Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations
α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Kawamata, Hibiki [verfasserIn] McLean, Pamela J. [verfasserIn] Sharma, Nutan [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|
| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 2001 |
|---|
| Schlagwörter: |
|---|
| Umfang: |
Online-Ressource |
|---|
| Reproduktion: |
2001 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 77(2001), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:77 ; year:2001 ; number:3 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.1471-4159.2001.00301.x |
|---|
| Katalog-ID: |
NLEJ243143753 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ243143753 | ||
| 003 | DE-627 | ||
| 005 | 20230506090159.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 120427s2001 xx |||||o 00| ||und c | ||
| 024 | 7 | |a 10.1046/j.1471-4159.2001.00301.x |2 doi | |
| 035 | |a (DE-627)NLEJ243143753 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 100 | 1 | |a Kawamata, Hibiki |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations |
| 264 | 1 | |a Oxford, UK |b Blackwell Science Ltd |c 2001 | |
| 300 | |a Online-Ressource | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. | ||
| 533 | |d 2001 |f Blackwell Publishing Journal Backfiles 1879-2005 |7 |2001|||||||||| | ||
| 650 | 4 | |a FRET | |
| 700 | 1 | |a McLean, Pamela J. |e verfasserin |4 aut | |
| 700 | 1 | |a Sharma, Nutan |e verfasserin |4 aut | |
| 700 | 1 | |a Hyman, Bradley T. |4 oth | |
| 773 | 0 | 8 | |i In |t Journal of neurochemistry |d Oxford : Wiley-Blackwell, 1956 |g 77(2001), 3, Seite 0 |h Online-Ressource |w (DE-627)NLEJ243927584 |w (DE-600)2020528-4 |x 1471-4159 |7 nnns |
| 773 | 1 | 8 | |g volume:77 |g year:2001 |g number:3 |g pages:0 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x |q text/html |x Verlag |z Deutschlandweit zugänglich |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-DJB | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 77 |j 2001 |e 3 |h 0 | ||
| author_variant |
h k hk p j m pj pjm n s ns |
|---|---|
| matchkey_str |
article:14714159:2001----::neatoosncennsnhlnefcoprisnds |
| hierarchy_sort_str |
2001 |
| publishDate |
2001 |
| allfields |
10.1046/j.1471-4159.2001.00301.x doi (DE-627)NLEJ243143753 DE-627 ger DE-627 rakwb Kawamata, Hibiki verfasserin aut Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations Oxford, UK Blackwell Science Ltd 2001 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| FRET McLean, Pamela J. verfasserin aut Sharma, Nutan verfasserin aut Hyman, Bradley T. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 77(2001), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:77 year:2001 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 2001 3 0 |
| spelling |
10.1046/j.1471-4159.2001.00301.x doi (DE-627)NLEJ243143753 DE-627 ger DE-627 rakwb Kawamata, Hibiki verfasserin aut Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations Oxford, UK Blackwell Science Ltd 2001 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| FRET McLean, Pamela J. verfasserin aut Sharma, Nutan verfasserin aut Hyman, Bradley T. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 77(2001), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:77 year:2001 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 2001 3 0 |
| allfields_unstemmed |
10.1046/j.1471-4159.2001.00301.x doi (DE-627)NLEJ243143753 DE-627 ger DE-627 rakwb Kawamata, Hibiki verfasserin aut Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations Oxford, UK Blackwell Science Ltd 2001 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| FRET McLean, Pamela J. verfasserin aut Sharma, Nutan verfasserin aut Hyman, Bradley T. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 77(2001), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:77 year:2001 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 2001 3 0 |
| allfieldsGer |
10.1046/j.1471-4159.2001.00301.x doi (DE-627)NLEJ243143753 DE-627 ger DE-627 rakwb Kawamata, Hibiki verfasserin aut Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations Oxford, UK Blackwell Science Ltd 2001 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| FRET McLean, Pamela J. verfasserin aut Sharma, Nutan verfasserin aut Hyman, Bradley T. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 77(2001), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:77 year:2001 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 2001 3 0 |
| allfieldsSound |
10.1046/j.1471-4159.2001.00301.x doi (DE-627)NLEJ243143753 DE-627 ger DE-627 rakwb Kawamata, Hibiki verfasserin aut Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations Oxford, UK Blackwell Science Ltd 2001 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. 2001 Blackwell Publishing Journal Backfiles 1879-2005 |2001|||||||||| FRET McLean, Pamela J. verfasserin aut Sharma, Nutan verfasserin aut Hyman, Bradley T. oth In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 77(2001), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:77 year:2001 number:3 pages:0 http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 2001 3 0 |
| source |
In Journal of neurochemistry 77(2001), 3, Seite 0 volume:77 year:2001 number:3 pages:0 |
| sourceStr |
In Journal of neurochemistry 77(2001), 3, Seite 0 volume:77 year:2001 number:3 pages:0 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| topic_facet |
FRET |
| isfreeaccess_bool |
false |
| container_title |
Journal of neurochemistry |
| authorswithroles_txt_mv |
Kawamata, Hibiki @@aut@@ McLean, Pamela J. @@aut@@ Sharma, Nutan @@aut@@ Hyman, Bradley T. @@oth@@ |
| publishDateDaySort_date |
2001-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ243927584 |
| id |
NLEJ243143753 |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243143753</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506090159.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2001 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1471-4159.2001.00301.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243143753</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Kawamata, Hibiki</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">2001</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2001</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2001||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">FRET</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">McLean, Pamela J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sharma, Nutan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hyman, Bradley T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">77(2001), 3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:77</subfield><subfield code="g">year:2001</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">77</subfield><subfield code="j">2001</subfield><subfield code="e">3</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| series2 |
Blackwell Publishing Journal Backfiles 1879-2005 |
| author |
Kawamata, Hibiki |
| spellingShingle |
Kawamata, Hibiki misc FRET Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations |
| authorStr |
Kawamata, Hibiki |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ243927584 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| author_role |
aut aut aut |
| collection |
NL |
| publishPlace |
Oxford, UK |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1471-4159 |
| topic_title |
Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations FRET |
| publisher |
Blackwell Science Ltd |
| publisherStr |
Blackwell Science Ltd |
| topic |
misc FRET |
| topic_unstemmed |
misc FRET |
| topic_browse |
misc FRET |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
b t h bt bth |
| hierarchy_parent_title |
Journal of neurochemistry |
| hierarchy_parent_id |
NLEJ243927584 |
| hierarchy_top_title |
Journal of neurochemistry |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ243927584 (DE-600)2020528-4 |
| title |
Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations |
| ctrlnum |
(DE-627)NLEJ243143753 |
| title_full |
Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations |
| author_sort |
Kawamata, Hibiki |
| journal |
Journal of neurochemistry |
| journalStr |
Journal of neurochemistry |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
2001 |
| contenttype_str_mv |
zzz |
| container_start_page |
0 |
| author_browse |
Kawamata, Hibiki McLean, Pamela J. Sharma, Nutan |
| container_volume |
77 |
| physical |
Online-Ressource |
| format_se |
Elektronische Aufsätze |
| author-letter |
Kawamata, Hibiki |
| doi_str_mv |
10.1046/j.1471-4159.2001.00301.x |
| author2-role |
verfasserin |
| title_sort |
interaction of α-synuclein and synphilin-1: effect of parkinson's disease-associated mutations |
| title_auth |
Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations |
| abstract |
α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. |
| abstractGer |
α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. |
| abstract_unstemmed |
α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1. |
| collection_details |
GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE |
| container_issue |
3 |
| title_short |
Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations |
| url |
http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x |
| remote_bool |
true |
| author2 |
McLean, Pamela J. Sharma, Nutan Hyman, Bradley T. |
| author2Str |
McLean, Pamela J. Sharma, Nutan Hyman, Bradley T. |
| ppnlink |
NLEJ243927584 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth |
| doi_str |
10.1046/j.1471-4159.2001.00301.x |
| up_date |
2024-07-06T04:27:08.708Z |
| _version_ |
1803802408343568385 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243143753</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506090159.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2001 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1471-4159.2001.00301.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243143753</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Kawamata, Hibiki</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Interaction of α-synuclein and synphilin-1: effect of Parkinson's disease-associated mutations</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd</subfield><subfield code="c">2001</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">α-Synuclein is a major component of Lewy bodies, a neuropathological feature of Parkinson's disease. Two α-synuclein mutations, Ala53Thr and Ala30Pro, are associated with early onset, familial forms of the disease. Recently, synphilin-1, a protein found to interact with α-synuclein by yeast two hybrid techniques, was detected in Lewy bodies. In this study we report the interaction of α-synuclein and synphilin-1 in human neuroglioma cells using a sensitive fluorescence resonance energy transfer technique. We demonstrate that the C-terminus of α-synuclein is closely associated with the C-terminus of synphilin-1. A weak interaction occurs between the N-terminus of α-synuclein and synphilin-1. The familial Parkinson's disease associated mutations of α-synuclein (Ala53Thr and Ala30Pro) also demonstrate a strong interaction between their C-terminal regions and synphilin-1. However, compared with wild-type α-synuclein, significantly less energy transfer occurs between the C-terminus of Ala53Thr α-synuclein and synphilin-1, suggesting that the Ala53Thr mutation alters the conformation of α-synuclein in relation to synphilin-1.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2001</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2001||||||||||</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">FRET</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">McLean, Pamela J.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Sharma, Nutan</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hyman, Bradley T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Journal of neurochemistry</subfield><subfield code="d">Oxford : Wiley-Blackwell, 1956</subfield><subfield code="g">77(2001), 3, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243927584</subfield><subfield code="w">(DE-600)2020528-4</subfield><subfield code="x">1471-4159</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:77</subfield><subfield code="g">year:2001</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1471-4159.2001.00301.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">77</subfield><subfield code="j">2001</subfield><subfield code="e">3</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| score |
7.401682 |