Author

M. B. Watkins

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Organism:E. coli· 1 Organism:human· 1 Assay:protein structure· 1

Frequent Co-Authors

N. Ando· 2 shared A. A. Burnim· 1 shared B. Bennett· 1 shared E. Antony· 1 shared E. I. Corless· 1 shared H. Wang· 1 shared J. B. Hopkins· 1 shared J. M. Redington· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersBiochemistry

N. Ando

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Author profile →

3 papers

Recent·Most cited

BiophysicsbioRxivJun 1, 2023

The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.

Y. Kyriukha, M. B. Watkins, J. M. Redington…·S. Korolev

This study identifies the PALB2 DNA-binding domain as an intrinsically disordered region that promotes DNA compaction through oligomerization, revealing a novel strand exchange mechanism.

DOI 10.1016/j.isci.2024.111259

humanprotein structure

𝕏 PostBluesky

BiochemistrybioRxivFeb 11, 2023

Conformational switching and flexibility in cobalamin-dependent methionine synthase studied by small-angle X-ray scattering and cryo-electron microscopy

M. B. Watkins, H. Wang, A. A. Burnim, N. Ando

This study uses SAXS and cryo-EM to describe the resting-state conformation of MetH and propose a model for its functional switching.

DOI 10.1073/pnas.2302531120

E. colicryo-EM

𝕏 PostBluesky

BiochemistrybioRxivPreprintNov 12, 2019

The flexible N-terminus of BchL protects its cluster in oxygenic environments and autoinhibits activity

E. I. Corless, S. M. S. Imran, M. B. Watkins…·E. Antony

This paper identifies a mechanism in BchL that protects its [4Fe-4S] cluster and autoinhibits activity, with ATP binding relieving inhibition and enabling complex formation with BchNB.

DOI 10.1101/840439

structural biologyexperimental assay

𝕏 PostBluesky