Author

N. Pozzi

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· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 4 Approach:experimental assay· 3 Organism:human· 3 Assay:protein structure· 3 Approach:mechanistic / dynamical model· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

M. Chinnaraj· 3 shared A. Biswas· 1 shared A. Patterson· 1 shared B. Bothner· 1 shared E. Antony· 1 shared E. Ruben· 1 shared E. Tajkhorshid· 1 shared F. Tedesco· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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3 shared papersBiochemistry

M. Chinnaraj

Mutual co-authors in cluster

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5 papers

Recent·Most cited

Atomistic Characterization of Beta-2-Glycoprotein I Domain V Interaction with Anionic Membranes

H. S. Hasdemir, N. Pozzi, E. Tajkhorshid

This study identifies key regions and binding modes of beta-2-glycoprotein I domain V interacting with anionic membranes, important for antiphospholipid syndrome pathogenesis.

bioRxiv · Mar 19, 2024Biophysics

The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.

Y. Kyriukha, M. B. Watkins, J. M. Redington, R. Dastvan, V. N. Uversky, J. B. Hopkins, N. Pozzi, S. Korolev

This study identifies the PALB2 DNA-binding domain as an intrinsically disordered region that promotes DNA compaction through oligomerization, revealing a novel strand exchange mechanism.

bioRxiv · Jun 1, 2023Biophysics

Dynamic states of eIF6 and SDS variants modulate interactions with uL14 of the 60S ribosomal subunit.

J. Elliff, A. Biswas, S. Kuppa, P. Roshan, R. Burd, M. Chinnaraj, A. Patterson, J. Mattice, S. Walker, N. Pozzi, E. Antony, B. Bothner, S. S. Origanti

This study identifies key residues in eIF6 and RPL23 that mediate their interaction and shows how mutations in SDS disrupt this interaction, offering a therapeutic target for cancer and SDS.

bioRxiv · Jul 29, 2022Biochemistry

Reduction of protein disulfide isomerase results in open conformations and stimulates dynamic exchange between structural ensembles

M. Chinnaraj, R. Flaumenhaft, N. Pozzi

This study uses smFRET to show PDI adopts three conformational ensembles, with redox state affecting their population and exchange rates.

bioRxiv · Dec 7, 2020Biophysics

X-ray and solution structures of human beta-2 glycoprotein I reveal a new mechanism of autoantibody recognition

E. Ruben, W. Planer, M. Chinnaraj, Z. Chen, X. Zuo, V. Pengo, V. De Filippis, R. Alluri, K. McCrae, P. Macor, F. Tedesco, N. Pozzi

This paper reveals the structure of human beta-2 glycoprotein I and shows that its elongated, flexible conformation allows autoantibodies to recognize an epitope without phospholipids.

bioRxiv · Feb 25, 2020Biochemistry