Author

D. C. Favaro

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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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:development & morphogenesis· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Research Focus:metabolism & bioenergetics· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

K. H. Gardner· 2 shared A. L. Davalos· 1 shared C. D. Lacerda· 1 shared C. KIKANI· 1 shared C. S. Farah· 1 shared G. Carretero· 1 shared I. M. Cuccovia· 1 shared J. Closson· 1 shared

Activity by Year

2023-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiochemistry

K. H. Gardner

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3 papers

Recent·Most cited

Identification of Small Molecule Ligand Binding Sites On and In the ARNT PAS-B Domain

X. Xu, J. Closson, L. P. Marcelino, D. C. Favaro, M. L. Silvestrini, R. Solazzo, L. T. Chong, K. H. Gardner

The paper identifies ligand-binding sites on and within the ARNT PAS-B domain using NMR, MD simulations, and ensemble docking, revealing distinct binding modes for three small molecules.

bioRxiv · Nov 3, 2023Biochemistry

Signal-regulated unmasking of the nuclear localization motif in the PAS domain regulates the nuclear translocation of PASK.

M. Xiao, S. Dhungel, R. Azad, D. C. Favaro, R. R. Pushpabai, K. H. Gardner, C. KIKANI

This study identifies a mechanism by which PASK's nuclear translocation is regulated by the interaction between its PAS-A domain and a PIM motif, which is modulated by metabolic signals.

bioRxiv · Sep 6, 2023Biochemistry

Uncovering the association mechanism between two intrinsically flexible proteins

A. L. Davalos, J. D. Rivera, D. C. Favaro, R. J. d. Oliveira, G. Carretero, C. D. Lacerda, I. M. Cuccovia, M. V. C. Cardoso, C. S. Farah, R. K. Salinas

The paper investigates how two intrinsically flexible proteins interact, finding that binding occurs via conformational selection and temperature affects the pathway to the native complex.

bioRxiv · Jun 19, 2023Biophysics