Glimpses of the molecular mechanisms of β2-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape
β2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full-length protein in vitro. Fibrils have been assembled fr...
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| Veröffentlicht in: | FEBS letters 2009-08, Vol.583 (16), p.2623-2629 |
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| container_title | FEBS letters |
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| creator | Platt, Geoffrey W. Radford, Sheena E. |
| description | β2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanisms of fibril formation from a full-length protein in vitro. Fibrils have been assembled from β2m under both low pH conditions, where the precursor is disordered, and at neutral pH where the protein is initially natively folded. Here we discuss the roles of sequence and structure in amyloid formation, the current understanding of the structural mechanisms of the early stages of aggregation of β2m at both low and neutral pH, and the common and distinct features of these assembly pathways. |
| doi_str_mv | 10.1016/j.febslet.2009.05.005 |
| format | Article |
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Here we discuss the roles of sequence and structure in amyloid formation, the current understanding of the structural mechanisms of the early stages of aggregation of β2m at both low and neutral pH, and the common and distinct features of these assembly pathways.</description><subject>Amyloid fibrils</subject><subject>dialysis-related amyloidosis</subject><subject>DRA</subject><subject>Mechanisms</subject><subject>Minireview</subject><subject>NMR</subject><subject>nuclear magnetic resonance</subject><subject>SEC</subject><subject>size exclusion chromatography</subject><subject>Structure</subject><subject>β2-microglobulin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNp9kd-q1DAQh4MonvXoIwh5gdZJ07SNF8rxcP4IB7xQr0OSTrpZ0qYk3dW98aF8EJ_JrnsQvBEGhvkN88HwEfKaQcmANW92pUOTAy5lBSBLECWAeEI2rGt5weume0o2AKwuRCv5BXmR8w7WuWPyOblgsuYcOrkhP-6CH-eMmUZHly3SMQa0-6ATHdFu9eTz-Gf362dVjN6mOIRo9sFP1HmTfKAuplEvPk50zQ5-SfEtvRqGhMM5XUtTG8c54HeKE6bhSIOe-mz1jC_JM6dDxleP_ZJ8vb35cn1fPHy6-3h99VAgF7IrzPqiblF0smJGMNmjZIyb1lZSguW9dA5a3nDWG15XXe-ENa42EmTLBRcNvyTvztx5b0bsLU5L0kHNyY86HVXUXv27mfxWDfGgqpbX0LAVcH8GfPMBj38PGaiTDbVTjzbUyYYCoVYb6vbmQ_X5JOHkACQAb1m3ot6fUbg-fPCYVLYeJ4u9T2gX1Uf_fy7_Db3anQg</recordid><startdate>20090820</startdate><enddate>20090820</enddate><creator>Platt, Geoffrey W.</creator><creator>Radford, Sheena E.</creator><general>Elsevier B.V</general><general>Elsevier Science B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>24P</scope><scope>5PM</scope></search><sort><creationdate>20090820</creationdate><title>Glimpses of the molecular mechanisms of β2-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape</title><author>Platt, Geoffrey W. ; Radford, Sheena E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e3598-b009a7e58921b519de9113b7c2990c3d9ff073631db3428df5cbf4b9097353563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amyloid fibrils</topic><topic>dialysis-related amyloidosis</topic><topic>DRA</topic><topic>Mechanisms</topic><topic>Minireview</topic><topic>NMR</topic><topic>nuclear magnetic resonance</topic><topic>SEC</topic><topic>size exclusion chromatography</topic><topic>Structure</topic><topic>β2-microglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Platt, Geoffrey W.</creatorcontrib><creatorcontrib>Radford, Sheena E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Wiley Online Library Open Access</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Platt, Geoffrey W.</au><au>Radford, Sheena E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glimpses of the molecular mechanisms of β2-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape</atitle><jtitle>FEBS letters</jtitle><date>2009-08-20</date><risdate>2009</risdate><volume>583</volume><issue>16</issue><spage>2623</spage><epage>2629</epage><pages>2623-2629</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>β2-microglobulin (β2m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. 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| ispartof | FEBS letters, 2009-08, Vol.583 (16), p.2623-2629 |
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| language | eng |
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| source | Wiley Free Content; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amyloid fibrils dialysis-related amyloidosis DRA Mechanisms Minireview NMR nuclear magnetic resonance SEC size exclusion chromatography Structure β2-microglobulin |
| title | Glimpses of the molecular mechanisms of β2-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape |
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