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Wiseman R. Luke
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http://hub.abes.fr/acs/periodical/achre4/2005/volume_38/issue_12/101021ar020073i/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_47/101021bi051608t/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_22/101021bi027319b/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_25/101021bi050352o/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_15/101021ja042929f/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_50/101021bi0511484/authorship/1
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Kinetic Stabilization of an Oligomeric Protein by a SingleLigand Binding Event
Native State Kinetic Stabilizationas a Strategy To AmeliorateProtein Misfolding Diseases: AFocus on the TransthyretinAmyloidoses
The Pathway by Which the Tetrameric Protein Transthyretin Dissociates
Kinetic Stabilization of an Oligomeric Protein under Physiological ConditionsDemonstrated by a Lack of Subunit Exchange: Implications for TransthyretinAmyloidosis
D18G Transthyretin Is Monomeric, Aggregation Prone, and Not Detectable inPlasma and Cerebrospinal Fluid: A Prescription for Central Nervous SystemAmyloidosis?
Partitioning Conformational Intermediates between Competing Refolding andAggregation Pathways: Insights into Transthyretin Amyloid Disease
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