Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions

(2017) Miguel Mompeán et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Cryo-EM structures of tau filaments from Alzheimer’s disease

(2017) Anthony W. P. Fitzpatrick et al.   NATURE

Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED

(2017) M Jason de la Cruz et al.   NATURE METHODS

Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation

(2017) Tariq Afroz et al.   Nature Communications

Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity

(2017) Pascal Krotee et al.   eLife

The N-terminal dimerization is required for TDP-43 splicing activity

(2017) Lei-Lei Jiang et al.   Scientific Reports

A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas

(2016) Alice Soragni et al.   CANCER CELL

Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets

(2016) Angela B. Soriaga et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

(2016) Michael T. Colvin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The activities of amyloids from a structural perspective

(2016) Roland Riek et al.   NATURE

The collection of MicroED data for macromolecular crystallography

(2016) Dan Shi et al.   Nature Protocols

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo

(2016) Sarah K. Kaufman et al.   NEURON

Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril

(2016) Andreas Schmidt et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

(2016) Marielle Aulikki Wälti et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Atomic resolution structure determination by the cryo-EM method MicroED

(2016) Shian Liu et al.   PROTEIN SCIENCE

2.3 A resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition

(2016) S. Banerjee et al.   SCIENCE

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation

(2016) Lei-Lei Jiang et al.   Scientific Reports

Atomic Structure of T6SS Reveals Interlaced Array Essential to Function

(2015) Daniel L. Clemens et al.   CELL

Uncovering the Mechanism of Aggregation of Human Transthyretin

(2015) Lorena Saelices et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

(2015) Alexis Rohou et al.   JOURNAL OF STRUCTURAL BIOLOGY

Structure of the toxic core of α-synuclein from invisible crystals

(2015) Jose A. Rodriguez et al.   NATURE

An atomic structure of human γ-secretase

(2015) Xiao-chen Bai et al.   NATURE

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM

(2015) Matthias Schmidt et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity

(2015) Quan Li et al.   Nature Communications

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

MicroED data collection and processing

(2015) Johan Hattne et al.   Acta Crystallographica A-Foundation and Advances

“Structural characterization of the minimal segment of TDP-43 competent for aggregation”

(2014) Miguel Mompeán et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution

(2014) Li Zhu et al.   HUMAN MOLECULAR GENETICS

Self-Assembling Properties of Peptides Derived from TDP-43 C-Terminal Fragment

(2014) Akash Saini et al.   LANGMUIR

High-resolution structure determination by continuous-rotation data collection in MicroED

(2014) Brent L Nannenga et al.   NATURE METHODS

The amyloid state and its association with protein misfolding diseases

(2014) Tuomas P. J. Knowles et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

The zipper groups of the amyloid state of proteins

(2013) James C. Stroud   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion

(2013) Lei-Lei Jiang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

TDP-43 Regulates the Microprocessor Complex Activity During In Vitro Neuronal Differentiation

(2013) Valerio Di Carlo et al.   MOLECULAR NEUROBIOLOGY

Quantifying the local resolution of cryo-EM density maps

(2013) Alp Kucukelbir et al.   NATURE METHODS

Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM

(2013) Xueming Li et al.   NATURE METHODS

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

(2012) Masato Kato et al.   CELL

The Amyloid State of Proteins in Human Diseases

(2012) David Eisenberg et al.   CELL

Cellular Model of TAR DNA-binding Protein 43 (TDP-43) Aggregation Based on Its C-terminal Gln/Asn-rich Region

(2012) Mauricio Budini et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

(2012) Sjors H.W. Scheres   JOURNAL OF STRUCTURAL BIOLOGY

T-REX: a web server for inferring, validating and visualizing phylogenetic trees and networks

(2012) A. Boc et al.   NUCLEIC ACIDS RESEARCH

Overview of theCCP4 suite and current developments

(2011) Martyn D. Winn et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Delineation of the Core Aggregation Sequences of TDP-43 C-Terminal Fragment

(2011) Akash Saini et al.   CHEMBIOCHEM

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

(2011) Stuart A. Sievers et al.   NATURE

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity

(2011) Weirui Guo et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Molecular basis for amyloid-  polymorphism

(2011) J.-P. Colletier et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hydrogen-bonding networks and RNA bases revealed by cryo electron microscopy suggest a triggering mechanism for calcium switches

(2011) P. Ge et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis

(2010) Brian C. Kraemer et al.   ACTA NEUROPATHOLOGICA

Deletion of TDP-43 down-regulates Tbc1d1, a gene linked to obesity, and alters body fat metabolism

(2010) P.-M. Chiang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Identifying the amylome, proteins capable of forming amyloid-like fibrils

(2010) Lukasz Goldschmidt et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Biology of Amyloid: Structure, Function, and Regulation

(2010) Jason Greenwald et al.   STRUCTURE

Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43

(2009) Takashi Nonaka et al.   HUMAN MOLECULAR GENETICS

Expression of TDP-43 C-terminal Fragmentsin VitroRecapitulates Pathological Features of TDP-43 Proteinopathies

(2009) Lionel M. Igaz et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

TDP-43 Depletion Induces Neuronal Cell Damage through Dysregulation of Rho Family GTPases

(2009) Yohei Iguchi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

TDP-43 Is a Developmentally Regulated Protein Essential for Early Embryonic Development

(2009) Chantelle F. Sephton et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular mechanisms for protein-encoded inheritance

(2009) Jed J W Wiltzius et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Structural insights into TDP-43 in nucleic-acid binding and domain interactions

(2009) P.-H. Kuo et al.   NUCLEIC ACIDS RESEARCH

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

(2009) Y.-J. Zhang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

(2008) Masato Hasegawa et al.   ANNALS OF NEUROLOGY

Colocalization of Transactivation-Responsive DNA-Binding Protein 43 and Huntingtin in Inclusions of Huntington Disease

(2008) Claudia Schwab et al.   JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY

Molecular structural basis for polymorphism in Alzheimer's  -amyloid fibrils

(2008) A. K. Paravastu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The physical basis of microtubule structure and stability

(2003) David Sept et al.   PROTEIN SCIENCE