Author

C. L. Gee

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· 6 Biophysics· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:protein folding & dynamics· 6 Assay:structural biology· 3 Organism:plant (other)· 2 Assay:protein structure· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1

Frequent Co-Authors

J. Kuriyan· 5 shared S. Marqusee· 3 shared A. S. G. Larsen· 2 shared B. Frolund· 2 shared C. C. Chi· 2 shared E. D. McSpadden· 2 shared L. Hamborg· 2 shared N. Griem-Krey· 2 shared

Activity by Year

2019-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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5 shared papersBiochemistry

J. Kuriyan

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

Nub1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome

C. Arkinson, K. C. Dong, C. L. Gee, S. M. Costello, S. Marqusee, A. Martin

This paper identifies how Nub1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome through a novel mechanism involving structural dynamics and proteasomal engagement.

bioRxiv · Jun 12, 2024Biochemistry

Ligand-induced CaMKIIα hub Trp403 flip, hub domain stacking and kinase inhibition

D. Narayanan, A. S. G. Larsen, S. J. Gauger, R. Adafia, R. B. Hammershoi, L. Hamborg, J. Bruus-Jensen, N. Griem-Krey, C. L. Gee, B. Frolund, M. M. Stratton, J. Kuriyan, J. S. Kastrup, A. E. Langkilde, P. Wellendorph, S. M. O. Solbak

This paper investigates how PIPA, a GHB analog, affects CaMKII hub domain conformation and stability, revealing a mechanism involving Trp403 flip and hub domain stacking that reduces kinase activity.

bioRxiv · Mar 26, 2024 · PreprintBiophysics

Crystal Structure of the kinase domain of a receptor tyrosine kinase from a choanoflagellate, Monosiga brevicollis

T. Bajaj, J. Kuriyan, C. L. Gee

The paper determines the crystal structure of a receptor tyrosine kinase from Monosiga brevicollis and shows its ability to phosphorylate tyrosine residues.

bioRxiv · Oct 7, 2022Biochemistry

Temporal and Spatial Resolution of a Protein Quake that Activates Hydrogen Tunneling in Soybean Lipoxygenase

J. P. Zaragoza, A. R. Offenbacher, S. Hu, C. L. Gee, Z. M. Firestein, N. Minnetian, Z. Deng, F. Fan, A. T. Iavarone, J. P. Klinman

This study investigates hydrogen tunneling in soybean lipoxygenase using X-ray and deuterium exchange experiments, revealing a protein quake mechanism linked to catalytic activation.

bioRxiv · Mar 31, 2022 · PreprintBiophysics

Crystal structure of an RNA/DNA strand exchange junction

J. C. Cofsky, G. J. Knott, C. L. Gee, J. A. Doudna

The paper reports the X-ray crystal structure of an RNA/DNA strand exchange junction, revealing structural principles of A-to-B helical transitions in RNA/DNA hybrids.

bioRxiv · Jan 24, 2022Biochemistry

Differences in the dynamics of the tandem-SH2 modules of the Syk and ZAP-70 tyrosine kinases

H. T. Hobbs, N. H. Shah, J. M. Badroos, C. L. Gee, S. Marqusee, J. Kuriyan

This study compares the conformational dynamics of the tandem-SH2 modules in Syk and ZAP-70 kinases, revealing differences in their autoinhibited states and activation mechanisms.

bioRxiv · Jul 20, 2021Biochemistry

GHB confers neuroprotection by stabilizing the CaMKIIα hub domain

U. Leurs, A. B. Klein, E. D. McSpadden, N. Griem-Krey, S. M. Solbak, J. Houlton, I. S. Villumsen, S. B. Vogensen, L. Hamborg, S. J. Gauger, L. B. Palmelund, A. S. G. Larsen, M. A. Shehata, C. D. Kelstrup, J. V. Olsen, , P. Wellendorph

This study shows that GHB stabilizes the CaMKII hub domain, providing neuroprotection in cellular and mouse models.

bioRxiv · Sep 28, 2020 · PreprintBiochemistry

Exploring the evolutionary history of kinetic stability in the alpha-lytic protease family

C. F. Nixon, S. A. Lim, Z. R. Sailer, I. N. Zheludev, C. L. Gee, B. A. Kelch, M. J. Harms, S. Marqusee

This study investigates how sequence variation in the alpha-lytic protease family relates to kinetic stability and energy landscapes, finding that pro-region size and specific amino acids influence folding speed and stability.

bioRxiv · Aug 30, 2020Biophysics

Variation in assembly stoichiometry in non-metazoan homologs of the hub domain of Ca2+/Calmodulin-dependent protein kinase II

E. D. McSpadden, Z. Xia, C. C. Chi, A. C. Susa, N. H. Shah, C. L. Gee, E. R. Williams, J. Kuriyan

The paper shows that hub domain assemblies of CaMKII-like proteins in green algae form larger oligomers than metazoan homologs, and that sequence changes can alter assembly stoichiometry.

bioRxiv · Jan 31, 2019Biochemistry