Author

J. J. Loparo

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 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:chromatin & epigenetic regulation· 4 Organism:bacteria (other)· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Assay:DNA methylation· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

A. T. Moreno· 2 shared E. S. Thrall· 2 shared S. Chang· 2 shared A. A. Drabek· 1 shared A. C. Kruse· 1 shared A. S. Baier· 1 shared C. L. Peterson· 1 shared E. Fivenson· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 8 mutual co-author links

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2 shared papersBiochemistry

A. T. Moreno

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Author profile →

6 papers

Recent·Most cited

Allosteric activation of cell wall synthesis during bacterial growth

I. Shlosman, E. Fivenson, M. Gilman, T. Sisley, S. Walker, T. G. Bernhardt, A. C. Kruse, J. J. Loparo

This study identifies a dynamic structural mechanism in a bacterial cell wall synthase that couples polymerization and crosslinking during cell elongation.

bioRxiv · Nov 7, 2022Biophysics

H2A.Z deposition by SWR1C involves multiple ATP-dependent steps

J. Fan, A. T. Moreno, A. S. Baier, J. J. Loparo, C. L. Peterson

This study identifies three ATP-dependent phases in H2A.Z deposition by SWR1C using single-molecule and ensemble methods, revealing a priming step and ATP concentration-dependent release of H2A/H2B.

bioRxiv · Jan 11, 2022Biochemistry

XLF acts as a flexible connector during non-homologous end joining

S. M. Carney, A. T. Moreno, S. C. Piatt, M. Cisneros-Aguirre, F. W. Lopezcolorado, J. M. Stark, J. J. Loparo

This study shows that the C-terminal tail of XLF is essential for DNA end alignment during NHEJ, with a minimal length required for efficient end joining.

bioRxiv · Jul 29, 2020Biochemistry

Compartmentalization of the replication fork by single-stranded DNA binding protein regulates translesion synthesis

S. Chang, E. S. Thrall, L. Laureti, V. Pages, J. J. Loparo

The paper shows that SSB remodeling at stalled replication forks enables Pol IV localization, which is essential for TLS on both strands by overcoming the gatekeeping role of the Pol III epsilon subunit.

bioRxiv · Mar 3, 2020Biochemistry

A gatekeeping function of the replicative polymerase controls pathway choice in the resolution of lesion-stalled replisomes

S. Chang, K. Naiman, E. S. Thrall, J. E. Kath, S. Jergic, N. Dixon, R. P. Fuchs, J. J. Loparo

This study shows how the replicative polymerase's proofreading subunit controls lesion resolution pathways in bacteria by restricting access to TLS polymerases.

bioRxiv · Jun 21, 2019Biochemistry

A flow extension tethered particle motion assay for single-molecule proteolysis

A. A. Drabek, J. J. Loparo, S. C. Blacklow

This paper introduces a flow extension tethered particle motion assay to study single-molecule proteolysis, enabling accurate assessment of protease activity by excluding multiply-tethered beads.

bioRxiv · Jan 23, 2019Biophysics