Author

A. Turkiewicz

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· 3 Research Focus:cell type annotation· 2 Organism:human· 2 Assay:imaging· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:differential expression· 1 Research Focus:metabolism & bioenergetics· 1 Assay:metabolomics· 1

Frequent Co-Authors

M. Englund· 2 shared S. Saarakkala· 2 shared B. D. Giaimo· 1 shared B. D. VanderWielen· 1 shared C. E. Collins· 1 shared E. Folkesson· 1 shared F. Oswald· 1 shared H. Isaksson· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiophysics

M. Englund

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Associations of human femoral condyle cartilage structure and composition with viscoelastic and constituent-specific material properties at different stages of osteoarthritis

M. Ebrahimi, A. Turkiewicz, M. A. J. Finnila, S. Saarakkala, M. Englund, R. K. Korhonen, P. Tanska

This study examines how structural and compositional changes in human knee cartilage relate to mechanical properties across osteoarthritis stages.

bioRxiv · May 1, 2022Biophysics

Mineral crystal thickness in calcified cartilage and subchondral bone in healthy and osteoarthritic knees

M. A. J. Finnilä, S. Das Gupta, M. J. Turunen, I. Kestilä, A. Turkiewicz, V. Lutz-Bueno, E. Folkesson, M. Holler, N. Ali, V. Hughes, H. Isaksson, J. Tjörnstrand, P. Önnerfjord, M. Guizar-Sicairos, S. Saarakkala, M. Englund

The paper measures mineral crystal thickness in calcified cartilage and subchondral bone of healthy and osteoarthritic knees, finding increased thickness in the unloaded lateral compartment and decreased thickness in subchondral bone with OA severity.

bioRxiv · Jun 15, 2021 · PreprintBiophysics

Structural and functional studies of the RBPJ-SHARP complex reveal conserved corepressor binding site

Z. Yuan, B. D. VanderWielen, B. D. Giaimo, L. Pan, C. E. Collins, A. Turkiewicz, K. Hein, F. Oswald, T. Borggrefe, R. A. Kovall

This study determines the structure of the RBPJ-SHARP complex and shows that SHARP binding is essential for RBPJ's repressor function in Notch signaling.

bioRxiv · May 10, 2018Biochemistry