Author

C. Nowotny

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

J. Chen· 2 shared M. Jin· 2 shared Z. Yu· 2 shared A. Diallo· 1 shared A. F. Brilot· 1 shared A. Fossati· 1 shared A. M. Smith· 1 shared A. Mancino· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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2 shared papersBiochemistry

J. Chen

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structural features of mTORC2 that control substrate-specific activities.

Z. Yu, J. Chen, E. Takagi, F. Wang, X. Liu, L.-M. Jourbert, B. Saha, C. Gleason, M. Jin, C. Li, C. Nowotny, D. Agard, Y. Cheng, D. Pearce

The paper determines the structure of mTORC2 and shows how substrate-specific interactions and conformational changes regulate its activity.

bioRxiv · Feb 3, 2022 · PreprintBiochemistry

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

M. Gupta, C. M. Azumaya, M. Moritz, S. Pourmal, A. Diallo, G. E. Merz, G. M. Jang, M. Bouhaddou, A. Fossati, A. F. Brilot, D. Diwanji, E. Hernandez, N. Herrera, H. T. Kratochvil, V. L. Lam, , K. I Pawar

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

bioRxiv · May 10, 2021 · PreprintBiophysics

PIKfyve inhibition blocks endolysosomal escape of α-synuclein fibrils and spread of α-synuclein aggregation

S. K. See, M. Chen, S. Bax, R. Tian, A. Woerman, E. Tse, I. E. Johnson, C. Nowotny, E. N. Munoz, J. Sengstack, D. R. Southworth, J. E. Gestwicki, M. D. Leonetti, M. Kampmann

The paper identifies PIKfyve inhibition as a strategy to block α-synuclein fibril escape from lysosomes, reducing aggregation spread in a human cell model.

bioRxiv · Jan 21, 2021 · PreprintCell Biology