Author

L. M. Nocka

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Assay:protein structure· 1 Assay:spatial transcriptomics· 1 Approach:statistical model· 1

Frequent Co-Authors

J. Kuriyan· 3 shared J. T. Groves· 3 shared J. K. Chung· 2 shared A. N. Parikh· 1 shared A. Weiss· 1 shared B. Stinger· 1 shared C. B. Carbone· 1 shared C.-W. Lin· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

J. Kuriyan

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4 papers

Recent·Most cited

A Saturation-Mutagenesis Analysis of the Interplay Between Stability and Activation in Ras

F. Hidalgo, L. M. Nocka, N. H. Shah, K. Gorday, N. R. Latorraca, P. Bandaru, S. Templeton, D. Lee, D. Karandur, J. G. Pelton, S. Marqusee, D. Wemmer, J. Kuriyan

This study shows that cancer hotspot mutations in Ras activate it regardless of stability, while non-hotspot mutations can be activating or deleterious depending on stability.

bioRxiv · Jan 6, 2022Biophysics

A two-component protein condensate of EGFR and Grb2 regulates Ras activation at the membrane

C.-W. Lin, L. M. Nocka, B. Stinger, J. DeGrandchamp, N. Lew, S. Alvarez, H. Phan, Y. Kondo, J. Kuriyan, J. T. Groves

This study shows that EGFR and Grb2 form a condensate that regulates Ras activation through phosphorylation and dimerization.

bioRxiv · Dec 12, 2021 · PreprintBiophysics

Coupling between lipid miscibility and phosphotyrosine driven protein condensation at the membrane

J. K. Chung, W. Y. C. Huang, C. B. Carbone, L. M. Nocka, A. N. Parikh, R. Vale, J. T. Groves

The paper shows that LAT protein condensation on membrane surfaces drives lipid phase separation, which in turn localizes K-Ras into the condensate, controlled by tyrosine phosphorylation.

bioRxiv · Jul 22, 2020 · PreprintBiophysics

Switch-like activation of Bruton’s tyrosine kinase by membrane-mediated dimerization

J. K. Chung, L. M. Nocka, Q. Wang, T. A. Kadlecek, A. Weiss, J. Kuriyan, J. T. Groves

The paper identifies a switch-like PIP3 sensing mechanism in Btk's PH-TH module that enhances sensitivity through dimerization and multiple PIP3 binding.

bioRxiv · Mar 17, 2018Biophysics