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 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 4 Research Focus:cell signaling & trafficking· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Organism:E. coli· 1 Organism:human· 1

Frequent Co-Authors

J. B. Hopkins· 2 shared 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. M. Redington· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersMicrobiology

J. B. Hopkins

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A General Mechanism for Initiating the General Stress Response in Bacteria

R. Baral, K. Ho, R. P. Kumar, J. B. Hopkins, M. B. Watkins, S. LaRussa, S. Caban-Penix, L. A. Calderone, N. Bradshaw

The paper identifies a coiled-coil linker mechanism in RsbU that activates the General Stress Response in bacteria by transducing signals from sensor domains.

bioRxiv · Feb 16, 2024Microbiology

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, R. Dastvan, V. N. Uversky, J. B. Hopkins, N. Pozzi, 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.

bioRxiv · Jun 1, 2023Biophysics

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.

bioRxiv · Feb 11, 2023Biochemistry

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, S. Origanti, J. P. Bacik, R. Kitelinger, M. S. Soffe, K. Danyal, L. C. Seefeldt, B. Bennett, N. Ando, 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.

bioRxiv · Nov 12, 2019 · PreprintBiochemistry