A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease

Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble ag...
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Autor*in:	Todd W. Miller [verfasserIn] Chun Zhou [verfasserIn] Silvia Gines [verfasserIn] Marcy E. MacDonald [verfasserIn] Nicholas D. Mazarakis [verfasserIn] Gillian P. Bates [verfasserIn] James S. Huston [verfasserIn] Anne Messer [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2005

Schlagwörter:	Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody

Übergeordnetes Werk:	In: Neurobiology of Disease - Elsevier, 2021, 19(2005), 1, Seite 47-56
Übergeordnetes Werk:	volume:19 ; year:2005 ; number:1 ; pages:47-56

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.nbd.2004.11.003

Katalog-ID:	DOAJ069117225

Internformat


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520			\|a Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders.
650		4	\|a Polyglutamine
650		4	\|a Aggregation
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650		4	\|a Huntingtin
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653		0	\|a Neurosciences. Biological psychiatry. Neuropsychiatry
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700	0		\|a Nicholas D. Mazarakis \|e verfasserin \|4 aut
700	0		\|a Gillian P. Bates \|e verfasserin \|4 aut
700	0		\|a James S. Huston \|e verfasserin \|4 aut
700	0		\|a Anne Messer \|e verfasserin \|4 aut
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allfields	10.1016/j.nbd.2004.11.003 doi (DE-627)DOAJ069117225 (DE-599)DOAJ0e311aa0cb004cb39f70adfd691ae40c DE-627 ger DE-627 rakwb eng RC321-571 Todd W. Miller verfasserin aut A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders. Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody Neurosciences. Biological psychiatry. Neuropsychiatry Chun Zhou verfasserin aut Silvia Gines verfasserin aut Marcy E. MacDonald verfasserin aut Nicholas D. Mazarakis verfasserin aut Gillian P. Bates verfasserin aut James S. Huston verfasserin aut Anne Messer verfasserin aut In Neurobiology of Disease Elsevier, 2021 19(2005), 1, Seite 47-56 (DE-627)268125414 (DE-600)1471408-5 1095953X nnns volume:19 year:2005 number:1 pages:47-56 https://doi.org/10.1016/j.nbd.2004.11.003 kostenfrei https://doaj.org/article/0e311aa0cb004cb39f70adfd691ae40c kostenfrei http://www.sciencedirect.com/science/article/pii/S0969996104002773 kostenfrei https://doaj.org/toc/1095-953X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4700 AR 19 2005 1 47-56
spelling	10.1016/j.nbd.2004.11.003 doi (DE-627)DOAJ069117225 (DE-599)DOAJ0e311aa0cb004cb39f70adfd691ae40c DE-627 ger DE-627 rakwb eng RC321-571 Todd W. Miller verfasserin aut A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders. Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody Neurosciences. Biological psychiatry. Neuropsychiatry Chun Zhou verfasserin aut Silvia Gines verfasserin aut Marcy E. MacDonald verfasserin aut Nicholas D. Mazarakis verfasserin aut Gillian P. Bates verfasserin aut James S. Huston verfasserin aut Anne Messer verfasserin aut In Neurobiology of Disease Elsevier, 2021 19(2005), 1, Seite 47-56 (DE-627)268125414 (DE-600)1471408-5 1095953X nnns volume:19 year:2005 number:1 pages:47-56 https://doi.org/10.1016/j.nbd.2004.11.003 kostenfrei https://doaj.org/article/0e311aa0cb004cb39f70adfd691ae40c kostenfrei http://www.sciencedirect.com/science/article/pii/S0969996104002773 kostenfrei https://doaj.org/toc/1095-953X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4700 AR 19 2005 1 47-56
allfields_unstemmed	10.1016/j.nbd.2004.11.003 doi (DE-627)DOAJ069117225 (DE-599)DOAJ0e311aa0cb004cb39f70adfd691ae40c DE-627 ger DE-627 rakwb eng RC321-571 Todd W. Miller verfasserin aut A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders. Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody Neurosciences. Biological psychiatry. Neuropsychiatry Chun Zhou verfasserin aut Silvia Gines verfasserin aut Marcy E. MacDonald verfasserin aut Nicholas D. Mazarakis verfasserin aut Gillian P. Bates verfasserin aut James S. Huston verfasserin aut Anne Messer verfasserin aut In Neurobiology of Disease Elsevier, 2021 19(2005), 1, Seite 47-56 (DE-627)268125414 (DE-600)1471408-5 1095953X nnns volume:19 year:2005 number:1 pages:47-56 https://doi.org/10.1016/j.nbd.2004.11.003 kostenfrei https://doaj.org/article/0e311aa0cb004cb39f70adfd691ae40c kostenfrei http://www.sciencedirect.com/science/article/pii/S0969996104002773 kostenfrei https://doaj.org/toc/1095-953X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4700 AR 19 2005 1 47-56
allfieldsGer	10.1016/j.nbd.2004.11.003 doi (DE-627)DOAJ069117225 (DE-599)DOAJ0e311aa0cb004cb39f70adfd691ae40c DE-627 ger DE-627 rakwb eng RC321-571 Todd W. Miller verfasserin aut A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders. Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody Neurosciences. Biological psychiatry. Neuropsychiatry Chun Zhou verfasserin aut Silvia Gines verfasserin aut Marcy E. MacDonald verfasserin aut Nicholas D. Mazarakis verfasserin aut Gillian P. Bates verfasserin aut James S. Huston verfasserin aut Anne Messer verfasserin aut In Neurobiology of Disease Elsevier, 2021 19(2005), 1, Seite 47-56 (DE-627)268125414 (DE-600)1471408-5 1095953X nnns volume:19 year:2005 number:1 pages:47-56 https://doi.org/10.1016/j.nbd.2004.11.003 kostenfrei https://doaj.org/article/0e311aa0cb004cb39f70adfd691ae40c kostenfrei http://www.sciencedirect.com/science/article/pii/S0969996104002773 kostenfrei https://doaj.org/toc/1095-953X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4700 AR 19 2005 1 47-56
allfieldsSound	10.1016/j.nbd.2004.11.003 doi (DE-627)DOAJ069117225 (DE-599)DOAJ0e311aa0cb004cb39f70adfd691ae40c DE-627 ger DE-627 rakwb eng RC321-571 Todd W. Miller verfasserin aut A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease 2005 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders. Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody Neurosciences. Biological psychiatry. Neuropsychiatry Chun Zhou verfasserin aut Silvia Gines verfasserin aut Marcy E. MacDonald verfasserin aut Nicholas D. Mazarakis verfasserin aut Gillian P. Bates verfasserin aut James S. Huston verfasserin aut Anne Messer verfasserin aut In Neurobiology of Disease Elsevier, 2021 19(2005), 1, Seite 47-56 (DE-627)268125414 (DE-600)1471408-5 1095953X nnns volume:19 year:2005 number:1 pages:47-56 https://doi.org/10.1016/j.nbd.2004.11.003 kostenfrei https://doaj.org/article/0e311aa0cb004cb39f70adfd691ae40c kostenfrei http://www.sciencedirect.com/science/article/pii/S0969996104002773 kostenfrei https://doaj.org/toc/1095-953X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2010 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4700 AR 19 2005 1 47-56
language	English
source	In Neurobiology of Disease 19(2005), 1, Seite 47-56 volume:19 year:2005 number:1 pages:47-56
sourceStr	In Neurobiology of Disease 19(2005), 1, Seite 47-56 volume:19 year:2005 number:1 pages:47-56
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody Neurosciences. Biological psychiatry. Neuropsychiatry
isfreeaccess_bool	true
container_title	Neurobiology of Disease
authorswithroles_txt_mv	Todd W. Miller @@aut@@ Chun Zhou @@aut@@ Silvia Gines @@aut@@ Marcy E. MacDonald @@aut@@ Nicholas D. Mazarakis @@aut@@ Gillian P. Bates @@aut@@ James S. Huston @@aut@@ Anne Messer @@aut@@
publishDateDaySort_date	2005-01-01T00:00:00Z
hierarchy_top_id	268125414
id	DOAJ069117225
language_de	englisch
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callnumber-first	R - Medicine
author	Todd W. Miller
spellingShingle	Todd W. Miller misc RC321-571 misc Polyglutamine misc Aggregation misc Intrabody misc Huntington's disease misc Huntingtin misc Antibody misc Neurosciences. Biological psychiatry. Neuropsychiatry A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease
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topic_title	RC321-571 A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease Polyglutamine Aggregation Intrabody Huntington's disease Huntingtin Antibody
topic	misc RC321-571 misc Polyglutamine misc Aggregation misc Intrabody misc Huntington's disease misc Huntingtin misc Antibody misc Neurosciences. Biological psychiatry. Neuropsychiatry
topic_unstemmed	misc RC321-571 misc Polyglutamine misc Aggregation misc Intrabody misc Huntington's disease misc Huntingtin misc Antibody misc Neurosciences. Biological psychiatry. Neuropsychiatry
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title	A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease
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title_full	A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease
author_sort	Todd W. Miller
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author_browse	Todd W. Miller Chun Zhou Silvia Gines Marcy E. MacDonald Nicholas D. Mazarakis Gillian P. Bates James S. Huston Anne Messer
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title_sort	human single-chain fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of huntington's disease
callnumber	RC321-571
title_auth	A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease
abstract	Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders.
abstractGer	Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders.
abstract_unstemmed	Amino-terminal fragments of huntingtin (htt) appear to result from proteolytic processing of the full-length protein in Huntington's disease (HD), and fragments containing pathological expansions of polyglutamine elicit toxicity in model systems. Such fragments are sequestered into insoluble aggregates, which may initially serve a cellular protective mechanism, while soluble fragments and/or oligomers may be a more acute toxic species. Agents which enhance mutant htt clearance have shown therapeutic potential in animal models of HD. Here, we present the first evidence of an htt-specific single-chain Fv intrabody (C4) that selectively targets the soluble fraction of amino-terminal htt fragments. Our findings suggest that the C4 intrabody binds weakly, but does not alter the levels of endogenous, full-length htt. C4 appears to decrease the steady-state levels of amino-terminal htt fragments by binding to non-aggregated, but not aggregated, htt species. Intrabodies may be used as potential curative agents, and as drug discovery tools, for HD and other misfolded protein disorders.
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title_short	A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease
url	https://doi.org/10.1016/j.nbd.2004.11.003 https://doaj.org/article/0e311aa0cb004cb39f70adfd691ae40c http://www.sciencedirect.com/science/article/pii/S0969996104002773 https://doaj.org/toc/1095-953X
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A human single-chain Fv intrabody preferentially targets amino-terminal huntingtin fragments in striatal models of Huntington's disease

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