Author

A. Pandini

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Organism:E. coli· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

A. Fornili· 1 shared A. Mey· 1 shared A. Ramanathan· 1 shared B. Islam· 1 shared B. Stieglitz· 1 shared C. J. Petzold· 1 shared C. Y. Ralston· 1 shared D. BHOWMIK· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiochemistry

A. Fornili

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

N4BP1 is dimerization-dependent linear ubiquitin reader regulating TNFR1 signalling through linear ubiquitin binding and Caspase-8-mediated processing

K. W. Kliza, W. Song, I. Pinzuti, S. Schaubeck, S. Kunzelmann, D. Kuntin, A. Fornili, A. Pandini, K. Hofmann, J. Garnett, B. Stieglitz, K. Husnjak

This study identifies N4BP1 as a dimerization-dependent linear ubiquitin reader that regulates TNFR1 signaling by modulating NF-κB and apoptosis pathways.

bioRxiv · Nov 2, 2021 · PreprintBiochemistry

Structural dynamics of the β-coronavirus Mpro protease ligand binding sites

E. Cho, M. Rosa, R. Anjum, S. Mehmood, M. Soban, M. Mujtaba, K. Bux, S. C. Dantu, A. Pandini, J. Yin, H. Ma, A. Ramanathan, B. Islam, A. Mey, D. BHOWMIK, S. Haider

The paper compares ligand-binding sites of Mpro proteases from SARS-CoV2, SARS-CoV, and MERS-CoV using deep learning and Markov state models to assess structural dynamics and conservation.

bioRxiv · Mar 31, 2021 · PreprintBiophysics

Allosteric priming of E. coli CheY by the flagellar motor protein FliM

P. Wheatley, A. Pandini, S. Gupta, Y. Chen, C. J. Petzold, C. Y. Ralston, D. F. Blair, S. M. Khan

This study uses molecular dynamics and experimental methods to show that phosphorylation of CheY increases its affinity for FliMN by altering conformational dynamics and sidechain burial.

Biophysical Journal · Sep 1, 2020Peer-reviewedBiophysics