Author

T. Schulte

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Biophysics· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:host-pathogen & immune response· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Organism:C. elegans· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1

Frequent Co-Authors

S. Ricagno· 3 shared G. Mazzini· 2 shared G. Merlini· 2 shared G. Palladini· 2 shared M. D. Panas· 2 shared M. Nuvolone· 2 shared N. Kedersha· 2 shared P. Milani· 2 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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3 shared papersBiophysics

S. Ricagno

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Nanobodies counteract the toxicity of an amyloidogenic light chain by stabilizing a partially open dimeric conformation

L. Broggini, M. Barzago, V. Speranzini, T. Schulte, F. Sonzini, M. Giono, M. Romeo, P. Milani, S. Caminito, G. Mazzini, P. Rognoni, G. Merlini, C. Pappone, L. Anastasia, M. Nuvolone, , S. Ricagno

This study identifies nanobodies that counteract the toxicity of an amyloidogenic light chain by stabilizing a partially open dimeric conformation, revealing insights into toxicity mechanisms.

bioRxiv · Aug 28, 2023Biophysics

The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with chemokine CXCL12

M. V. Mantonico, F. De Leo, G. Quilici, L. Colley, F. De Marchis, M. Crippa, T. Schulte, C. Zucchelli, S. Ricagno, G. Giachin, m. ghitti, M. E. Bianchi, G. Musco

This study identifies the acidic intrinsically disordered region of HMGB1 as critical for forming a dynamic fuzzy heterocomplex with CXCL12, which enhances inflammatory signaling through CXCR4.

bioRxiv · Jun 6, 2023Biochemistry

Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter

T. Schulte, A. Chaves-Sanjuan, G. Mazzini, V. Speranzini, F. Lavatelli, F. Ferri, C. Palizzotto, M. Mazza, P. Milani, M. Nuvolone, A.-C. Vogt, G. Palladini, G. Merlini, M. Bolognesi, S. Ferro, , S. Ricagno

The paper presents a cryo-EM structure of AA amyloid fibrils from a cat with renal failure, revealing a distinct amyloid fold despite high sequence homology to human and mouse SAA.

bioRxiv · May 9, 2022Biophysics

Caprin-1 binding to the critical stress granule protein G3BP1 is regulated by pH

T. Schulte, M. D. Panas, L. Wiliams, N. Kedersha, J. S. Fleck, T. J. C. Tan, A. Olsson, A. M. Morro, L. Hanke, J. Nilvebrant, K. A. Giang, P.-A. Nygren, P. Anderson, A. Achour, G. M. McInerney

This study shows that Caprin-1 binds to G3BP1's NTF2 domain with pH sensitivity, regulating stress granule formation through a SLiM-mediated mechanism.

bioRxiv · Feb 5, 2021Biochemistry

Revisiting G3BP-S149 phosphorylation and its impact on stress granule assembly

M. D. Panas, N. Kedersha, T. Schulte, R. M. Branca, P. Ivanov, P. J. Anderson

The paper investigates the role of G3BP1-S149 phosphorylation in stress granule assembly, revealing that unintended mutations in engineered constructs confound previous conclusions about S149's effect.

bioRxiv · Apr 9, 2019Cell Biology