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Biochemistry|January 28, 1999
Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formationH A Lashuel, Z Lai, J W KellyFEBS Letters|November 18, 2000
Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon associationG Cingolani, H A Lashuel, L Gerace, et al.Protein Science : a Publication of the Protein Society|October 23, 1997
Oligomerization properties of GCN4 leucine zipper e and g position mutantsX Zeng, H Zhu, H A Lashuel, et al.Biochemistry|August 19, 1997
Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriersZ Lai, J McCulloch, H A Lashuel, et al.Genes & Development|December 31, 1998
Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)L Hengst, U Göpfert, H A Lashuel, et al.Biochemistry|October 16, 1999
The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditionsH A Lashuel, C Wurth, L Woo, et al.Protein Expression and Purification|October 6, 1998
Recombinant human retinol-binding protein refolding, native disulfide formation, and characterizationY Xie, H A Lashuel, G J Miroy, et al.Bioorganic & Medicinal Chemistry|April 13, 1999
The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solutionP Chitnumsub, W R Fiori, H A Lashuel, et al.Journal of the American Chemical Society|February 21, 2012
Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials scienceH A Lashuel, S R Labrenz, L Woo, et al.Nature Structural Biology|August 31, 2000
A glimpse of a possible amyloidogenic intermediate of transthyretinK Liu, H S Cho, H A Lashuel, et al.Pageof 2