Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors

TTR and TTR bind by x‐ray crystallography (View interaction)

[1]  G. Murshudov,et al.  Refinement of macromolecular structures by the maximum-likelihood method. , 1997, Acta crystallographica. Section D, Biological crystallography.

[2]  James C Sacchettini,et al.  Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis. , 2004, Journal of medicinal chemistry.

[3]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[4]  Jay Painter,et al.  Electronic Reprint Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Motion Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Motion , 2005 .

[5]  Kevin Cowtan,et al.  research papers Acta Crystallographica Section D Biological , 2005 .

[6]  A. Olofsson,et al.  A comparative analysis of 23 structures of the amyloidogenic protein transthyretin. , 2000, Journal of molecular biology.

[7]  James C. Sacchettini,et al.  Rational design of potent human transthyretin amyloid disease inhibitors , 2000, Nature Structural Biology.

[8]  M. Skinner,et al.  The Diflunisal Trial: Study accrual and drug tolerance , 2012, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

[9]  James C Sacchettini,et al.  Structural insight into pH-induced conformational changes within the native human transthyretin tetramer. , 2008, Journal of molecular biology.

[10]  P. Evans,et al.  Scaling and assessment of data quality. , 2006, Acta crystallographica. Section D, Biological crystallography.

[11]  Steven M. Johnson,et al.  The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug. , 2012, Journal of molecular biology.

[12]  Randy J. Read,et al.  Acta Crystallographica Section D Biological , 2003 .

[13]  Steven M. Johnson,et al.  Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses. , 2010, Current opinion in structural biology.

[14]  Randy J. Read,et al.  Phenix - a comprehensive python-based system for macromolecular structure solution , 2012 .

[15]  Steven M. Johnson,et al.  Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. , 2005, Accounts of chemical research.

[16]  A. Leslie,et al.  The integration of macromolecular diffraction data. , 2006, Acta crystallographica. Section D, Biological crystallography.

[17]  Andrea Rizzi,et al.  Synthesis and biological activity of flurbiprofen analogues as selective inhibitors of beta-amyloid(1)(-)(42) secretion. , 2005, Journal of medicinal chemistry.

[18]  L. Cendron,et al.  Acidic pH-induced conformational changes in amyloidogenic mutant transthyretin. , 2007, Journal of molecular biology.

[19]  J. Kelly,et al.  Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants , 2004, Laboratory Investigation.

[20]  I. Polikarpov,et al.  Novel Zn2+-binding Sites in Human Transthyretin , 2010, The Journal of Biological Chemistry.

[21]  Igor Polikarpov,et al.  Identification of a novel ligand binding motif in the transthyretin channel. , 2010, Bioorganic & medicinal chemistry.

[22]  S. Catinella,et al.  Synthesis and biological activity of flurbiprofen analogues as selective inhibitors of beta-amyloid(1)(-)(42) secretion. , 2005, Journal of medicinal chemistry.

[23]  J. Kelly,et al.  Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. , 1992, Biochemistry.

[24]  Fabrizio Chiti,et al.  Amyloid formation by globular proteins under native conditions. , 2009, Nature chemical biology.

[25]  A G Leslie,et al.  Biological Crystallography Integration of Macromolecular Diffraction Data , 2022 .

[26]  A. Wojtczak,et al.  Structures of human transthyretin complexed with thyroxine at 2.0 A resolution and 3',5'-dinitro-N-acetyl-L-thyronine at 2.2 A resolution. , 1996, Acta crystallographica. Section D, Biological crystallography.