Author

G. Merlini

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

Biology Disciplines

Click to filter author papers

Biophysics· 2 Biochemistry· 1 Pathology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Assay:cryo-EM· 2 Research Focus:protein structure prediction· 2 Organism:C. elegans· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

G. Palladini· 4 shared S. Ricagno· 4 shared F. Lavatelli· 3 shared G. Mazzini· 3 shared P. Milani· 3 shared A.-C. Vogt· 2 shared E. Zini· 2 shared F. Ferri· 2 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

4 shared papersBiophysics

G. Palladini

Mutual co-authors in cluster

Author profile →

4 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

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

AA-amyloidosis in cats (Felis catus) housed in shelters

F. Ferri, S. Ferro, F. Porporato, C. Callegari, C. Guglielmetti, M. Mazza, M. Ferrero, C. Crino, E. Gallo, M. Drigo, L. M. Coppola, G. Gerardi, T. P. Schulte, S. Ricagno, M. Vogel, , E. Zini

The paper reports high prevalence of AA-amyloidosis in sheltered cats, linking shelter stay duration to disease severity and identifying SAA as the causative protein.

bioRxiv · May 4, 2022 · PreprintPathology

Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain (AL) amyloidosis patient

P. Swuec, F. Lavatelli, M. Tasaki, C. Paissoni, P. Rognoni, M. Maritan, F. Brambilla, P. Milani, P. Mauri, C. Camilloni, G. Palladini, G. Merlini, S. Ricagno, M. Bolognesi

The paper reports the cryo-EM structure of cardiac amyloid fibrils from an AL amyloidosis patient, revealing key structural features of the light chain variable domain involved in fibril formation.

bioRxiv · Oct 17, 2018Biochemistry