Identification of syntaxin 1A as a novel binding protein for presenilin-1.
Mutations in the presenilin 1 gene have been shown to result in Alzheimer's disease. Presenilin 1 is a multi-transmembrane protein with a large hydrophilic loop near the C-terminus. This region is required for known functions of presenilin 1. We have constrained this loop within the active site...
| Hlavní autoři: | , , , , , , , , , , , |
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| Médium: | Journal article |
| Jazyk: | English |
| Vydáno: |
2000
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| _version_ | 1826291070881759232 |
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| author | Smith, S Anderson, H Yu, G Robertson, A Allen, S Tyler, S Naylor, R Mason, G Wilcock, G Roche, P Fraser, P Dawbarn, D |
| author_facet | Smith, S Anderson, H Yu, G Robertson, A Allen, S Tyler, S Naylor, R Mason, G Wilcock, G Roche, P Fraser, P Dawbarn, D |
| author_sort | Smith, S |
| collection | OXFORD |
| description | Mutations in the presenilin 1 gene have been shown to result in Alzheimer's disease. Presenilin 1 is a multi-transmembrane protein with a large hydrophilic loop near the C-terminus. This region is required for known functions of presenilin 1. We have constrained this loop within the active site of the bacterial protein, thioredoxin, to mimic its native conformational state. This hybrid protein was used as bait in a yeast two hybrid screen in an attempt to identify presenilin binding proteins. By this method syntaxin 1A, a synaptic plasma membrane protein, was identified as a novel binding protein for presenilin 1. In vitro experiments confirm the two-hybrid results suggesting that PS1 binds syntaxin under physiological conditions. |
| first_indexed | 2024-03-07T02:53:52Z |
| format | Journal article |
| id | oxford-uuid:ae9c84a2-e223-44a4-a5c7-9eb0698dfa2d |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T02:53:52Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:ae9c84a2-e223-44a4-a5c7-9eb0698dfa2d2022-03-27T03:43:45ZIdentification of syntaxin 1A as a novel binding protein for presenilin-1.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:ae9c84a2-e223-44a4-a5c7-9eb0698dfa2dEnglishSymplectic Elements at Oxford2000Smith, SAnderson, HYu, GRobertson, AAllen, STyler, SNaylor, RMason, GWilcock, GRoche, PFraser, PDawbarn, DMutations in the presenilin 1 gene have been shown to result in Alzheimer's disease. Presenilin 1 is a multi-transmembrane protein with a large hydrophilic loop near the C-terminus. This region is required for known functions of presenilin 1. We have constrained this loop within the active site of the bacterial protein, thioredoxin, to mimic its native conformational state. This hybrid protein was used as bait in a yeast two hybrid screen in an attempt to identify presenilin binding proteins. By this method syntaxin 1A, a synaptic plasma membrane protein, was identified as a novel binding protein for presenilin 1. In vitro experiments confirm the two-hybrid results suggesting that PS1 binds syntaxin under physiological conditions. |
| spellingShingle | Smith, S Anderson, H Yu, G Robertson, A Allen, S Tyler, S Naylor, R Mason, G Wilcock, G Roche, P Fraser, P Dawbarn, D Identification of syntaxin 1A as a novel binding protein for presenilin-1. |
| title | Identification of syntaxin 1A as a novel binding protein for presenilin-1. |
| title_full | Identification of syntaxin 1A as a novel binding protein for presenilin-1. |
| title_fullStr | Identification of syntaxin 1A as a novel binding protein for presenilin-1. |
| title_full_unstemmed | Identification of syntaxin 1A as a novel binding protein for presenilin-1. |
| title_short | Identification of syntaxin 1A as a novel binding protein for presenilin-1. |
| title_sort | identification of syntaxin 1a as a novel binding protein for presenilin 1 |
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