Author

G. Giachin

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· 4 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:chromatin & epigenetic regulation· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Organism:Drosophila· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

A. N. Volkov· 1 shared A. Sosic· 1 shared B. Gatto· 1 shared C. Mota· 1 shared C. Salata· 1 shared C. Zubieta· 1 shared C. Zucchelli· 1 shared D. de Sanctis· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

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1 shared paperBiochemistry

A. N. Volkov

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Author profile →

5 papers

Recent·Most cited

Metal ion activation and DNA recognition by the Deinococcus radiodurans manganese sensor DR2539

C. Mota, M. Webster, M. Saidi, U. Kapp, C. Zubieta, G. Giachin, J. A. Manso, D. de Sanctis

This study investigates the metal ion activation and DNA recognition mechanisms of DR2539 in Deinococcus radiodurans using biophysical analyses and structural data.

bioRxiv · Feb 12, 2024 · PreprintBiophysics

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

A novel conformational state for SARS-CoV-2 main protease

E. Fornasier, M. L. Macchia, G. Giachin, A. Sosic, M. Pavan, M. Sturlese, C. Salata, S. Moro, B. Gatto, M. Bellanda, R. Battistutta

This paper reports a new conformational state of SARS-CoV-2 main protease, revealing structural changes that could inform the design of novel antiviral inhibitors.

bioRxiv · Mar 4, 2021 · PreprintBiochemistry

Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins

L. Qin, F. Ben Bdira, Y. G. J. Sterckx, A. N. Volkov, J. Vreede, G. Giachin, P. van Schaik, M. Ubbink, R. T. Dame

This study identifies the molecular mechanism by which H-NS proteins switch DNA binding states in response to osmotic changes, showing that ionic strength affects electrostatic interactions between domains.

bioRxiv · Sep 5, 2019Biochemistry

Deciphering copper coordination in the animal prion protein amyloidogenic domain

G. Salzano, M. Brennich, G. Mancini, T. H. Tran, G. Legname, P. D'Angelo, G. Giachin

This study investigates copper coordination in the non-OR region of prion proteins from different animal species, revealing structural differences linked to TSE resistance or susceptibility.

bioRxiv · Dec 28, 2018Biochemistry