Feixia Chu, Ph.D.
Affiliations: | 2004 | University of California, San Francisco, San Francisco, CA |
Area:
Pharmaceutical Chemistry, Biochemistry, Analytical ChemistryGoogle:
"Feixia Chu"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Alma L. Burlingame | grad student | 2004 | UCSF | |
| (Defining protein -protein interaction surfaces: A chemical and mass spectrometric approach.) | ||||
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Publications
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| Chiosis G, McNutt S, Roychowdhury T, et al. (2024) Phosphorylation-Driven Epichaperome Assembly: A Critical Regulator of Cellular Adaptability and Proliferation. Research Square |
| Gupta R, Liu Y, Wang H, et al. (2020) Structural Analysis of the Regulatory GAF Domains of cGMP Phosphodiesterase Elucidates the Allosteric Communication Pathway. Journal of Molecular Biology |
| Irwin MJ, Gupta R, Gao XZ, et al. (2019) The molecular architecture of photoreceptor phosphodiesterase 6 (PDE6) with activated G protein elucidates the mechanism of visual excitation. The Journal of Biological Chemistry |
| Chu F, Hogan D, Gupta R, et al. (2019) Allosteric Regulation of Rod Photoreceptor Phosphodiesterase 6 (PDE6) Elucidated by Chemical Cross-Linking and Quantitative Mass Spectrometry. Journal of Molecular Biology |
| Chu F, Thornton DT, Nguyen HT. (2018) Chemical cross-linking in the structural analysis of protein assemblies. Methods (San Diego, Calif.) |
| Karagöz GE, Acosta-Alvear D, Nguyen HT, et al. (2017) An unfolded protein-induced conformational switch activates mammalian IRE1. Elife. 6 |
| Ee LS, McCannell KN, Tang Y, et al. (2017) An Embryonic Stem Cell-Specific NuRD Complex Functions through Interaction with WDR5. Stem Cell Reports |
| Rodina A, Wang T, Yan P, et al. (2016) The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature |
| Zeng-Elmore X, Gao XZ, Pellarin R, et al. (2014) Molecular architecture of photoreceptor phosphodiesterase elucidated by chemical cross-linking and integrative modeling. Journal of Molecular Biology. 426: 3713-28 |
| Street TO, Zeng X, Pellarin R, et al. (2014) Elucidating the mechanism of substrate recognition by the bacterial Hsp90 molecular chaperone. Journal of Molecular Biology. 426: 2393-404 |