Author

T. Viennet

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· 1 Biophysics· 1 Scientific Communication & Education· 1

Signature Assays, Organisms & Methods

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Approach:benchmark study· 1 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:database / resource· 1 Approach:experimental assay· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

H. Arthanari· 2 shared A. Hatos· 1 shared A. K. Buell· 1 shared A. Salguero· 1 shared B. Meszaros· 1 shared B. Strodel· 1 shared B. Uluca· 1 shared C. M. Jeffries· 1 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersScientific Communication & Education

H. Arthanari

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Author profile →

3 papers

Recent·Most cited

MIADE metadata guidelines: Minimum Information About a Disorder Experiment

B. Meszaros, A. Hatos, N. Palopoli, F. Quaglia, E. Salladini, K. Van Roey, H. Arthanari, Z. Dosztanyi, I. C. Felli, P. D. Fischer, J. Hoch, C. M. Jeffries, S. Longhi, E. Maiani, S. Orchard, , N. E. Davey

The paper introduces MIADE guidelines to standardize metadata for experiments studying intrinsically disordered proteins, improving data interpretation and reproducibility.

bioRxiv · Jul 12, 2022 · PreprintScientific Communication & Education

PH Domain-Mediated Autoinhibition and Oncogenic Activation of Akt

H. Bae, T. Viennet, E. Park, N. Chu, A. Salguero, M. J. Eck, H. Arthanari, P. A. Cole

This study identifies a mutation in the PH domain of Akt that enhances autoinhibition and reveals the molecular mechanism of Akt activation as an oncogenic driver.

bioRxiv · May 25, 2022Biochemistry

A structural and kinetic link between membrane association and amyloid fibril formation of α-Synuclein

T. Viennet, M. M. Wördehoff, B. Uluca, C. Poojari, H. Shaykhalishahi, D. Willbold, B. Strodel, H. Heise, A. K. Buell, W. Hoyer, M. Etzkorn

This study investigates how α-Synuclein interacts with membrane surfaces and how these interactions influence its aggregation into amyloid fibrils.

bioRxiv · Aug 8, 2017Biophysics