Author

S. Milanova

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 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:machine learning (classical)· 1 Assay:multiome· 1 Assay:proteomics· 1

Frequent Co-Authors

A. F. Pinto· 1 shared A. Nordstrom· 1 shared A. Viljamaa· 1 shared A. Zacharouli· 1 shared A.-G. Thorsell· 1 shared B. Bozoky· 1 shared B. Schmierer· 1 shared C. Bjorkegren· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperBiochemistry

A. F. Pinto

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

A distinctive tumor compartment in pancreatic lobules defined by nascent stroma and classical tumor cell phenotype

S. I. M. Söderqvist, A. Viljamaa, N. Geyer, C. Strell, N. Hekmati, J. Engstrand, E. Sparrelid, C. Salmen, R. L. Heuchel, A. Zacharouli, P. Ghorbani, S. Harrizi, Y. Hamidi, O. Khorosjutina, S. Milanova, , M. Gerling

This study identifies a distinctive PDAC niche in pancreatic lobules characterized by nascent stroma and classical tumor cell phenotype, highlighting the role of acinar-to-ductal metaplasia and microenvironmental factors in tumor progression.

bioRxiv · Mar 14, 2024 · PreprintCancer Biology

14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface

T. Karlberg, P. Hornyak, A. F. Pinto, S. Milanova, M. Ebrahimi, M. Lindberg, N. Pullen, A. Nordstrom, E. Loverli, R. Caraballo, E. V. Wong, K. Nareoja, A.-G. Thorsell, M. Elofsson, E. M. De La Cruz, , H. Schuler

This study identifies a novel hydrophobic interface between 14-3-3 proteins and Pseudomonas exotoxins-S and -T, showing 14-3-3 activates these toxins by preventing aggregation, independent of their C-terminal phosphopeptide binding motifs.

bioRxiv · Jun 8, 2018Biochemistry