Author

P. Bernado

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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Biophysics· 6 Biochemistry· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:protein structure· 6 Research Focus:protein folding & dynamics· 5 Approach:statistical model· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

N. Sibille· 6 shared F. Allemand· 5 shared A. Sagar· 4 shared A. Fournet· 3 shared A. Barducci· 2 shared A. Estana· 2 shared A. le Maire· 2 shared A. Morato· 2 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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6 shared papersBiophysics

N. Sibille

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction

M. Guillien, A. Mouhand, A. Sagar, A. Fournet, F. Allemand, G. A. N. Pereira, A. Thureau, P. Bernado, J.-L. Baneres, N. Sibille

The paper investigates how phosphorylation of GPCR C-terminal domains affects their conformation and arrestin interaction, revealing phosphorylation-dependent structural changes that influence signaling outcomes.

Structure · Nov 1, 2023Peer-reviewedBiophysics

Site-Specific Introduction of Alanines for the NMR Investigation of Low-Complexity Regions and Large Biomolecular Assemblies

C. A. Elena-Real, A. Urbanek, L. Imbert, A. Morato, A. Fournet, F. Allemand, N. Sibille, J. BOISBOUVIER, P. Bernado

This paper introduces a method to site-specifically incorporate isotopically labeled alanines into proteins for NMR studies, enabling structural analysis of large biomolecular assemblies and low-complexity regions.

bioRxiv · May 8, 2023 · PreprintBiochemistry

The structure of pathogenic huntingtin exon-1 defines the bases of its aggregation propensity

C. A. Elena-Real, A. Sagar, A. Urbanek, M. Popovic, A. Morato, A. Estana, A. Fournet, X. L. Lund, Z.-D. Shi, L. Costa, A. Thureau, F. Allemand, R. E. Swenson, P.-E. Milhiet, A. Barducci, , P. Bernado

This study investigates how the structure of pathogenic huntingtin exon-1 with expanded poly-Q tracts influences its aggregation propensity and fibril formation.

bioRxiv · Oct 25, 2022Biophysics

Conformational buffering underlies functional selection in intrinsically disordered protein regions

N. S. Gonzalez-Foutel, W. M. Borcherds, J. Glavina, S. Barrera-Vilarmau, A. Sagar, A. Estana, A. Barozet, G. Fernandez-Ballester, C. Blanes-Mira, I. E. Sanchez, G. de Prat Gay, J. Cortes, P. Bernado, R. V. Pappu, A. S. Holehouse, , L. B. Chemes

The paper identifies conformational buffering as a mechanism that conserves spatial dimensions in disordered protein regions despite sequence variation, enabling functional selection.

bioRxiv · May 14, 2021Biophysics

Molecular and cellular insight into Escherichia coli SslE and its role during biofilm maturation

P. Corsini, S. Wang, S. Rehman, K. Fenn, A. Sagar, S. Sirovica, L. Cleaver, C. J. C. Edwards-Gayle, G. Mastroianni, B. Dorgan, L. M. Sewell, S. Lynham, D. Iuga, W. T. Franks, J. Jarvis, , J. A. Garnett

This study investigates the structure and function of SslE in E. coli biofilm maturation, showing its role in aggregate formation and exopolysaccharide distribution under acidic conditions.

bioRxiv · Feb 7, 2021Microbiology

Structural insights into the cooperative interaction of the intrinsically disordered co-activator TIF2 with retinoic acid receptor heterodimer (RXR/RAR)

L. Senicourt, A. le Maire, F. Allemand, J. E. Carvalho, L. Guee, P. Germain, M. Schubert, P. Bernado, W. Bourguet, N. Sibille

The paper determines the structural features of TIF2NRID and its cooperative binding to RXR/RAR, revealing partially structured regions and the role of flanking sequences.

bioRxiv · Oct 28, 2020Biophysics

Multivalent interactions between eIF4G1, Pub1 and Pab1 drive the formation of protein condensates

B. Chaves-Arquero, S. Martinez-Lumbreras, N. Sibille, S. Camero, P. Bernado, M. A. Jimenez, S. Zorrilla, J. M. Perez-Canadillas

The paper studies interactions between eIF4G1, Pub1, and Pab1 using NMR and SAXS, revealing their role in forming protein condensates and regulating stress granule formation.

bioRxiv · Aug 7, 2020 · PreprintBiophysics

Interplay of protein disorder in retinoic acid receptor heterodimer and its corepressor regulates gene expression

T. N. Cordeiro, N. Sibille, P. Germain, P. Barthe, A. Boulahtouf, F. Allemand, R. Bailly, V. Vivat, C. Ebel, A. Barducci, W. Bourguet, A. le Maire, P. Bernado

This study shows that the structural dynamics of the H12 helix in RXR/RAR heterodimers and the intrinsic disorder of N-CoR regulate gene expression through conformational changes and corepressor complex formation.

bioRxiv · Oct 25, 2018Biophysics