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Pathogenetic mechanisms of amyloid A amyloidosis

Proceedings of the National Academy of Sciences - PNAS, 2013-10, Vol.110 (40), p.16115-16120

2013

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Trapping of palindromic ligands within native transthyretin prevents amyloid formation

Proceedings of the National Academy of Sciences - PNAS, 2010-11, Vol.107 (47), p.20483-20488

2010

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Antibodies to human serum amyloid P component eliminate visceral amyloid deposits

Nature (London), 2010-11, Vol.468 (7320), p.93-97

2010

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Hereditary Systemic Amyloidosis Due to Asp76Asn Variant β2-Microglobulin

The New England journal of medicine, 2012-06, Vol.366 (24), p.2276-2283

2012

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Isolation and characterization of pharmaceutical grade human pentraxins, serum amyloid P component and C‐reactive protein, for clinical use

Journal of immunological methods, 2012-10, Vol.384 (1-2), p.92-102

2012

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Hereditary systemic amyloidosis due to Asp76Asn variant [beta]2-microglobulin

The New England journal of medicine, 2012-06, Vol.366 (24), p.2276

2012

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Hereditary Systemic Amyloidosis Due to Asp76Asn Variant β 2 -Microglobulin

The New England journal of medicine, 2012-06, Vol.366 (24), p.2276-2283

2012

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Structural and functional characterization of three human immunoglobulin κ light chains with different pathological implications

Biochimica et biophysica acta, 1996-12, Vol.1317 (3), p.161-167

1996

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Review: Immunoglobulin Light Chain Amyloidosis—The Archetype of Structural and Pathogenic Variability

Journal of Structural Biology, 2000-06, Vol.130 (2-3), p.280-289

2000

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Conformational Switching and Fibrillogenesis in the Amyloidogenic Fragment of Apolipoprotein A-I

The Journal of biological chemistry, 2003-01, Vol.278 (4), p.2444-2451

2003

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Structural basis of ligand specificity in the human pentraxins, C-reactive protein and serum amyloid P component

Journal of molecular recognition, 2011-03, Vol.24 (2), p.371-377

2011

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Recombinant amyloidogenic domain of ApoA-I: Analysis of its fibrillogenic potential

Biochemical and biophysical research communications, 2006-12, Vol.351 (1), p.223-228

2006

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Structural and Folding Dynamic Properties of the T70N Variant of Human Lysozyme

The Journal of biological chemistry, 2003-07, Vol.278 (28), p.25910-25918

2003

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The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide

The American journal of pathology, 1999-09, Vol.155 (3), p.695

1999

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Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure

Protein science, 2001-01, Vol.10 (1), p.187-199

2001

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Solution structure of beta(2)-microglobulin and insights into fibrillogenesis

Biochimica et biophysica acta, 2005-11, Vol.1753 (1), p.76

2005

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Capillary electrophoresis investigation of a partially unfolded conformation of beta(2)-microglobulin

Electrophoresis, 2002-03, Vol.23 (6), p.918

2002

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Affinity capillary electrophoresis is a powerful tool to identify transthyretin binding drugs for potential therapeutic use in amyloidosis

Electrophoresis, 2000-09, Vol.21 (15), p.3280-3289

2000

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Evidence That Amyloidogenic Light Chains Undergo Antigen-Driven Selection

Blood, 1998-04, Vol.91 (8), p.2948-2954

1998

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β 2‐microglobulin can be refolded into a native state from ex vivo amyloid fibrils

European journal of biochemistry, 1998-11, Vol.258 (1), p.61-67

1998

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The New Apolipoprotein A-I Variant Leu174 -> Ser Causes Hereditary Cardiac Amyloidosis, and the Amyloid Fibrils Are Constituted by the 93-Residue N-Terminal Polypeptide

The American journal of pathology, 1999-09, Vol.155 (3), p.695-702

1999

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Hepatitis C virus‐associated cryoglobulinaemicglomerulonephritis with delayed appearance ofmonoclonal cryoglobulinaemia

Nephrology, dialysis, transplantation, 2001-02, Vol.16 (2), p.432-434

2001

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Use of Anti‐(β2 Microglobulin) mAb to Study Formation of Amyloid Fibrils

European journal of biochemistry, 1997-10, Vol.249 (1), p.21-26

1997

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Effects of a vitamin E-modified dialyzer (Excebrane) on beta-2-microglobulin structure and removal

Contributions to nephrology, 1999, Vol.127, p.147-155

1999

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Pathogenetic mechanisms of amyloid A amyloidosis

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

Antibodies to human serum amyloid P component eliminate visceral amyloid deposits

Hereditary Systemic Amyloidosis Due to Asp76Asn Variant β2-Microglobulin

Isolation and characterization of pharmaceutical grade human pentraxins, serum amyloid P component and C‐reactive protein, for clinical use

Hereditary systemic amyloidosis due to Asp76Asn variant [beta]2-microglobulin

Hereditary Systemic Amyloidosis Due to Asp76Asn Variant β 2 -Microglobulin

Structural and functional characterization of three human immunoglobulin κ light chains with different pathological implications

Review: Immunoglobulin Light Chain Amyloidosis—The Archetype of Structural and Pathogenic Variability

Conformational Switching and Fibrillogenesis in the Amyloidogenic Fragment of Apolipoprotein A-I

Structural basis of ligand specificity in the human pentraxins, C-reactive protein and serum amyloid P component

Recombinant amyloidogenic domain of ApoA-I: Analysis of its fibrillogenic potential

Structural and Folding Dynamic Properties of the T70N Variant of Human Lysozyme

The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide

Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure

Solution structure of beta(2)-microglobulin and insights into fibrillogenesis

Capillary electrophoresis investigation of a partially unfolded conformation of beta(2)-microglobulin

Affinity capillary electrophoresis is a powerful tool to identify transthyretin binding drugs for potential therapeutic use in amyloidosis

Evidence That Amyloidogenic Light Chains Undergo Antigen-Driven Selection

β 2‐microglobulin can be refolded into a native state from ex vivo amyloid fibrils

The New Apolipoprotein A-I Variant Leu174 -> Ser Causes Hereditary Cardiac Amyloidosis, and the Amyloid Fibrils Are Constituted by the 93-Residue N-Terminal Polypeptide

Hepatitis C virus‐associated cryoglobulinaemicglomerulonephritis with delayed appearance ofmonoclonal cryoglobulinaemia

Use of Anti‐(β2 Microglobulin) mAb to Study Formation of Amyloid Fibrils

Effects of a vitamin E-modified dialyzer (Excebrane) on beta-2-microglobulin structure and removal

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