21. Nguyen,
H. N.; Huynh, U.; Zastrow, M.
L.* Fluorescent protein-based Zn2+
sensors reveal distinct responses of
aerobic and anaerobic Escherichia coli
cultures to excess Zn2+.
J. Biol. Chem. 2024,
in press. [link]
20. Jensen, G. C.; Janis, M. K.; Nguyen, H. N.; David, O. W.; Zastrow, M. L.* Perspective: Fluorescent protein-based sensors for detecting essential metal ions across the tree of life. ACS Sens. 2024, 9, 1622-1643. [link]
19. Jensen,
G. C.; Janis, M. K.; Jara, J.; Abbasi, N.;
Zastrow, M. L.*
Zinc-Induced Fluorescence Turn-On in Native and Mutant
Phycoerythrobilin-Binding Orange Fluorescent Proteins.
bioRxiv preprint [link]. Biochemistry 2023,
62, 2828-2840. [link]
18. Janis, M. K.†; Zou, W.†; Zastrow, M. L.* A Single Site Mutation Tunes Fluorescence and Chromophorylation of an Orange Fluorescent Cyanobacteriochrome. bioRxiv preprint [link]. ChemBioChem 2023, 24, e2023003. [link]
17. Huynh, U.; Nguyen, H. N.; Trinh, B. K.; Elhaj, J.;
Zastrow, M. L.* A bioinformatic analysis of zinc
transporters in intestinal Lactobacillaceae.
Metallomics 2023, 15,
mfad044. [link]
16. Huynh, U. & Zastrow, M. L.* Metallobiology of
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15. Zou, W.; Nguyen, H. N.; Zastrow, M. L.* Mutant Flavin-Based Fluorescent Protein Sensors for Detecting Intracellular Zinc and Copper in Escherichia coli. ACS Sens. 2022, 7, 3369-3378. [link]
14. Zhao, H. & Zastrow, M. L.* Transition Metals Induce Quenching of Monomeric Near-Infrared Fluorescent Proteins. Biochemistry 2022, 61, 494-504. [link]
13. Huynh, U.; Qiao, M.; King, J.; Trinh, B.; Valdez, J.; Haq, M.; Zastrow, M. L.* Differential Effects of Transition Metals on Growth and Metal Uptake for Two Distinct Lactobacillus Species. Microbiol. Spectr. 2022, 10, e01006-21. [link]
12. Zou, W.; Le, K.; Zastrow, M. L.* Live Cell Copper-Induced Fluorescence Quenching of the Flavin-Binding Fluorescent Protein CreiLOV. ChemBioChem 2020, 21, 1356-1363. [link]
11. Borghesani, V.; Zastrow, M.L.; Tolbert, A. E.; Deb, A.; Penner-Hahn, J. E.; Pecoraro, V. L.* Co(II) Substitution Enhances the Esterase Activity of a de Novo Designed Zn(II) Carbonic Anhydrase. Chem. Eur. J. 2024, e202304367. [link]
10. Zastrow, M. L.†; Huang, Z. H.†; Lippard, S. J.* HaloTag-Based Hybrid Targetable and Ratiometric Sensors for Intracellular Zinc. ACS Chem. Biol. 2020, 15, 396-406. [link]
9. Ruckthong, L.; Zastrow, M. L.; Stuckey, J. A.*; Pecoraro, V. L.* A Crystallographic Examination of Predisposition Versus Preorganization in de Novo Designed Metalloproteins. J. Am. Chem. Soc. 2016, 138, 11979-11988. [link]
8. Zastrow, M. L.†; Radford, R. J.†; Chyan, W.; Anderson, C. T.; Zhang, D. Y.; Loas, A.; Tzounopoulos, T.; Lippard, S. J.* Reaction-Based Probes for Imaging Mobile Zinc in Live Cells and Tissues. ACS Sens. 2016, 1, 32-39. †Co-first authors. [link]
7. Anderson, C. T.; Radford, R. J.; Zastrow, M. L.; Zhang, D. Y.; Apfel, U.-P.; Lippard, S. J.*; Tzounopoulos, T.* Modulation of extrasynaptic NMDA receptors by synaptic and tonic zinc. Proc. Natl. Acad. Sci. U.S.A. 2015, 112, E2705-E2714. [link]
6. Rivera-Fuentes, P.; Wrobel, A.; Zastrow, M. L.; Khan, M.; Georgiou, J.; Luyben, T. T.; Roder, J. C.; Okamoto, K.; Lippard, S. J.* A far-red emitting probe for unambiguous detection of mobile zinc in acidic vesicles and deep tissue. Chem. Sci. 2015, 6, 1944-1948. [link]
5. Yu, F.; Cangelosi, V. M.; Zastrow, M. L.; Tegoni, M.; Plegaria, J. S.; Tebo, A. G.; Mocny, C. S.; Ruckthong, L.; Qayyum, H.; Pecoraro, V. L.* Protein Design: Toward Functional Metalloenzymes. Chem. Rev. 2014, 114, 3495-3578. [link]
4. Zastrow, M. L. & Pecoraro, V. L.* Designing Hydrolytic Zinc Metalloenzymes. Biochemistry 2014, 53, 957-978. [link]
3. Zastrow, M. L. & Pecoraro, V. L.* Designing functional metalloproteins: from structural to catalytic metal sites. Coord. Chem. Rev. 2013, 257, 2565-2588. [link]
2. Zastrow, M. L. & Pecoraro, V. L.* Influence of Active Site Location on Catalytic Activity in de Novo-Designed Zinc Metalloenzymes. J. Am. Chem. Soc. 2013, 135, 5895-5903. [link]
1. Zastrow, M. L.; Peacock, A. F. A.; Stuckey, J. A.; Pecoraro, V. L.* Hydrolytic catalysis and structural stabilization in a designed metalloprotein. Nature Chem. 2012, 4, 118-123. [link]
