Author

G. G. Gundersen

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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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:human· 1 Organism:mouse· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Vahabikashi· 1 shared C. Ostlund· 1 shared C. Y. Park· 1 shared F. A. S. Nicdao· 1 shared G. G. Luxton· 1 shared G. W. G. Luxton· 1 shared H. J. Worman· 1 shared J. J. Fredberg· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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1 shared paperBiophysics

A. Vahabikashi

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3 papers

Recent·Most cited

Nuclear lamin isoforms differentially contribute to LINC complex-dependent nucleocytoskeletal coupling and whole cell mechanics

A. Vahabikashi, S. Sivagurunathan, F. A. S. Nicdao, Y. L. Han, C. Y. Park, X. Wong, J. R. Tran, G. G. Gundersen, K. Reddy, G. G. Luxton, M. Guo, J. J. Fredberg, Y. Zheng, S. A. Adam, R. D. Goldman

This study shows that different nuclear lamin isoforms modulate cell and nuclear mechanics by affecting LINC complex stability and heterochromatin structure in mouse embryonic fibroblasts.

bioRxiv · May 12, 2021Biophysics

Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins

S. M. Lim, V. E. Cruz, S. Antoku, G. G. Gundersen, T. Schwartz

The paper reports the crystal structure of FHOD1-Nes2G complexes, revealing that the FH3 domain of formins binds spectrin repeats and suggests overlapping functions of Nesprin1/2 in actin-bundle recruitment for nuclear movement.

bioRxiv · Jun 19, 2020Biochemistry

Imbalanced Nucleocytoskeletal Connections Create Common Polarity Defects in Progeria and Physiological Aging

W. Chang, Y. Wang, G. W. G. Luxton, C. Ostlund, H. J. Worman, G. G. Gundersen

This study identifies imbalanced nucleocytoskeletal connections as a cause of polarity defects in progeria and aging, showing that rebalancing these connections can restore normal cell function.

bioRxiv · Dec 15, 2018Cell Biology