Glycosylation and prion protein.
Recent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycof...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2002
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| _version_ | 1826297681745543168 |
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| author | Rudd, P Merry, A Wormald, M Dwek, R |
| author_facet | Rudd, P Merry, A Wormald, M Dwek, R |
| author_sort | Rudd, P |
| collection | OXFORD |
| description | Recent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycoforms" as a diagnostics tool has been discussed. The possibility exists that the glycans may play a role in the location of the prion protein on the neuronal cell surface. Alternative topologies and tethering of the prion glycoprotein on the cell membrane affect glycan site occupancy and may play a role in disease pathogenesis. |
| first_indexed | 2024-03-07T04:35:23Z |
| format | Journal article |
| id | oxford-uuid:cfbe0444-ef3b-4a17-b762-8e6ffc4331cc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T04:35:23Z |
| publishDate | 2002 |
| record_format | dspace |
| spelling | oxford-uuid:cfbe0444-ef3b-4a17-b762-8e6ffc4331cc2022-03-27T07:44:50ZGlycosylation and prion protein.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:cfbe0444-ef3b-4a17-b762-8e6ffc4331ccEnglishSymplectic Elements at Oxford2002Rudd, PMerry, AWormald, MDwek, RRecent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycoforms" as a diagnostics tool has been discussed. The possibility exists that the glycans may play a role in the location of the prion protein on the neuronal cell surface. Alternative topologies and tethering of the prion glycoprotein on the cell membrane affect glycan site occupancy and may play a role in disease pathogenesis. |
| spellingShingle | Rudd, P Merry, A Wormald, M Dwek, R Glycosylation and prion protein. |
| title | Glycosylation and prion protein. |
| title_full | Glycosylation and prion protein. |
| title_fullStr | Glycosylation and prion protein. |
| title_full_unstemmed | Glycosylation and prion protein. |
| title_short | Glycosylation and prion protein. |
| title_sort | glycosylation and prion protein |
| work_keys_str_mv | AT ruddp glycosylationandprionprotein AT merrya glycosylationandprionprotein AT wormaldm glycosylationandprionprotein AT dwekr glycosylationandprionprotein |