Author

G. Pintacuda

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· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Approach:experimental assay· 2 Assay:protein structure· 2 Approach:statistical model· 2 Organism:fungi (other)· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Bertarello· 1 shared A. Daskalov· 1 shared A. H. Larsen· 1 shared A. Loquet· 1 shared A. Martel· 1 shared A. Natalello· 1 shared A. Noubhani· 1 shared B. Bardiaux· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperBiophysics

A. Bertarello

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3 papers

Recent·Most cited

Mg2+-dependent conformational equilibria in CorA: an integrated view on transport regulation

N. T. Johansen, M. Bonaccorsi, T. Bengtsen, A. H. Larsen, F. G. Tidemand, M. C. Pedersen, P. Huda, J. Berndtsson, T. Darwish, N. R. Yepuri, A. Martel, T. Pomorski, A. Bertarello, M. S. Sansom, M. Rapp, , L. Arleth

This study investigates the conformational dynamics of CorA, revealing Mg2+-dependent conformational equilibria and dynamic behavior through SANS, MD simulations, and NMR.

bioRxiv · Aug 20, 2021Biophysics

Structural and molecular basis of cross-seeding barriers in amyloids

A. Loquet, A. Daskalov, V. Coustou, N. El Mammeri, M. Berbon, L. Andreas, B. Bardiaux, J. Stanek, A. Noubhani, B. Kauffmann, J. Wall, G. Pintacuda, S. Saupe, B. Habenstein

This study identifies molecular determinants that prevent cross-seeding between structurally similar amyloids, revealing that side-chain positions, not just backbone structure, dictate prion specificity.

bioRxiv · Jul 6, 2020Biochemistry

Conformational stability and dynamics in crystals recapitulate protein behaviour in solution

B. M. Sala, T. Le Marchand, G. Pintacuda, C. Camilloni, A. Natalello, S. Ricagno

This study shows that conformational dynamics and stability of β2m in crystals mirror its behavior in solution, supporting the use of crystals for studying protein unfolding and aggregation.

bioRxiv · Apr 27, 2020Biochemistry