet. 23:1999;47-51.
-
(1999)
Nat. Genet.
, vol.23
, pp. 47-51
-
-
Saigoh, K.1
Wang, Y.L.2
Suh, J.G.3
Yamanishi, T.4
Sakai, Y.5
Kiyosawa, H.6
Harada, T.7
Ichihara, N.8
Wakana, S.9
Kikuchi, T.10
-
23
-
-
0032190090
-
The ubiquitin pathway in Parkinson's disease
-
Leroy E., Boyer R., Auburger G., Leube B., Ulm G., Mezey E., Harta G., Brownstein M.J., Jonnalagada S., Chernova T.et al. The ubiquitin pathway in Parkinson's disease. Nature. 395:1998;451-452.
-
(1998)
Nature
, vol.395
, pp. 451-452
-
-
Leroy, E.1
Boyer, R.2
Auburger, G.3
Leube, B.4
Ulm, G.5
Mezey, E.6
Harta, G.7
Brownstein, M.J.8
Jonnalagada, S.9
Chernova, T.10
-
24
-
-
0037131567
-
The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
-
UCH-L1 appears to contain two enzymatic activities in vitro, acting both as a ubiquitin hydrolase and ubiquitin ligase. A polymorphic variant of UCH-L1 (S18Y) that decreases one's risk for PD has reduced ligase activity in vitro. The authors suggest that both ligase and hydrolase activities of UCH-L1 may be involved in disease pathogenesis
-
Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility. Cell. 111:2002;209-218 UCH-L1 appears to contain two enzymatic activities in vitro, acting both as a ubiquitin hydrolase and ubiquitin ligase. A polymorphic variant of UCH-L1 (S18Y) that decreases one's risk for PD has reduced ligase activity in vitro. The authors suggest that both ligase and hydrolase activities of UCH-L1 may be involved in disease pathogenesis.
-
(2002)
Cell
, vol.111
, pp. 209-218
-
-
Liu, Y.1
Fallon, L.2
Lashuel, H.A.3
Liu, Z.4
Lansbury P.T., Jr.5
-
25
-
-
0034282219
-
The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly
-
Ortolan T.G., Tongaonkar P., Lambertson D., Chen L., Schauber C., Madura K. The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly. Nat. Cell. Biol. 2:2000;601-608.
-
(2000)
Nat. Cell. Biol.
, vol.2
, pp. 601-608
-
-
Ortolan, T.G.1
Tongaonkar, P.2
Lambertson, D.3
Chen, L.4
Schauber, C.5
Madura, K.6
-
26
-
-
0035142877
-
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
-
Meacham G.C., Patterson C., Zhang W., Younger J.M., Cyr D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell. Biol. 3:2001;100-105.
-
(2001)
Nat. Cell. Biol.
, vol.3
, pp. 100-105
-
-
Meacham, G.C.1
Patterson, C.2
Zhang, W.3
Younger, J.M.4
Cyr, D.M.5
-
27
-
-
0036850456
-
Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
-
A Drosophila model of the polyglutamine disease spinobulbar muscular atrophy was used to show that chaperones and the proteasome work additively to modulate disease pathogenesis. The authors also show that another protein modification, the ubiquitin-like sumoylation, suppresses polyglutamine-mediated toxicity
-
Chan H.Y., Warrick J.M., Andriola I., Merry D., Bonini N.M. Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila. Hum. Mol. Genet. 11:2002;2895-2904 A Drosophila model of the polyglutamine disease spinobulbar muscular atrophy was used to show that chaperones and the proteasome work additively to modulate disease pathogenesis. The authors also show that another protein modification, the ubiquitin-like sumoylation, suppresses polyglutamine-mediated toxicity.
-
(2002)
Hum. Mol. Genet.
, vol.11
, pp. 2895-2904
-
-
Chan, H.Y.1
Warrick, J.M.2
Andriola, I.3
Merry, D.4
Bonini, N.M.5
-
28
-
-
0036606540
-
ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
-
Nishitoh H., Matsuzawa A., Tobiume K., Saegusa K., Takeda K., Inoue K., Hori S., Kakizuka A., Ichijo H. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16:2002;1345-1355.
-
(2002)
Genes Dev.
, vol.16
, pp. 1345-1355
-
-
Nishitoh, H.1
Matsuzawa, A.2
Tobiume, K.3
Saegusa, K.4
Takeda, K.5
Inoue, K.6
Hori, S.7
Kakizuka, A.8
Ichijo, H.9
-
29
-
-
0037114971
-
Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
-
Ryu E.J., Harding H.P., Angelastro J.M., Vitolo O.V., Ron D., Greene L.A. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J. Neurosci. 22:2002;10690-10698.
-
(2002)
J. Neurosci.
, vol.22
, pp. 10690-10698
-
-
Ryu, E.J.1
Harding, H.P.2
Angelastro, J.M.3
Vitolo, O.V.4
Ron, D.5
Greene, L.A.6
-
30
-
-
0037461730
-
Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
-
The authors used the anti-amyloid compound Congo red to disrupt preformed aggregates and to prevent nucleation of the mutant protein in cellular and animal models of polyglutamine disease. These effects correlated with preserved motor function and increased life span in a mouse model of HD
-
Sanchez I., Mahlke C., Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature. 421:2003;373-379 The authors used the anti-amyloid compound Congo red to disrupt preformed aggregates and to prevent nucleation of the mutant protein in cellular and animal models of polyglutamine disease. These effects correlated with preserved motor function and increased life span in a mouse model of HD.
-
(2003)
Nature
, vol.421
, pp. 373-379
-
-
Sanchez, I.1
Mahlke, C.2
Yuan, J.3
-
31
-
-
0037041426
-
Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
-
Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416:2002;535-539.
-
(2002)
Nature
, vol.416
, pp. 535-539
-
-
Walsh, D.M.1
Klyubin, I.2
Fadeeva, J.V.3
Cullen, W.K.4
Anwyl, R.5
Wolfe, M.S.6
Rowan, M.J.7
Selkoe, D.J.8
-
32
-
-
0037041420
-
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
-
In showing that even aggregates of non-disease proteins are sufficient to induce cell death, the authors suggest that neuronal cells are inherently susceptible to aggregated protein
-
Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511 In showing that even aggregates of non-disease proteins are sufficient to induce cell death, the authors suggest that neuronal cells are inherently susceptible to aggregated protein.
-
(2002)
Nature
, vol.416
, pp. 507-511
-
-
Bucciantini, M.1
Giannoni, E.2
Chiti, F.3
Baroni, F.4
Formigli, L.5
Zurdo, J.6
Taddei, N.7
Ramponi, G.8
Dobson, C.M.9
Stefani, M.10
-
33
-
-
0034578389
-
Aggresomes, inclusion bodies and protein aggregation
-
Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell. Biol. 10:2000;524-530.
-
(2000)
Trends Cell. Biol.
, vol.10
, pp. 524-530
-
-
Kopito, R.R.1
-
34
-
-
0037033074
-
Parkin accumulation in aggresomes due to proteasome impairment
-
Junn E., Lee S.S., Suhr U.T., Mouradian M.M. Parkin accumulation in aggresomes due to proteasome impairment. J. Biol. Chem. 277:2002;47870-47877.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 47870-47877
-
-
Junn, E.1
Lee, S.S.2
Suhr, U.T.3
Mouradian, M.M.4
-
35
-
-
0032576605
-
Aggresomes: A cellular response to misfolded proteins
-
Johnston J.A., Ward C.L., Kopito R.R. Aggresomes: a cellular response to misfolded proteins. J. Cell. Biol. 143:1998;1883-1898.
-
(1998)
J. Cell. Biol.
, vol.143
, pp. 1883-1898
-
-
Johnston, J.A.1
Ward, C.L.2
Kopito, R.R.3
-
36
-
-
0035910069
-
Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
-
Ma J., Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. USA. 98:2001;14955-14960.
-
(2001)
Proc. Natl. Acad. Sci. USA
, vol.98
, pp. 14955-14960
-
-
Ma, J.1
Lindquist, S.2
-
37
-
-
0034652127
-
Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
-
Krobitsch S., Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc. Natl. Acad. Sci. USA. 97:2000;1589-1594.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 1589-1594
-
-
Krobitsch, S.1
Lindquist, S.2
-
38
-
-
0037047123
-
Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis
-
•] demonstrate that aggregates of polyglutamine proteins are dynamic structures, with some proteins sequestered irreversibly whereas others associate transiently. These papers also suggest inclusions containing different polyglutamine proteins exhibit distinct protein-recruitment profiles and sequestration kinetics, perhaps providing clues to disease-specific pathogenesis
-
•] demonstrate that aggregates of polyglutamine proteins are dynamic structures, with some proteins sequestered irreversibly whereas others associate transiently. These papers also suggest inclusions containing different polyglutamine proteins exhibit distinct protein-recruitment profiles and sequestration kinetics, perhaps providing clues to disease-specific pathogenesis.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 9310-9315
-
-
Chai, Y.1
Shao, J.2
Miller, V.M.3
Williams, A.4
Paulson, H.L.5
-
41
-
-
0036850529
-
Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
-
Yang W., Dunlap J.R., Andrews R.B., Wetzel R. Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum. Mol. Genet. 11:2002;2905-2917.
-
(2002)
Hum. Mol. Genet.
, vol.11
, pp. 2905-2917
-
-
Yang, W.1
Dunlap, J.R.2
Andrews, R.B.3
Wetzel, R.4
-
42
-
-
0033391428
-
Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
-
Cummings C.J., Reinstein E., Sun Y., Antalffy B., Jiang Y., Ciechanover A., Orr H.T., Beaudet A.L., Zoghbi H.Y. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron. 24:1999;879-892.
-
(1999)
Neuron
, vol.24
, pp. 879-892
-
-
Cummings, C.J.1
Reinstein, E.2
Sun, Y.3
Antalffy, B.4
Jiang, Y.5
Ciechanover, A.6
Orr, H.T.7
Beaudet, A.L.8
Zoghbi, H.Y.9
-
43
-
-
0032475941
-
Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
-
Klement I.A., Skinner P.J., Kaytor M.D., Yi H., Hersch S.M., Clark H.B., Zoghbi H.Y., Orr H.T. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell. 95:1998;41-53.
-
(1998)
Cell
, vol.95
, pp. 41-53
-
-
Klement, I.A.1
Skinner, P.J.2
Kaytor, M.D.3
Yi, H.4
Hersch, S.M.5
Clark, H.B.6
Zoghbi, H.Y.7
Orr, H.T.8
-
44
-
-
18444386197
-
A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration
-
Watase K., Weeber E.J., Xu B., Antalffy B., Yuva-Paylor L., Hashimoto K., Kano M., Atkinson R., Sun Y., Armstrong D.L.et al. A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration. Neuron. 34:2002;905-919.
-
(2002)
Neuron
, vol.34
, pp. 905-919
-
-
Watase, K.1
Weeber, E.J.2
Xu, B.3
Antalffy, B.4
Yuva-Paylor, L.5
Hashimoto, K.6
Kano, M.7
Atkinson, R.8
Sun, Y.9
Armstrong, D.L.10
-
45
-
-
0037015081
-
Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
-
Chen S., Ferrone F.A., Wetzel R. Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc. Natl. Acad. Sci. USA. 99:2002;11884-11889.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 11884-11889
-
-
Chen, S.1
Ferrone, F.A.2
Wetzel, R.3
-
47
-
-
0035336658
-
Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
-
Jana N.R., Zemskov E.A., Wang G., Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet. 10:2001;1049-1059.
-
(2001)
Hum. Mol. Genet.
, vol.10
, pp. 1049-1059
-
-
Jana, N.R.1
Zemskov, E.A.2
Wang, G.3
Nukina, N.4
-
48
-
-
0036121310
-
Arfaptin 2 regulates the aggregation of mutant huntingtin protein
-
Peters P.J., Ning K., Palacios F., Boshans R.L., Kazantsev A., Thompson L.M., Woodman B., Bates G.P., D'Souza-Schorey C. Arfaptin 2 regulates the aggregation of mutant huntingtin protein. Nat. Cell. Biol. 4:2002;240-245.
-
(2002)
Nat. Cell. Biol.
, vol.4
, pp. 240-245
-
-
Peters, P.J.1
Ning, K.2
Palacios, F.3
Boshans, R.L.4
Kazantsev, A.5
Thompson, L.M.6
Woodman, B.7
Bates, G.P.8
D'Souza-Schorey, C.9
-
49
-
-
0035976835
-
Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
-
Tofaris G.K., Layfield R., Spillantini M.G. alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509:2001;22-26.
-
(2001)
FEBS Lett.
, vol.509
, pp. 22-26
-
-
Tofaris, G.K.1
Layfield, R.2
Spillantini, M.G.3
-
50
-
-
0034884622
-
Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells
-
Rideout H.J., Larsen K.E., Sulzer D., Stefanis L. Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells. J. Neurochem. 78:2001;899-908.
-
(2001)
J. Neurochem.
, vol.78
, pp. 899-908
-
-
Rideout, H.J.1
Larsen, K.E.2
Sulzer, D.3
Stefanis, L.4
-
51
-
-
0033030565
-
Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
-
Chai Y., Koppenhafer S.L., Shoesmith S.J., Perez M.K., Paulson H.L. Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8:1999;673-682.
-
(1999)
Hum. Mol. Genet.
, vol.8
, pp. 673-682
-
-
Chai, Y.1
Koppenhafer, S.L.2
Shoesmith, S.J.3
Perez, M.K.4
Paulson, H.L.5
-
52
-
-
0033607801
-
Degradation of alpha-synuclein by proteasome
-
Bennett M.C., Bishop J.F., Leng Y., Chock P.B., Chase T.N., Mouradian M.M. Degradation of alpha-synuclein by proteasome. J. Biol. Chem. 274:1999;33855-33858.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 33855-33858
-
-
Bennett, M.C.1
Bishop, J.F.2
Leng, Y.3
Chock, P.B.4
Chase, T.N.5
Mouradian, M.M.6
-
53
-
-
0037421691
-
SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity
-
Yoo S.Y., Pennesi M.E., Weeber E.J., Xu B., Atkinson R., Chen S., Armstrong D.L., Wu S.M., Sweatt J.D., Zoghbi H.Y. SCA7 knockin mice model human SCA7 and reveal gradual accumulation of mutant ataxin-7 in neurons and abnormalities in short-term plasticity. Neuron. 37:2003;383-401.
-
(2003)
Neuron
, vol.37
, pp. 383-401
-
-
Yoo, S.Y.1
Pennesi, M.E.2
Weeber, E.J.3
Xu, B.4
Atkinson, R.5
Chen, S.6
Armstrong, D.L.7
Wu, S.M.8
Sweatt, J.D.9
Zoghbi, H.Y.10
-
54
-
-
0034737299
-
Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
-
Yamamoto A., Lucas J.J., Hen R. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell. 101:2000;57-66.
-
(2000)
Cell
, vol.101
, pp. 57-66
-
-
Yamamoto, A.1
Lucas, J.J.2
Hen, R.3
-
55
-
-
0032499264
-
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
-
Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., Yokochi M., Mizuno Y., Shimizu N. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature. 392:1998;605-608.
-
(1998)
Nature
, vol.392
, pp. 605-608
-
-
Kitada, T.1
Asakawa, S.2
Hattori, N.3
Matsumine, H.4
Yamamura, Y.5
Minoshima, S.6
Yokochi, M.7
Mizuno, Y.8
Shimizu, N.9
-
56
-
-
0347298778
-
Spongiform degeneration in mahoganoid mutant mice
-
This paper describes prion-like spongiform neurodegeneration in mahoganoid mutant mice. Mahoganoid encodes an E3 ubiquitin ligase that interacts with the E2 UBC5, which is active during misfolded protein-induced stress response. This suggests that mahoganoid plays a vital role in the metabolism of misfolded protein
-
He L., Lu X.Y., Jolly A.F., Eldridge A.G., Watson S.J., Jackson P.K., Barsh G.S., Gunn T.M. Spongiform degeneration in mahoganoid mutant mice. Science. 299:2003;710-712 This paper describes prion-like spongiform neurodegeneration in mahoganoid mutant mice. Mahoganoid encodes an E3 ubiquitin ligase that interacts with the E2 UBC5, which is active during misfolded protein-induced stress response. This suggests that mahoganoid plays a vital role in the metabolism of misfolded protein.
-
(2003)
Science
, vol.299
, pp. 710-712
-
-
He, L.1
Lu, X.Y.2
Jolly, A.F.3
Eldridge, A.G.4
Watson, S.J.5
Jackson, P.K.6
Barsh, G.S.7
Gunn, T.M.8
-
57
-
-
6844258835
-
Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
-
van Leeuwen F.W., de Kleijn D.P., van den Hurk H.H., Neubauer A., Sonnemans M.A., Sluijs J.A., Koycu S., Ramdjielal R.D., Salehi A., Martens G.J.et al. Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science. 279:1998;242-247.
-
(1998)
Science
, vol.279
, pp. 242-247
-
-
Van Leeuwen, F.W.1
De Kleijn, D.P.2
Van den Hurk, H.H.3
Neubauer, A.4
Sonnemans, M.A.5
Sluijs, J.A.6
Koycu, S.7
Ramdjielal, R.D.8
Salehi, A.9
Martens, G.J.10
-
58
-
-
0037193469
-
Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
-
Lindsten K., de Vrij F.M., Verhoef L.G., Fischer D.F., van Leeuwen F.W., Hol E.M., Masucci M.G., Dantuma N.P. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell. Biol. 157:2002;417-427.
-
(2002)
J. Cell. Biol.
, vol.157
, pp. 417-427
-
-
Lindsten, K.1
De Vrij, F.M.2
Verhoef, L.G.3
Fischer, D.F.4
Van Leeuwen, F.W.5
Hol, E.M.6
Masucci, M.G.7
Dantuma, N.P.8
-
59
-
-
0034131044
-
Impaired proteasome function in Alzheimer's disease
-
Keller J.N., Hanni K.B., Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J. Neurochem. 75:2000;436-439.
-
(2000)
J. Neurochem.
, vol.75
, pp. 436-439
-
-
Keller, J.N.1
Hanni, K.B.2
Markesbery, W.R.3
-
60
-
-
0035910634
-
Proteasomal function is impaired in substantia nigra in Parkinson's disease
-
McNaught K.S., Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297:2001;191-194.
-
(2001)
Neurosci. Lett.
, vol.297
, pp. 191-194
-
-
McNaught, K.S.1
Jenner, P.2
-
61
-
-
0035476688
-
Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
-
Yedidia Y., Horonchik L., Tzaban S., Yanai A., Taraboulos A. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20:2001;5383-5391.
-
(2001)
EMBO J.
, vol.20
, pp. 5383-5391
-
-
Yedidia, Y.1
Horonchik, L.2
Tzaban, S.3
Yanai, A.4
Taraboulos, A.5
-
62
-
-
0037195647
-
Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
-
This paper and [36,63] show that the prion protein is retrogradely transported out of the endoplasmic reticulum for proteasome degradation. Proteasome inhibition led to an increase in the cytosolic concentration of prion protein (PrP) and induced PrP aggregation. The accumulation of even small amounts of PrP in the cytosol was neurotoxic in cells and transgenic mice
-
Ma J., Wollmann R., Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science. 298:2002;1781-1785 This paper and [36,63] show that the prion protein is retrogradely transported out of the endoplasmic reticulum for proteasome degradation. Proteasome inhibition led to an increase in the cytosolic concentration of prion protein (PrP) and induced PrP aggregation. The accumulation of even small amounts of PrP in the cytosol was neurotoxic in cells and transgenic mice.
-
(2002)
Science
, vol.298
, pp. 1781-1785
-
-
Ma, J.1
Wollmann, R.2
Lindquist, S.3
-
63
-
-
0037195617
-
Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
-
Ma J., Lindquist S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science. 298:2002;1785-1788.
-
(2002)
Science
, vol.298
, pp. 1785-1788
-
-
Ma, J.1
Lindquist, S.2
-
66
-
-
0036678146
-
The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
-
Morley J.F., Brignull H.R., Weyers J.J., Morimoto R.I. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 99:2002;10417-10422.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 10417-10422
-
-
Morley, J.F.1
Brignull, H.R.2
Weyers, J.J.3
Morimoto, R.I.4
-
67
-
-
0032475931
-
Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
-
Saudou F., Finkbeiner S., Devys D., Greenberg M.E. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell. 95:1998;55-66.
-
(1998)
Cell
, vol.95
, pp. 55-66
-
-
Saudou, F.1
Finkbeiner, S.2
Devys, D.3
Greenberg, M.E.4
-
68
-
-
0037134460
-
Polyglutamine expansion, protein aggregation, proteasome activity, and neural survival
-
Ding Q., Lewis J.J., Strum K.M., Dimayuga E., Bruce-Keller A.J., Dunn J.C., Keller J.N. Polyglutamine expansion, protein aggregation, proteasome activity, and neural survival. J. Biol. Chem. 277:2002;13935-13942.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 13935-13942
-
-
Ding, Q.1
Lewis, J.J.2
Strum, K.M.3
Dimayuga, E.4
Bruce-Keller, A.J.5
Dunn, J.C.6
Keller, J.N.7
-
69
-
-
0037101837
-
Polyglutamine and transcription: Gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects
-
Luthi-Carter R., Strand A.D., Hanson S.A., Kooperberg C., Schilling G., La Spada A.R., Merry D.E., Young A.B., Ross C.A., Borchelt D.R.et al. Polyglutamine and transcription: gene expression changes shared by DRPLA and Huntington's disease mouse models reveal context-independent effects. Hum. Mol. Genet. 11:2002;1927-1937.
-
(2002)
Hum. Mol. Genet.
, vol.11
, pp. 1927-1937
-
-
Luthi-Carter, R.1
Strand, A.D.2
Hanson, S.A.3
Kooperberg, C.4
Schilling, G.5
La Spada, A.R.6
Merry, D.E.7
Young, A.B.8
Ross, C.A.9
Borchelt, D.R.10
-
70
-
-
12244298155
-
Cell death triggered by polyglutamine-expanded huntingtin in a neuronal cell line is associated with degradation of CREB-binding protein
-
Jiang H., Nucifora F.C. Jr., Ross C.A., DeFranco D.B. Cell death triggered by polyglutamine-expanded huntingtin in a neuronal cell line is associated with degradation of CREB-binding protein. Hum. Mol. Genet. 12:2003;1-12.
-
(2003)
Hum. Mol. Genet.
, vol.12
, pp. 1-12
-
-
Jiang, H.1
Nucifora F.C., Jr.2
Ross, C.A.3
DeFranco, D.B.4
-
71
-
-
0035937523
-
Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity
-
Nucifora F.C. Jr., Sasaki M., Peters M.F., Huang H., Cooper J.K., Yamada M., Takahashi H., Tsuji S., Troncoso J., Dawson V.L.et al. Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science. 291:2001;2423-2428.
-
(2001)
Science
, vol.291
, pp. 2423-2428
-
-
Nucifora F.C., Jr.1
Sasaki, M.2
Peters, M.F.3
Huang, H.4
Cooper, J.K.5
Yamada, M.6
Takahashi, H.7
Tsuji, S.8
Troncoso, J.9
Dawson, V.L.10
-
72
-
-
0034730745
-
Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila
-
Pham A.D., Sauer F. Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila. Science. 289:2000;2357-2360.
-
(2000)
Science
, vol.289
, pp. 2357-2360
-
-
Pham, A.D.1
Sauer, F.2
-
73
-
-
0037150687
-
Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
-
Dunah A.W., Jeong H., Griffin A., Kim Y.M., Standaert D.G., Hersch S.M., Mouradian M.M., Young A.B., Tanese N., Krainc D. Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease. Science. 296:2002;2238-2243.
-
(2002)
Science
, vol.296
, pp. 2238-2243
-
-
Dunah, A.W.1
Jeong, H.2
Griffin, A.3
Kim, Y.M.4
Standaert, D.G.5
Hersch, S.M.6
Mouradian, M.M.7
Young, A.B.8
Tanese, N.9
Krainc, D.10
-
74
-
-
0034705224
-
Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans
-
Satyal S.H., Schmidt E., Kitagawa K., Sondheimer N., Lindquist S., Kramer J.M., Morimoto R.I. Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 97:2000;5750-5755.
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 5750-5755
-
-
Satyal, S.H.1
Schmidt, E.2
Kitagawa, K.3
Sondheimer, N.4
Lindquist, S.5
Kramer, J.M.6
Morimoto, R.I.7
-
75
-
-
0035668573
-
Inhibition of polyglutamine aggregation in R6/2 HD brain slices-complex dose-response profiles
-
Smith D.L., Portier R., Woodman B., Hockly E., Mahal A., Klunk W.E., Li X.J., Wanker E., Murray K.D., Bates G.P. Inhibition of polyglutamine aggregation in R6/2 HD brain slices-complex dose-response profiles. Neurobiol. Dis. 8:2001;1017-1026.
-
(2001)
Neurobiol. Dis.
, vol.8
, pp. 1017-1026
-
-
Smith, D.L.1
Portier, R.2
Woodman, B.3
Hockly, E.4
Mahal, A.5
Klunk, W.E.6
Li, X.J.7
Wanker, E.8
Murray, K.D.9
Bates, G.P.10
-
76
-
-
0037014426
-
Protein misfolding, amyloid formation, and neurodegeneration: A critical role for molecular chaperones?
-
Muchowski P.J. Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones? Neuron. 35:2002;9-12.
-
(2002)
Neuron
, vol.35
, pp. 9-12
-
-
Muchowski, P.J.1
-
77
-
-
0036501074
-
Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
-
Bailey C.K., Andriola I.F., Kampinga H.H., Merry D.E. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum. Mol. Genet. 11:2002;515-523.
-
(2002)
Hum. Mol. Genet.
, vol.11
, pp. 515-523
-
-
Bailey, C.K.1
Andriola, I.F.2
Kampinga, H.H.3
Merry, D.E.4
-
78
-
-
0037184063
-
Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity
-
Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S., Tanaka K., Taniguchi N., Sobue G. Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity. J. Biol. Chem. 277:2002;36793-36798.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 36793-36798
-
-
Niwa, J.1
Ishigaki, S.2
Hishikawa, N.3
Yamamoto, M.4
Doyu, M.5
Murata, S.6
Tanaka, K.7
Taniguchi, N.8
Sobue, G.9
-
79
-
-
0033638333
-
Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins
-
Zhou P., Bogacki R., McReynolds L., Howley P.M. Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins. Mol. Cell. 6:2000;751-756.
-
(2000)
Mol. Cell.
, vol.6
, pp. 751-756
-
-
Zhou, P.1
Bogacki, R.2
McReynolds, L.3
Howley, P.M.4
-
80
-
-
0036788304
-
Gene silencing in mammals by small interfering RNAs
-
McManus M.T., Sharp P.A. Gene silencing in mammals by small interfering RNAs. Nat. Rev. Genet. 3:2002;737-747.
-
(2002)
Nat. Rev. Genet.
, vol.3
, pp. 737-747
-
-
McManus, M.T.1
Sharp, P.A.2
|