Author

G. A. Bezerra

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Oberholzer· 1 shared A. Thompson· 1 shared B. Dimitrov· 1 shared B. G. Davis· 1 shared D. Mamalis· 1 shared D. S. Froese· 1 shared E. MacLean· 1 shared E. Rembeza· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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1 shared paperBiochemistry

A. Oberholzer

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3 papers

Recent·Most cited

Gluebodies improve crystal reliability and diversity through transferable nanobody mutations that introduce constitutive close contacts

M. Ye, M. Makola, J. Newman, M. Fairhead, E. MacLean, N. D. Wright, L. Koekemoer, A. Thompson, G. A. Bezerra, G. Yi, H. Li, V. L. Rangel, D. Mamalis, H. Aitkenhead, B. G. Davis, , F. von Delft

The paper engineers nanobody interfaces to improve crystal reliability and diversity, resulting in better diffraction and multiple polymorphs.

bioRxiv · Jul 26, 2022 · PreprintBiochemistry

Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism

G. A. Bezerra, W. R. Foster, H. J. Bailey, K. G. Hicks, S. W. Sauer, B. Dimitrov, J. G. Okun, J. Rutter, S. Koelker, W. W. Yue

This study presents the crystal structure of human DHTKD1 and a 3D reconstruction of the DLST inner core, revealing structural insights into lysine catabolism and potential drug targets.

bioRxiv · Jan 20, 2020Biochemistry

Structural basis of human 5,10-methylenetetrahydrofolate reductase (MTHFR) regulation by phosphorylation and S-adenosylmethionine inhibition

D. S. Froese, J. Kopec, E. Rembeza, G. A. Bezerra, A. Oberholzer, T. Suormala, S. Lutz, R. Chalk, O. Borkowska, M. Baumgartner, W. Yue

This study presents the 2.5 Å resolution crystal structure of human MTHFR, revealing its architecture and how phosphorylation and SAM binding regulate its activity.

bioRxiv · Feb 26, 2018Biochemistry