Author

R. B. Nowak

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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Cell Biology· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 4 Approach:experimental assay· 2 Organism:human· 2 Assay:imaging· 2 Approach:microscopy & imaging analysis· 2 Organism:mouse· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

V. M. Fowler· 4 shared C. Cheng· 2 shared A. S. Smith· 1 shared D. S. Gokhin· 1 shared H. Alimohamadi· 1 shared I. C. Ghiran· 1 shared J. Papoin· 1 shared J. Parreno· 1 shared

Activity by Year

2017-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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4 shared papersCell Biology

V. M. Fowler

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Author profile →

4 papers

Recent·Most cited

Nanoscale organization of Actin Filaments in the Red Blood Cell Membrane Skeleton

R. B. Nowak, H. Alimohamadi, K. Pestonjamasp, P. Rangamani, V. M. Fowler

This study investigates the nanoscale organization of F-actin nodes in red blood cell membranes using advanced microscopy and computational analysis, revealing non-uniform distribution and dynamic behavior.

bioRxiv · Mar 7, 2021 · PreprintBiophysics

Tropomyosin 3.5 protects F-actin networks required for tissue biomechanical properties

C. Cheng, R. B. Nowak, M. B. Amadeo, S. K. Biswas, W.-K. Lo, V. M. Fowler

This study shows that Tpm3.5 stabilizes F-actin networks in mouse lens fiber cells, maintaining tissue biomechanical properties and mechanical resilience.

bioRxiv · Jun 29, 2018Cell Biology

The effects of mechanical strain on mouse eye lens capsule and cellular microstructure

J. Parreno, C. Cheng, R. B. Nowak, V. M. Fowler

This study examines how mechanical strain affects the structure of mouse eye lenses, finding reversible and irreversible changes in microstructure depending on strain magnitude.

bioRxiv · Jan 14, 2018Cell Biology

Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability

A. S. Smith, R. B. Nowak, S. Zhou, M. Gianetto, D. S. Gokhin, J. Papoin, I. C. Ghiran, L. Blanc, J. Wan, V. M. Fowler

This paper shows that myosin IIA interacts with the spectrin-actin membrane skeleton in red blood cells to control membrane curvature and deformability by exerting contractile forces.

bioRxiv · Oct 19, 2017Cell Biology