Author

P. J. Loll

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

J. Beld· 3 shared K. C. Grasty· 3 shared E. J. D'Lauro· 2 shared P. Rotsides· 2 shared C. Guzik· 1 shared L. J. Maciunas· 1 shared M. V. Rao· 1 shared N. Webber· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersBiochemistry

J. Beld

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Author profile →

4 papers

Recent·Most cited

The VanS sensor histidine kinase from type-B VRE recognizes vancomycin directly

L. J. Maciunas, P. Rotsides, E. J. D'Lauro, S. Brady, J. Beld, P. J. Loll

This study shows that type-B VanS from VRE directly interacts with vancomycin, activating its autokinase activity and confirming a direct sensing mechanism for VanS.

bioRxiv · Jul 9, 2023 · PreprintBiochemistry

Novel Diazirine Photoprobes for the Identification of Vancomycin-Binding Proteins

P. Rotsides, P. J. Lee, N. Webber, K. C. Grasty, J. Beld, P. J. Loll

This paper develops diazirine-based vancomycin photoprobes with improved specificity and fewer chemical modifications for identifying vancomycin-binding proteins.

bioRxiv · Jun 15, 2023Biochemistry

Structure of VanS from Vancomycin-Resistant Enterococci: A Sensor Kinase with Weak ATP Binding

K. C. Grasty, C. Guzik, E. J. D'Lauro, S. B. Padrick, J. Beld, P. J. Loll

The paper presents X-ray structures of VanS CA domains from VRE types A and C, revealing weak ATP binding with low millimolar KD values, suggesting a regulatory mechanism for resistance gene expression.

bioRxiv · Dec 12, 2022Biochemistry

Ubiquitin Substrates Dramatically Increase Ataxin3 Deubiquitinating Activity: Allosteric crosstalk connects three distinct sites

M. V. Rao, K. C. Grasty, P. D. Mehetre, P. J. Loll

This study shows that ubiquitin conjugates significantly enhance ataxin3 deubiquitinating activity through allosteric interactions involving three distinct sites on the enzyme.

bioRxiv · May 5, 2020 · PreprintBiochemistry