Understanding the complex mechanisms of β2-microglobulin amyloid assembly

The effects of an ideal β-turn on β-2 microglobulin fold stability

(2011) Matteo Colombo et al.   JOURNAL OF BIOCHEMISTRY

A Diversity of Assembly Mechanisms of a Generic Amyloid Fold

(2011) Timo Eichner et al.   MOLECULAR CELL

Conformational Conversion during Amyloid Formation at Atomic Resolution

(2011) Timo Eichner et al.   MOLECULAR CELL

Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic  2-microglobulin variant

(2011) K. Domanska et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structure of the Preamyloid Dimer of β-2-Microglobulin from Covalent Labeling and Mass Spectrometry

(2010) Vanessa Leah Mendoza et al.   BIOCHEMISTRY

Stacked Sets of Parallel, In-register β-Strands of β2-Microglobulin in Amyloid Fibrils Revealed by Site-directed Spin Labeling and Chemical Labeling

(2010) Carol L. Ladner et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Folding and Fibrillogenesis: Clues from β2-Microglobulin

(2010) Enrico Rennella et al.   JOURNAL OF MOLECULAR BIOLOGY

Intermolecular Alignment in β2-Microglobulin Amyloid Fibrils

(2010) Galia T. Debelouchina et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Magic Angle Spinning NMR Analysis of β2-Microglobulin Amyloid Fibrils in Two Distinct Morphologies

(2010) Galia T. Debelouchina et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structures of native and affinity-enhanced WT1 epitopes bound to HLA-A0201: Implications for WT1-based cancer therapeutics

(2010) Oleg Y. Borbulevych et al.   MOLECULAR IMMUNOLOGY

Prion-like transmission of protein aggregates in neurodegenerative diseases

(2010) Patrik Brundin et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages

(2010) Cong Liu et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Metal binding sheds light on mechanisms of amyloid assembly

(2010) Matthew F. Calabrese et al.   Prion

DE-loop mutations affect β2 microglobulin stability, oligomerization, and the low-pH unfolded form

(2010) Carlo Santambrogio et al.   PROTEIN SCIENCE

Molecular dynamics simulation of β2-microglobulin in denaturing and stabilizing conditions

(2010) Federico Fogolari et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

A β2-microglobulin cleavage variant fibrillates at near-physiological pH

(2009) Dorthe B. Corlin et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation

(2009) Stefano Ricagno et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Delineating the Conformational Elements Responsible for Cu2+-Induced Oligomerization of β-2 Microglobulin

(2009) Dorottya V. Blaho et al.   BIOCHEMISTRY

Copper Binding to β-2-Microglobulin and Its Pre-Amyloid Oligomers

(2009) Rapole Srikanth et al.   BIOCHEMISTRY

Mechanism of Lysophosphatidic Acid-Induced Amyloid Fibril Formation of β2-Microglobulinin Vitrounder Physiological Conditions

(2009) Henriett Pál-Gábor et al.   BIOCHEMISTRY

Prion dynamics and the quest for the genetic determinant in protein-only inheritance

(2009) Suzanne S Sindi et al.   CURRENT OPINION IN MICROBIOLOGY

Native-unlike Long-lived Intermediates along the Folding Pathway of the Amyloidogenic Protein β2-Microglobulin Revealed by Real-time Two-dimensional NMR

(2009) Alessandra Corazza et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Globular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid Fibrils

(2009) Helen E. White et al.   JOURNAL OF MOLECULAR BIOLOGY

A Generic Mechanism of β2-Microglobulin Amyloid Assembly at Neutral pH Involving a Specific Proline Switch

(2009) Timo Eichner et al.   JOURNAL OF MOLECULAR BIOLOGY

An Unfolded CH1 Domain Controls the Assembly and Secretion of IgG Antibodies

(2009) Matthias J. Feige et al.   MOLECULAR CELL

NMR-based characterization of a refolding intermediate of β2-microglobulin labeled using a wheat germ cell-free system

(2009) Atsushi Kameda et al.   PROTEIN SCIENCE

Could They All Be Prion Diseases?

(2009) G. Miller   SCIENCE

DE loop mutations affect β2-microglobulin stability and amyloid aggregation

(2008) Stefano Ricagno et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Growth of β2-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH

(2008) Kazuhiro Hasegawa et al.   BIOCHEMICAL JOURNAL

Amyloid Nucleation Triggered by Agitation of β2-Microglobulin under Acidic and Neutral pH Conditions

(2008) Kenji Sasahara et al.   BIOCHEMISTRY

Equilibrium Unfolding Thermodynamics of β 2 -Microglobulin Analyzed through Native-State H/D Exchange

(2008) Enrico Rennella et al.   BIOPHYSICAL JOURNAL

A Common β-Sheet Architecture Underliesin Vitroandin Vivoβ2-Microglobulin Amyloid Fibrils

(2008) Thomas R. Jahn et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Kinetic Coupling of Folding and Prolyl Isomerization of β2-Microglobulin Studied by Mutational Analysis

(2008) Michiko Sakata et al.   JOURNAL OF MOLECULAR BIOLOGY

The Controlling Roles of Trp60 and Trp95 in β2-Microglobulin Function, Folding and Amyloid Aggregation Properties

(2008) Gennaro Esposito et al.   JOURNAL OF MOLECULAR BIOLOGY

HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein β 2-microglobulin upon release from the MHC-1

(2008) John P. Hodkinson et al.   JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY

Amyloid formation by globular proteins under native conditions

(2008) Fabrizio Chiti et al.   Nature Chemical Biology

A regulatable switch mediates self-association in an immunoglobulin fold

(2008) Matthew F Calabrese et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Lysophospholipids induce the nucleation and extension of  2-microglobulin-related amyloid fibrils at a neutral pH

(2008) T. Ookoshi et al.   NEPHROLOGY DIALYSIS TRANSPLANTATION

Characteristics of dialysis-related amyloidosis in patients on haemodialysis therapy for more than 30 years

(2008) S. Otsubo et al.   NEPHROLOGY DIALYSIS TRANSPLANTATION

The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity

(2008) M. J. Feige et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Cu(II) organizes β-2-microglobulin oligomers but is released upon amyloid formation

(2008) Kwasi Antwi et al.   PROTEIN SCIENCE

Dialysis-Related Amyloidosis: Pathogenesis Focusing on AGE Modification

(2003) Toshimitsu Niwa   SEMINARS IN DIALYSIS

Dynamic of β2-Microglobulin Fibril Formation and Reabsorption: The Role of Proteolysis

(2003) Vittorio Bellotti et al.   SEMINARS IN DIALYSIS

The role of disulfide bond in the amyloidogenic state of β2-microglobulin studied by heteronuclear NMR

(2002) Hidenori Katou et al.   PROTEIN SCIENCE

The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition

(2002) Giuliana Verdone et al.   PROTEIN SCIENCE