Molecular Bases of Proteinopathies 

2020-2022 virtual meeting of talks and discussion on "protein multimerization: the good, bad, and exciting aspects"

The goal of this event is to bring scientific leaders working in the field of 'Amyloid Research' together from across the globe

The ZOOMinar series on “Molecular Basis of Proteinopathies” will cover recent breakthroughs in this exciting multidisciplinary area of research from experts in the field. When conferences have been canceled around the world, these virtual presentations and discussions will provide unique opportunities for everyone to learn about recent findings, new topics, and cutting-edge techniques. The live presentations are on Tuesdays (August 2020) and Saturdays (from September 2020 to August 2021) from 10:00 AM to ~11:00 AM (EDT); and Mondays (from October 2021 onwards) from 12:00 noon EST/EDT. This virtual seminar includes a ~35 minutes presentation and ~15 minutes for questions and answers. This series has >1000 registered participants from all over the world. The virtual presentations will be recorded and made available on a YouTube channel (search for the "amyloid symposium").


Ayyalusamy (Rams) RamamoorthyBiophysics and Chemistry, University of Michigan


Joan Shea, Chemistry and Biochemistry & Physics, University of California Santa Barbara


Magda Ivanova, Department of Neurology, University of Michigan


Samuel McCalpin,  Chemistry, University of Michigan


Current schedule: Mondays @12:00 noon ESTThe invited lectures on Proteinopathies will take place via Zoom. After a brief introduction of the speaker by a moderator  (<2 minutes), the invited speaker will present the lecture for 25-30 minutes followed by a question-and-answer session led by the moderator (for ~15 minutes). Lectures will be recorded to allow offline viewing, but the recording will be turned off at the speaker's preference. To facilitate the question-and-answer session, the audience will be invited to submit questions during the lecture using the Q&A folder in Zoom. After the lecture, the moderator will read the questions to the speaker (or a subset of related questions) and if needed unmute a participant for follow-up discussion. Depending on the availability of the speaker, the informal discussion may continue for ~20 minutes after the formal session.  

If you are an expert in the following area(s) and wish to give a talk, please contact us. 

Invited Speakers

April 24, 2023

Dr. Kanchan Garai

Tata Institute of Fundamental Research, Hyderabad, India

"Investigation of amyloid aggregation using single molecule fluorescence techniques"

April 24, 2023

Dr. Sason Shaik

The Hebrew University, Israel

"Assessing the Potentials of Static vs. Oscillating Electric Fields to Decompose Senile Plaques"

April 17, 2023

Dr. Burkhard Bechinger

University of Strasbourg, France

"Lipid-driven assembly of polypeptide complexes"

April 17, 2023

Dr. Santosh Kumar Jha

CSIR-National Chemical Laboratory, Pune, India

"Mechanistic insights into the stress-induced aggregation of 

TDP-43 in ALS"

April 17, 2023

Dr. Rizwan Khan

Aligarh Muslim University, India

"Amyloid Induction and Inhibition"

April 17, 2023

Dr. Burkhard Bechinger

University of Strasbourg, France


April 10, 2023

Dr. Sapun Parekh

University of Texas, Austin

"Heterogeneous structures (and order) of disordered FUS condensation"

April 10, 2023

Dr. Nikolay Dokholyan

Penn State University College of Medicine

"Molecular Etiologies of Neurodegeneration"

April 03, 2023

Dr. Tang Ben Zhong

The Hong Kong University of Science & Technology (HKUST), 

Hong Kong, China


April 03, 2023

Dr. Wei Qiang

Binghamton University

"Cross-Seeding Between Beta-Amyloid Variants In-Vitro and In Cells"

March 27, 2023

Dr. Yoh Matsuki

Osaka University, Japan

March 27, 2023

Dr. Jing Xu

University of California Merced

"How do molecular motors overcome tau inhibition to maintain cargo transport?"

March 20, 2023 CANCELLED

Dr. Ellen Nollen

European Research Institute for the Biology of Ageing, 

University of Groningen, Netherlands


March 20, 2023 CANCELLED

Dr. Samuel Grant

National High Magnetic Field Lab, Florida State University, & FAMU


March 13, 2023 (*8:00 AM, New York time)

Dr. Kenji Sugase

Kyoto University

"Multiple-State Monitoring of SOD1 Amyloid Formation at Single-Residue Resolution by Rheo-NMR Spectroscopy"

March 13, 2023 (*8:00 AM, New York time)

Dr. Heather Wilkins

University of Kansas

"Amyloid Precursor Protein and Mitochondria"

March 06, 2023 (*8:00 AM, New York time)

Dr. Ashutosh Tiwari

Michigan Technological University, Houghton

"Protein Aggregates and Cellular Toxicity: 

What is the Connection?"

March 06, 2023 (*8:00 AM, New York time)

Dr. Xin Zhang

Westlake University, China

"New Methods to Visualize Protein Aggregation in Live Cells"

February 27, 2023 (*8:00 AM, New York time)

Dr. Kazhuhiro Irie

Graduate School of Agriculture, Kyoto University, Japan

"Synthesis and Characterization of Dimer and Trimer Models of Amyloid β40 Tethered at the C-Terminal Region"

February 27, 2023 (*8:00 AM, New York time)

Dr. Erwan Bezard

CNRS, France

"Towards modeling of proteinopathies in non-human primates"

February 20, 2023 (*8:00 AM, New York time)

Dr. Katsumi Matsuzaki

Kyoto University, Japan

"How do membranes initiate Alzheimer's Disease?"

February 20, 2023 (*8:00 AM, New York time)

Dr. Yoshitaka Ishii

Tokyo Institute of Technology, Japan

"Structures and Misfolding Kinetics of Amyloid-beta Fibrils Studied by Solid-state NMR and CryoEM"

February 13, 2023 (*8:00 AM, New York time)

Dr. Tomohide Saio

Tokushima University, Japan

"NMR investigation of the regulators in protein folding and assembly"

February 13, 2023 

(*8:00 AM, New York time)

Dr. Takaomi Saido

RIKEN Center for Brain Science, Japan

"GPCR-based treatment of preclinical Alzheimer’s disease"

February 06, 2023 (*8:00 AM, New York time)

Dr. Masaki Okumura

Tohoku University, Japan

"Understanding the mechanism by which Protein Disulfide Isomerase (PDI) family guide proper oxidative folding"

February 06, 2023 (*8:00 AM, New York time)

Dr. Takahiro Murakoa

Tokyo University of Agriculture and Technology

Kanagawa Institute of Industrial Science and Technology (KISTEC), Japan

"Functional assembly of polypeptides for injured brain regeneration"

January 30, 2023 (*8:00 AM, New York time)

Dr. Human Rezaei

CNRS, France

"Toward a link between the dynamic of prion replication, prion evolution and tissue spreading"

January 30, 2023 (*8:00 AM, New York time)

Dr. Sven Saupe

CNRS, University of Bordeaux, France

"Amyloid signaling motifs in fungal and bacterial regulated cell death pathways"

January 23, 2023 (*8:00 AM, New York time)

Dr. Emma Sparr

Lund University, Sweden

"Decorated vesicles- Interactions between α-synuclein 

and lipid membranes"

January 23, 2023 (*8:00 AM, New York time)

Dr. Loren Andreas

Max Planck Institute, Göttingen, Germany

"Structure of a lipidic alpha-Synuclein aggregation intermediate"

January 16, 2023 (*8:00 AM, New York time)

Dr. Gunnar Schroeder

Forschungszentrum Jülich

"Cryo-EM Studies of Amyloid Fibrils"

January 16, 2023 (*8:00 AM, New York time)

Dr. Ronald Melki

CNRS, France

"Alpha-synuclein fibrillar aggregates polymorphism and distinct synucleinopathies"

January 09, 2023 (*8:00 AM, New York time)

Dr. Per Westermark

Uppsala University, Sweden

"Type A and Type B fibrils in transthyretin (ATTR) amyloidosis"

January 09, 2023 (*8:00 AM, New York time)

Dr. Marie Doumic

Inria, CNRS and Sorbonne Université, France

"Mathematical Modelling for Protein Polymerisation: Results and Open Questions"

December 12, 2022

Dr. Francois-Xavier Theillet

CNRS, France

"Atomic scale analysis of IDPs expressed in live mammalian cells, using in-cell NMR at 310 K"

December 12, 2022

Dr. Tae Hun Kim

University of Toronto (Canada), 

Case Western Reserve University, Cleveland (USA)

"Elucidating protein-protein interactions within phase-separated droplets by NMR"

December 05, 2022

Dr. Liliana Quintanar

Cinvestav (Center for Research and Advanced Studies), 

Mexico City, México

"Metal ions and protein aggregation: From the brain to the human lens"

December 05, 2022

Dr. Christiano L. Dias

New Jersey Institute of Technology

"Lipid Membrane Damage by Amyloid-Like Peptides: Insights from Unbiased All-Atom Simulations "

November 28, 2022

Dr. Pau Bernado

Center for Structure Biology, Montpellier, France

"Structure of Pathogenic Huntingtin Exon-1"

November 28, 2022

Dr. Vijay Rangachari

University of Southern Mississippi

"Alpha-Synuclein induced heterotypic fibril polymorphs of TDP-43"

November 21, 2022

Dr. Axel Abelein

Karolinska Institutet, Sweden

"Molecular mechanisms of metal ion modulation of amyloid-beta aggregation"

November 14, 2022

Dr. Andela Saric

Institute of Science and Technology, Austria

"Physics of amyloid self-replication and inhibition"

November 14, 2022

Dr. Neville Vassallo

University of Malta

"Mitochondrial poration by amyloidogenic peptides"

November 07, 2022

Dr. Frederic Rousseau

Switch Laboratory, 

Katholieke Universiteit Leuven, Belgium

"Heterotypic amyloid interactions modulate amyloid assembly and structure"

November 07, 2022

Dr. Wenwei Zheng

Arizona State University

"Computational methods for interpreting intrinsically disordered protein interactions"

October 31, 2022

Dr. Francesco Simone Ruggeri

Wageningen University 

"Ultrastructural Characterisation of Amyloid Formation One Molecule at a Time"

October 31, 2022

Dr. Ruiqing Ni

University of Zurich, Switzerland

"Non-invasive imaging of amyloid-beta and tau"

October 24, 2022

Dr. Thomas Michaels

Department of Biology, Institute of Biochemistry, 

ETH Zurich, Switzerland

"Control of protein aggregation"

October 24, 2022

Dr. Daniel Raleigh

Stony Brook University, 

"Amylin  (IAPP) Induced b-cell Death: From Molecular Biophysics to Potential Therapeutic Applications"

October 17, 2022

Dr. Sara Linse

Lund University, 


"Secondary nucleation in amyloid formation"

October 17, 2022

Dr. Minkoo Ahn

Institute of Structural and Molecular Biology, 

University College London, UK

"Modulating co-translational protein folding by rational design and ribosome engineering"

October 10, 2022

Dr. Ken Dill

Stony Brook University

"The biophysics of protein aggregation"

October 03, 2022

Dr. Aaron Wilber

Florida State University, 

"A Parietal-Hippocampal Network for Figuring Out Where You Are And What to Do Next is Dysfunctional in AD"

September 26, 2022

Dr. Hilal Lashuel

EPFL, Switzerland

"Revisiting the grammar of Huntingtin aggregation, inclusion formation

and toxicity in Huntington’s disease"

September 26, 2022

Dr. Antoine Loquet

University of Bordeaux

"Amyloids in signalling processes as seen by solid-state NMR"

September 19, 2022

Dr. Marie Skepö

Lund University

"Antimicrobial and Antifungal Saliva Protein Histatin 5 "

September 19, 2022

Dr. Stefan Rüdiger

University of Utrecht

"Chaperoning protein aggregation diseases "

September 12, 2022

Dr. Wei-Feng Xue

University of Kent, 


"The polymorphic landscape of amyloid assembly revealed by AFM and individual particle structural reconstruction"

September 12, 2022

Dr. Per Hammarström

Linköping University

"Amyloid polymorphism in neurodegenerative disease"

July 25, 2022

Dr. Rebecca Berlow

University of North Carolina at Chapel Hill

"Rewriting the Rules of Molecular Competition: Transcriptional Regulation by Intrinsically Disordered Proteins"

July 25, 2022

Dr. Hariom Yadav

University of South Florida

"Role of Microbiome and Its Modulators in Maintaining Our Brain Health"

July 18, 2022

Dr. Marina Ramirez-Alvarado

Mayo Clinic

"When antibodies misbehave, misfold, and kill - the biophysics of aggregation, toxicity, and rescue in vitro and in cell culture"

July 11, 2022

Dr. Ujjayini Ghosh

University of California, San Francisco

"Integrated Cryo-EM and Solid-state NMR Structure of Amyloid-β Fibrils from Alzheimer’s Disease Brain"

July 11, 2022

Dr. Wolfgang Hoyer

Heinrich Heine University Düsseldorf


"Formation and interactions of metastable 

Aβ oligomers"

June 27, 2022

Sara Linse, Steve Bourgault, Sandrine Ongeri, Lucie Khemtemourian, Samuel McCalpin

"Good, Bad, and Ugly Aspects of Thioflavin-T"

June 20, 2022

Dr. Irving Vega

Michigan State University

"Modulators of tau protein dynamics: from toxic to less toxic"

June 20, 2022

Dr. Martina Pannuzzo

Instituto Italiano di Technologia, 


"A combined theoretical and computational approach to disentangle the molecular events at the intersection of amyloid pore and fibrils formation"

June 13, 2022

Dr. Paolo Arosio



"Interplay between condensation and amyloid formation"

June 13, 2022

Dr. Tom Rothstein

Western Michigan University

"My Quarter Century of FameFAIM"

June 06, 2022

Dr. Yoshitaka Ishii

Tokyo Institute of Technology, Japan

"Solid-state NMR studies highlight structural differences and cross-seeding properties of amyloid-beta fibrils"

June 06, 2022

Dr. Pernilla Wittung-Stafshede

Chalmers University of Technology


"Cross-reactivity of Parkinson’s disease protein alpha-synuclein:

Consequences for amyloid formation"

May 30, 2022

Dr. Cláudio Gomes

Faculdade de Ciências da Universidade de Lisboa, Portugal

"Modulators of protein aggregation and toxicity in neurodegenerative diseases"

May 30, 2022

Dr. Dave Klenerman

University of Cambridge, UK

"Charactersing the protein aggregates  formed in humans during the development of neurodegenerative disease"

May 23, 2022

Dr. Guido Pintacuda

Lyon University, France

"Conformational dynamics by NMR in crystals: a tool for detection aggregation propensity of folded and soluble proteins"

May 23, 2022

Dr. Jinghui Luo

Laboratory of Nanoscale Biology, Paul Scherrer Institute, Switzerland

"Transmembrane protein engineering for studying amyloid proteins "

May 16, 2022

Dr. Jun-Xia Lu

ShanghaiTech University, China

"The Amyloid Structures in Cell Necroptosis"

May 16, 2022

Dr. Thimmaiah Govindaraju

Jawaharlal Nehru Centre for Advanced Scientific Research, India

"Alzheimer’s Disease:

Pathophysiology, diagnostic and therapeutic modalities"

May 09, 2022

Dr. Eri Chatani

Kobe University, Japan

"Investigating protein assembly in the nucleation of amyloid fibrils"

May 09, 2022

Dr. James Shorter 

University of Pennsylvania, Philadelphia

"Countering deleterious phase transitions in ALS/FTD"

May 02, 2022

Dr. Michele Vendruscolo

University of Cambridge, UK

"Kinetics-Based Drug Discovery for Neurodegenerative Diseases"

May 02, 2022

Dr. Joel Watts

University of Toronto, Canada

"Strains of Pathological Protein Aggregates in Neurodegenerative Diseases"

April 25, 2022

Dr. Michael Heneka

University of Bonn Medical Center, Germany


Dr. Daniel Raleigh 

Stony Brook University


April 18, 2022

Dr. Avindra Nath


"Aggregates of HIV-Tat protein complexed with amyloid beta peptide accelerate neurodegeneration"

Dr. Gal Bitan 


"Discovery of exophers in mammalian neurons - implications for brain health and disease"

April 11, 2022

Dr. Takahiro Watanabe-Nakayama

Kanazawa University


"Single molecule observation of amyloid aggregation"

Dr. Guido Pintacuda

Lyon University, France

"Conformational dynamics by NMR in crystals: a tool for detection aggregation propensity of folded and soluble proteins"

April 04, 2022

Dr. Dylan Murray

University of California, Davis

"Low complexity protein domain assembly mechanisms"

April 04, 2022

Dr. Henry Paulson

University of Michigan, Ann Arbor


March 28, 2022

Dr. Daniel Huster

Institut für Medizinische Physik und Biophysik, Leipzig,  Germany

"The Structure and Dynamics of Mutated Amyloid β Fibrils"

March 28, 2022

Dr. Olga Gursky

Boston University

"Protein amyloid cofactors: Charged side chain arrays meet their match"

March 21, 2022

Dr. Sandrine Ongeri


Dr. Nicolo Tonali

CNRS, Université Paris Saclay, France

"Folded peptidomimetics based on cross-interactions involved in the prevention of amyloid proteins aggregation"

March 14, 2022

Dr. Robert Tycko


"Structures and Structural Variations in Amyloid Fibrils (Amyloid-beta and Others): Insights from Solid State NMR and Electron Microscopy"

March 14, 2022

Dr. Antoine Loquet

University of Bordeaux

"Amyloids in signalling processes as seen by solid-state NMR"

March 07, 2022

Dr. Nicolas Fawzi

Brown University

"Using NMR spectroscopy to see RNA-binding protein phase separation and aggregation"

March 07, 2022

Dr. James Nowick

University of California, Irvine

"Exploring Amyloid Oligomers with Macrocyclic β-Sheet Peptides"

Presentations from Early Career Researchers - a mini-symposium (March 05, 2022, from 10:00 AM EST)

Organizers of the ZOOMinar series invite early career researchers (students and post-doctoral fellows) to present their research related to "High-resolution (experimentally determined) structures of amyloid proteins". The goal is to provide opportunities for early-career researchers to present their latest research findings, interact with experts with multidisciplinary expertise, and gain critical feedback and collaborations.

To be considered for a short presentation in the ZOOMinar series, you will need to email a title, reference to a published paper, and graphics (or TOC figure) by Dec. 01, 2021. Emails:;

*Additional details about this mini-symposium will be provided later. 

Panel: Samuel McCalpin (Michigan), Anoop Arunagiri (Michigan), Samuel Kotler (NIH)



Feb. 28, 2022

Dr. Kenjiro Ono

Department of Neurology

Kanazawa University, Japan

"HMW Aβ oligomers are important targets for disease modifying approach of Alzheimer's disease"

Feb. 28, 2022

Dr. Justin Legleiter

West Virginia University

"Huntingtin aggregation in the presence of lipid membranes: Implications for Huntington’s disease"

Feb. 21, 2022

Dr. Alexander Kai Büll 

Technical University of Denmark

"Thermodynamics of amyloid fibril formation"

Feb. 21, 2022

Dr. Shai Rahimipour 

Bar-Ilan University, Israel

"Toward Early Diagnosis and Therapy of Alzheimer's Disease"

Feb. 14, 2022

Dr. Claudio Luchinat

CERM, Florence, Italy

"Molecular Aspects of Protein Aggregation"

Feb. 14, 2022

Dr. Raz Jelinek

Ben-Gurion University, Israel

"Natural amyloid fibrils as catalysts of physiological and pathological reactions: a new paradigm in disease?"

Feb. 07, 2022

Dr. Andisheh Abedini

Stonybrook University 

"Cellular mechanisms of IAPP-induced islet β-cell dysfunction in diabetes"

Feb. 07, 2022

Dr. Ralf Langen

University of Southern California

"Conformationally Specific Huntingtin Binders as Potential Biomarkers or Therapeutics"

Jan. 31, 2022

Dr. Ioana Mariuca Ilie 

University of Amsterdam

"Antibody binding modulates the dynamics of the cellular prion protein"

Jan. 31, 2022

Dr. Amedeo Caflisch

University of Zurich

"Kinetic control of fibril formation and design of antiprion compounds"

January 24, 2022

Dr. Fabrizio Chiti

University of Florance, Italy

"Physicochemical basis of the displacement of amyloidogenic proteins and misfolded protein oligomers from biological membranes"

January 24, 2022

Dr. Jin Hyung Lee

Stanford University

"Illuminating neural circuits: from molecules to MRI for precision brain health"

January 17, 2022

Dr. Christopher Martyniuk

University of Florida

"Zebrafish as a model to understand pesticide-induced neurotoxicity:​ Relevance to Parkinson's disease"

Dr. Matthias Buck

Case Western Reserve University

"NMR and Molecular Dynamics Studies on Protein-Protein Interactions: Examples from the Class of Dynamic Protein Complexes"

January 10, 2022

Dr. Rohit Pappu

Washington University, St.Louis

"Linkage of folding and binding on phase separation"

December 13, 2021

Dr. Pu-Chen Ke

Monash University, Australia

"Mitigating amyloidogenesis with nanomaterials"

December 13, 2021

Dr. Jeremy Schmit

Kansas State University, 

"The landscape of amyloid misfolding"

December 06, 2021

Dr. Eitan Lerner

Hebrew University, Israel

"Integrative studies of the structural dynamics of alpha-Synuclein forms"

December 06, 2021

Dr. Gregory Hudalla

University of Florida

"Form and Function of Glycosylated Peptide Nanofibers"

November 29, 2021

Professor Eric Brown

McMaster University, Canada

"Bugs, drugs and cell systems"

November 22, 2021

Dr. Sami Barmada

University of Michigan

"Autophagy and cell type-specific factors regulating autophagy in neurodegenerative disease models"

November 22, 2021

Dr. Céline Galvagnion-Büll

University of Copenhagen 

"Alpha-synuclein – membrane interactions: the influence of lipid composition on the kinetics of protein aggregation"

November 15, 2021

Professor Dr. Marcus Faendrich

Ulm University, Germany

"Cryo-EM structures of ex vivo amyloid fibrils

November 01, 2021

Professor Roland Riek


"Amyloids: from the origin to end of life"

November 01, 2021

Professor Anant Paravastu 

Georgia Institute of Technology

"Structural Studies of Alzheimer’s Amyloid-β Oligomers: why would a β-sheet peptide aggregate be limited in size?"

October 04, 2021 Dr. Dennis J. Selkoe

August 21, 2021

Gary Lorigan

Professor, Miami University, Ohio

Annelise E. Barron

Associate Professor 

Department of Bioengineering

Stanford University

August 4, 2020

A Hypothesis for How Innate Immune Dysregulation May Cause Alzheimer’s Dementia; 

and How We May Be Able to Prevent It

 We are investigating the early-stage etiology of sporadic Alzheimer's Disease (AD), for which 420+ clinical trials by Pharma have failed over the past 15 years to produce an effective drug. What causes the accumulation of Aβ peptide-rich fibrils and plaques in an aging brain? What are Aβ's physiological functions? We focus on Aβ's interactions with the human cathelicidin peptide, LL-37, an antibacterial and antiviral innate immune system effector and modulator that is ubiquitous in tissues and expressed by myriad cell types, yet unique in the human proteome. Recently, evidence has built that chronic  Herpesvirus or P. gingivalis infections of human brain tissue may precipitate many cases of sporadic dementia labeled as Alzheimer’s Disease. We present experimental evidence and discuss our developing hypothesis that the antiviral and antibacterial peptide LL-37, which can be chronically under-expressed in humans based on dietary and lifestyle factors or degraded by P. gingivalis virulence factors, is a natural binding partner of Aβ that inhibits formation of AD fibrils and plaques, such that LL-37 and Aβ have a toxin/antitoxin relationship. We demonstrate binding between LL-37 and Aβ by Transmission Electron Microscopy (TEM), Surface Plasmon Resonance Imaging (SPRi), and circular dichroism (CD) spectroscopy. TEM shows that LL-37 inhibits the fibrillization of Aβ, especially the formation of long, straight fibrils characteristic of AD, while CD spectroscopy reveals that LL-37 binding prevents Aβ from adopting β-type secondary structure. Analytical Ultracentrifugation (AUC) and Small-Angle X-ray Scattering (SAXS) prove that LL-37 and Aβ form a unique, water-soluble, 1:1 complex. In vitro cell culture studies using primary human microglia and neuronal cells indicates that these two peptides neutralize each other’s cytotoxic effects on these cells. Finally, studies in 5XFAD and wildtype transgenic mice, and Drosophila Melanogaster, support these findings. We discuss what all of this means in the context of the prevention and treatment of Alzheimer’s dementia. 

Rakez Kayed 


Department of Neurology, 

University of Texas Medical Branch 


August 11, 2020

“Polymorphism of Protein Aggregates in Alzheimer’s Disease and Related Dementias” 


Andrew P. Lieberman 


Director of Neuropathology

University of Michigan Medical School

August 18, 2020

Polyglutamine-mediated proteotoxicity in SBMA

Amy Gladfelter 


Department of Biology

University of North Carolina

August 25, 2020

“Specific viral RNA drives the SARS CoV-2 nucleocapsid to phase separate " 

A mechanistic understanding of the SARS-CoV-2 viral replication cycle is essential to develop new therapies for the COVID-19 global health crisis. In this study, we show that the SARS-CoV-2 nucleocapsid protein (N-protein) undergoes liquid-liquid phase separation (LLPS) with the viral genome, and propose a model of viral packaging through LLPS. N-protein condenses with specific RNA sequences in the first 1000 nts (5’-End) under physiological conditions and is enhanced at human upper airway temperatures. N-protein condensates exclude non-packaged RNA sequences. We comprehensively map sites bound by N-protein in the 5’-End and find preferences for single-stranded RNA flanked by stable structured elements. Liquid-like N-protein condensates form in mammalian cells in a concentration-dependent manner and can be altered by small molecules. Condensation of N-protein is sequence and structure specific, sensitive to human body temperature, and manipulatable with small molecules thus presenting screenable processes for identifying antiviral compounds effective against SARS-CoV-2.  

Silvia Marchesan  


Chemical & Pharmaceutical Sciences Department, University of Trieste 

September 12, 2020

“Entry to peptide Wonderland through the rabbit-hole”  


Aphrodite Kapurniotu


TUM School of Life Sciences, 

Technical University of Munich (TUM)

September 19, 2020

“IAPP cross interactions: from discovery to exploitation" 


Marc Diamond  


Center for Alzheimer's and Neurodegenerative Diseases,  University of Texas Southwestern Medical Center  

September 26, 2020

New insights into tau prion propagation” 


David Eisenberg 


Department of Chemistry and Biochemistry and Biological Chemistry 

University of California, Los Angeles 

October 3, 2020

Pathogenic vs Reversible Functional Amyloid"

Samrat Mukhopadhyay   


Centre for Protein Science, Design & Engineering,

Indian Institute of Science Education and Research 

October 10, 2020

"The Role of Intrinsic Disorder and Dynamics in Biological Phase Transitions "  


Martin Muschol  

Associate Professor & Graduate Director

Department of Physics

University of South Florida

October 17, 2020

“Distinct species of amyloid oligomers and their biological activities”


Jennifer Lee  

Senior Investigator

Laboratory of Protein Conformation and Dynamics



October 24, 2020

The complex landscape of α-synuclein


Markus Zweckstetter 


German Center for Neurodegenerative Diseases (DZNE)

Max Planck Institute for Biophysical Chemistry

University Medical Centre Göttingen 

October 31, 2020

Molecular underpinnings of the life and death of Tau"


Birgit Strodel 


Research Centre Jülich

Institute for Structural Biochemistry 

November 7, 2020

“Computational studies on the effects of in vivo conditions on amyloid-β aggregation”


Cong Liu 

Principal Investigator

Interdisciplinary Research Center on Biology & Chemistry

Shanghai Institute of Organic Chemistry

Chinese Academy of Sciences 


November 14, 2020

“How chaperones regulate protein phase transition and its role in neurodegenerative disease”  

Songi Han  


Department of Chemistry & Biochemistry 

Department of Chemical Engineering 

University of California Santa Barbara


November 21, 2020

"Tracking the dynamic conformation ensemble of tau along its aggregation pathway" 

Meytal Landau   

Associate Professor 

Department of Biology

Technion - Israel Institute of Technology  


December 5, 2020

"Virulent and Antibacterial Fibrils in Infectious and Aggregation Diseases" 


Christian Griesinger & Leif Antonchmidt  

Professor (Dr. Christian Griesinger)

Researcher (Dr. Leif Antonchmidt)

Dept. of NMR based structural biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany



December 12, 2020

"Interference with protein aggregation at the membrane: structural biology and therapy"

Vladimir Uversky 


College of Medicine Molecular Medicine

University of South Florida 


December 19, 2020

"From polyfunctionality to multipathogenicity with intrinsic disorder"      

Elisar Barbar & Heather Forsythe  

Professor (Dr. Elisar Barbar)

Graduate Student (Heather Forsythe)

Faculty Director of the Oregon State University Biomolecular NMR Facility, and Department Head      

January 09, 2020

"Multivalency and protein disorder in virus protein interactions: Common themes among Rabies virus and SARS-CoV2

Mei Hong     


Department of Chemistry

Massachusetts Institute of Technology  


January 16, 2021

"Molecular structures of glucagon and tau fibrils from NMR

Elizabeth Rhoades      

Associate Professor 

Department of Chemistry

University of Pennsylvania 


January 23, 2021

"Investigating the role of N-terminal acetylation on alpha-synuclein structure and function

Laura P.W. Ranum

Director of Center for NeuroGenetics 

University of Florida


January 30, 2021

"Repeat associated non-AUG (RAN) translation in neurodegenerative disease: molecular insights and therapeutic opportunities

Ehud Gazit 


Tel Aviv University,  

February 06, 2021

"Metabolite Self-Assembly: Extension of the amyloid hypothesis"

Dieter Willbold 


Institute of Complex Systems & Forschungszentrum Juelich GmbH

February 13, 2021

"Aβ oligomer disassembly into monomers is beneficial for cognition and memory in transgenic and non-transgenic Alzheimer animal models"

Stephen Meredith  


University of Chicago

February 20, 2021  

"Heterogeneity of Aβ Aggregates"

Yuji Sugita

Chief Scientist


February 27, 2021

"Replica-exchange simulations on the conformational dynamics of spike protein on the surface of SARS-CoV-2

March 06, 2021

Alemayehu Gorfe

Associate Professor  

University of Texas, Houston  

"The intrinsically disordered membrane anchor of Ras proteins sorts membrane lipids"

March 13, 2021

Samir Maji


Biosciences and Bioengineering, 

IIT,  Bombay 

"p53 amyloid formation associated with cancer

March 20, 2021

John Straub

Professor, Boston University

"The roles of monomer and membrane in Aβ-protein genesis and aggregation"

Communications Biology volume 4, Article number: 120 (2021).

The thermodynamic hypothesis of protein folding, known as the “Anfinsen’s dogma” states that the native structure of a protein represents a free energy minimum determined by the amino acid sequence. However, inconsistent with the Anfinsen’s dogma, globular proteins can misfold to form amyloid fibrils, which are ordered aggregates associated with diseases such as Alzheimer’s and Parkinson’s diseases. Here, we present a general concept for the link between folding and misfolding. We tested the accessibility of the amyloid state for various proteins upon heating and agitation. Many of them showed Anfinsen-like reversible unfolding upon heating, but formed amyloid fibrils upon agitation at high temperatures. We show that folding and amyloid formation are separated by the supersaturation barrier of a protein. Its breakdown is required to shift the protein to the amyloid pathway. Thus, the breakdown of supersaturation links the Anfinsen’s intramolecular folding universe and the intermolecular misfolding universe.

No ZOOMinar 

on March 27th and April 3rd

Enjoy the break!

April 10, 2021

Sudipta Maiti

Tata Institute of Fundamental Research, 

Mumbai 400005, INDIA

Email:, URL:

“Probing toxic protein oligomers: From test tubes to patient-derived neurons”

Understanding how amyloid aggregates actually become toxic is one of the challenges in developing a treatment for diseases such as Alzheimer’s and Parkinson’s. One of the major possibilities is that the small oligomeric aggregates incorporate into the cell membrane and make specific functional structures which ultimately cause toxicity. However, very little is known about the structure of the oligomers, the stoichiometry of the toxic oligomer, its insertion into the membrane, and subsequent cellular interactions. Perhaps the hardest problem is to establish the correlation of all these parameters with the actual disease. Here we address these issues for Amyloid-beta, which is associated with Alzheimer’s disease. Nature has provided some clues for Alzheimer’s in terms of the location of disease-accelerating mutations, correlations with other protein isoforms, and neuron-type specific vulnerabilities. However, they have been hard to interpret.  Using tools such as nanosecond FCS, time resolved FRET, solid state NMR, membrane-mediated SERS, single molecule photobleaching, and Alzheimer’s patient-derived neurons, we are finally making sense of some of these clues.


1)     Dey et al., Chem. Eur. J., (2021),

2)     Dey et al., Physical Chemistry Chemical Physics (2020) 22 (26), 14613

3)     Chandra et al., Chemical Communications (2018) 54 (56), 7750-7753

4)     Bhowmik et al., ACS Nano (2015), 9 (9), 9070-9077

5)     Sarkar et al., Angewandte Chemie (2014) 126 (27), 6948-6948.

April 17, 2021

Sheena Radford   


Structural Molecular Biology, Univ. of Leeds    

"Seeing the molecular details of amyloid formation"

April 17, 2021

Sabine Ulamec

"A short motif in the N-terminal region of alpha-synuclein is critical for aggregation"

April 24, 2021

Omar El-Agnaf 

Executive Director

Qatar Biomedical Research Institute 

Joint Professor 

College of Health and Life Sciences

“Role of α-synuclein phosphorylation at serine 129 in the pathogenesis of synucleinopathies: an active debate"

Parkinson’s disease (PD) and dementia with Lewy bodies (DLB) are human neurodegenerative diseases characterized neuropathologically by the presence of neuronal α-synuclein inclusions, named as Lewy bodies and Lewy neurites. Increasing number of studies highlighted the aberrant accumulation of phosphorylated α-synuclein at the residue Serine129 (pS129) in the brain of PD and DLB patients, suggesting that phosphorylation may play a vital role in the regulation of α-synuclein aggregation and subsequent neuronal degeneration. However, a comprehensive understating of the exact role of α-synuclein phosphorylation at S129 is still lacking. Here, we study the time-point at which pS129 modification occurs in the process of α-synuclein aggregation and its role in initiation, progression and cellular toxicity of the disease. Therefore, with the collaboration of many international teams we have addressed this issue by designing and executing important in vitro, ex vivo, and in vivo experiments using various models, in addition to post-mortem human brain studies. Contrary to the putative view of pS129-α-synuclein being particularly disease-relevant form of α-synuclein, we suggest that pS129 diminished aggregation-propensity, attenuated cytotoxicity, and occurs subsequent to initial α-synuclein aggregation. Our novel findings have important implications for the design of future neuropathological studies and the development of therapeutic approaches targeting of distinct α-synuclein species. 

April 24, 2021

Henrike Heise

Forschungszentrum Juelich GmbH