Author

J. R. Requena

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· 3 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 3 Approach:statistical model· 3 Approach:deep learning· 2 Organism:mouse· 2 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

E. Biasini· 5 shared G. Spagnolli· 5 shared L. C. Fernandez· 3 shared p. faccioli· 3 shared A. Boldrini· 2 shared A. Iglesias· 2 shared H. Erana· 2 shared J. Castilla· 2 shared

Activity by Year

2018-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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5 shared papersBiochemistry

E. Biasini

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Author profile →

5 papers

Recent·Most cited

Solid state NMR reveals a parallel in register architecture for an infectious recombinant prion

M. Martin-Pastor, Y. B. Codeseira, G. Spagnolli, H. Erana, L. C. Fernandez, D. Martin, S. Bravo, N. Lopez-Lorenzo, A. Iglesias, R. Lopez-Moreno, R. Sabate, S. Veiga, H. Rezaei, E. Biasini, V. M. Sanchez-Pedregal, , J. R. Requena

The paper uses solid state NMR to analyze the structure of infectious recombinant prion, finding support for the parallel in register beta stack model over the 4-rung beta-solenoid model.

bioRxiv · Jul 20, 2021 · PreprintBiochemistry

All-Atom Simulation of the HET-s Prion Replication

L. Terruzzi, G. Spagnolli, A. Boldrini, J. R. Requena, E. Biasini, p. faccioli

This study uses all-atom simulations to investigate HET-s prion replication, finding similarities in templating mechanisms between fungal and mammalian prions.

PLOS Computational Biology · Sep 18, 2020Peer-reviewedBiophysics

Structural features of an infectious recombinant PrPSc prion using solid state NMR

M. Martin-Pastor, Y. B. Codeseira, G. Spagnolli, H. Erana, L. C. Fernandez, S. Bravo, A. Iglesias, R. Lopez-Moreno, S. Veiga, E. Biasini, V. M. Sanchez-Pedregal, J. Castilla, J. R. Requena

This study uses solid-state NMR to analyze the structure of a recombinant PrPSc prion and validates a proposed atomistic model of its beta-solenoid structure.

bioRxiv · Apr 8, 2020 · PreprintBiochemistry

PHARMACOLOGICAL PROTEIN INACTIVATION BY TARGETING FOLDING INTERMEDIATES

G. Spagnolli, T. Massignan, A. Astolfi, S. Biggi, P. Brunelli, M. Libergoli, A. Ianeselli, S. Orioli, A. Boldrini, L. Terruzzi, G. Maietta, M. Rigoli, N. Lopez Lorenzo, L. C. Fernandez, L. Tosatto, , E. Biasini

The paper discovers non-native metastable states in protein folding pathways and develops a novel drug discovery approach, PPI-FIT, to target these intermediates to lower protein expression.

bioRxiv · Mar 31, 2020 · PreprintBiochemistry

Full Atomistic Model Of Prion Structure And Conversion

G. Spagnolli, M. Rigoli, S. Orioli, A. M. Sevillano, P. Faccioli, H. Wille, E. Biasini, J. R. Requena

The paper builds the first atomic-resolution model of mouse PrPSc using experimental data and computational methods, simulating the conversion of PrPC to PrPSc and providing a physically-coherent mechanism for prion propagation.

bioRxiv · Dec 22, 2018Biochemistry