Determination of the structure and dynamics of the fuzzy coat of an amyloid fibril of IAPP using cryo-electron microscopy

Autor: Z. Faidon Brotzakis, Thomas Löhr, Steven Truong, Samuel E. Hoff, Massimiliano Bonomi, Michele Vendruscolo

In recent years, major advances in cryo-electron microscopy (cryo-EM) have enabled the routine determination of complex biomolecular structures at atomic resolution. An open challenge for this approach, however, concerns large systems that exhibit co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0351634e64f93aec5281c7cd2a1353a5
https://hal.science/hal-03834207/file/2022.05.29.493873v1.full.pdf

Conformational Entropy as a Potential Liability of Computationally Designed Antibodies

Autor: Michele Vendruscolo, Pietro Sormanni, Thomas Löhr

Publikováno v: Biomolecules; Volume 12; Issue 5; Pages: 718

In silico antibody discovery is emerging as a viable alternative to traditional in vivo and in vitro approaches. Many challenges, however, remain open to enabling the properties of designed antibodies to match those produced by the immune system. A m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66437ec6813a51e5cf6210c9e8579ef6

Effects of α-tubulin acetylation on microtubule structure and stability

Autor: Didier Portran, Eva Nogales, Thomas Löhr, Michele Vendruscolo, Rui Zhang, Lisa Eshun-Wilson, Maxence V. Nachury, Daniel B. Toso, James S. Fraser, Massimiliano Bonomi

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 21
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (21), pp.10366-10371. ⟨10.1073/pnas.1900441116⟩

Significance Microtubules are polymers of αβ-tubulin that play important roles in the cell. Regulation of their dynamics is critical for function and includes the posttranslational modification of tubulin. While most of tubulin modifications reside

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95b2d799528e00039db6eb53ecd85561
https://doi.org/10.1073/pnas.1900441116

An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase

Autor: Eric Wang, Zev A Ripstein, John L. Rubinstein, Alexander E. Conicella, Ai Nguyen, Lewis E. Kay, Peter Schuck, Rui Huang, Thomas Löhr, Michele Vendruscolo

Publikováno v: Proc Natl Acad Sci U S A

VCP/p97, an enzyme critical to proteostasis, is regulated through interactions with protein adaptors targeting it to specific cellular tasks. One such adaptor, p47, forms a complex with p97 to direct lipid membrane remodeling. Here, we use NMR and ot

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b2fd7b17e802dc585b5e3535d006476
https://europepmc.org/articles/PMC7585011/

Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease

Autor: Benedetta Mannini, Roberta Pierattelli, Thomas Löhr, Massimiliano Bonomi, Carlo Camilloni, Thomas C. T. Michaels, Francesco Simone Ruggeri, Gabriella T. Heller, Alfonso De Simone, Michele Vendruscolo, Francesco A. Aprile, Christopher M. Dobson, Ryan Limbocker, Michele Perni, Isabella C. Felli, Tuomas P. J. Knowles

Publikováno v: Science Advances 6 (2020) 45
Science Advances
Science Advances, 2020, 6 (45), pp.eabb5924. ⟨10.1126/sciadv.abb5924⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2020, 6 (45), pp.eabb5924. ⟨10.1126/sciadv.abb5924⟩
Science Advances, 6(45)

A small molecule binds to a disordered protein in its monomeric form, preventing its aggregation linked to Alzheimer’s disease.
Disordered proteins are challenging therapeutic targets, and no drug is currently in clinical use that modifies the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b3641cfe696a5f6d6e115e314da75d9