Article
A single mutation promotes amyloidogenicity through a highly promiscuous dimer interface.
Structure (London, England : 1993) - 12 May 2010
Peterson Francis C, Baden Elizabeth M, Owen Barbara A L, Volkman Brian F, Ramirez-Alvarado Marina
Abstract excerpt
Light chain amyloidosis is a devastating protein misfolding disease characterized by the accumulation of amyloid fibrils that causes tissue damage and organ failure. These fibrils are composed of monoclonal light chain protein secreted from an abnormal proliferation of bone marrow plasma cells. We previously reported that amyloidogenic light chain protein AL-09 adopts an altered dimer while its germline protein...
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