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X-ray kinetic studies of microtubule assembly using synchrotron radiation

Eva-Maria Mandelkow
Arnold Harmsen
Joan Bordas
Research16 Oct 1980
Nature

Volume: 287, P: 595-599
Tubulin hoops

EVA-MARIA MANDELKOW
ECKHARD MANDELKOW
CAROLYN COHEN
Research17 Feb 1977
Nature

Volume: 265, P: 655-657
Role of fimbrin and villin in determining the interfilament distances of actin bundles

Paul Matsudaira
Eckhard Mandelkow
Klaus Weber
Research20 Jan 1983
Nature

Volume: 301, P: 209-214
Tau in physiology and pathology

Tau is a microtubule-stabilizing protein that aggregates in several neurodegenerative diseases. In this Review, Wang and Mandelkow describe the structure, expression and post-translational modifications of tau, and the functions of this protein in health and in disease.

Yipeng Wang
Eckhard Mandelkow
Reviews03 Dec 2015
Nature Reviews Neuroscience

Volume: 17, P: 22-35
Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils

Adriana Savastano
Garima Jaipuria
Markus Zweckstetter
ResearchOpen Access03 Dec 2020
Scientific Reports

Volume: 10, P: 1-14
A mechanistic model of tau amyloid aggregation based on direct observation of oligomers

Alzheimer’s disease is characterized by the aggregation of the Abeta peptide and the tau protein. Here the authors track the formation of wild-type or mutant tau oligomers through to large aggregates and gain insights into the molecular basis of how tau mutations cause disease by altering the aggregation pathway.

Sarah L. Shammas
Gonzalo A. Garcia
David Klenerman
ResearchOpen Access30 Apr 2015
Nature Communications

Volume: 6, P: 1-10
Plasma extracellular vesicle tau and TDP-43 as diagnostic biomarkers in FTD and ALS

Plasma extracellular vesicles contain quantifiable amounts of TDP-43 and full-length tau, allowing the accurate assessment of pathology in frontotemporal dementia, frontotemporal dementia spectrum disorders and amyotrophic lateral sclerosis.

Madhurima Chatterjee
Selcuk Özdemir
Anja Schneider
ResearchOpen Access18 Jun 2024
Nature Medicine

Volume: 30, P: 1771-1783
Lysine/RNA-interactions drive and regulate biomolecular condensation

Processing bodies (P-bodies) are non-membrane-bound protein/RNA granules in the cytosol. Here the authors combine bioinformatics, NMR and cell based assays and find that lysine is enriched in the disordered regions of P-body-associated proteins and show that lysine-rich polypeptides form highly dynamic lysine/RNA-coacervates and lysine acetylation reverses liquid-liquid phase separation.

Tina Ukmar-Godec
Saskia Hutten
Markus Zweckstetter
ResearchOpen Access02 Jul 2019
Nature Communications

Volume: 10, P: 1-15
Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

The chaperone Hsp90 plays a key role in maintaining cellular homeostasis. Here the authors provide structural insights into substrate recognition and the pro-folding mechanism of Hsp90/co-chaperone complexes by studying the complex of Hsp90 with its co-chaperone FKBP51 and the substrate Tau bound Hsp90/FKBP51 ternary complex using a NMR based integrative approach.

Javier Oroz
Bliss J. Chang
Markus Zweckstetter
ResearchOpen Access31 Oct 2018
Nature Communications

Volume: 9, P: 1-13
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

The microtubule associated protein Tau also interacts with filamentous actin. Here the authors combine biophysical experiments and NMR studies to characterize the structural changes that occur in Tau upon binding to filamentous actin and show that phosphorylation of serine 262 attenuates actin binding of Tau.

Yunior Cabrales Fontela
Harindranath Kadavath
Markus Zweckstetter
ResearchOpen Access07 Dec 2017
Nature Communications

Volume: 8, P: 1-12
Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Tau forms aggregates in the brains of Alzheimer patients. Here, the authors identify conditions, where the microtubule-binding repeats of Tau undergo a phosphorylation-dependent liquid–liquid phase separation, leading to molecular crowding in the formed Tau liquid droplets and characterize them by NMR and other biophysical methods.

Susmitha Ambadipudi
Jacek Biernat
Markus Zweckstetter
ResearchOpen Access17 Aug 2017
Nature Communications

Volume: 8, P: 1-13
Initiation and modulation of Tau protein phase separation by the drug suramin

Prabhu Rajaiah Prince
Janine Hochmair
Christian Betzel
ResearchOpen Access09 Mar 2023
Scientific Reports

Volume: 13, P: 1-13
Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein

Jaroslaw Majewski
Emmalee M. Jones
Eva Y. Chi
ResearchOpen Access07 Aug 2020
Scientific Reports

Volume: 10, P: 1-13
Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo

Marianna Karina Gorsky
Sylvie Burnouf
Linda Partridge
ResearchOpen Access04 Mar 2016
Scientific Reports

Volume: 6, P: 1-12

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X-ray kinetic studies of microtubule assembly using synchrotron radiation

Tubulin hoops

Role of fimbrin and villin in determining the interfilament distances of actin bundles

Tau in physiology and pathology

Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers

Plasma extracellular vesicle tau and TDP-43 as diagnostic biomarkers in FTD and ALS

Lysine/RNA-interactions drive and regulate biomolecular condensation

Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex

Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau

Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Initiation and modulation of Tau protein phase separation by the drug suramin

Lipid membrane templated misfolding and self-assembly of intrinsically disordered tau protein

Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo

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