Author

L. Gakhar

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 Biophysics· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:chromatin & epigenetic regulation· 2 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Approach:microscopy & imaging analysis· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1

Frequent Co-Authors

N. J. Schnicker· 5 shared D. Dey· 2 shared S. S. Hasan· 2 shared S. Singh· 2 shared A. Stanfield· 1 shared A. Y. Minard· 1 shared B. D. Freudenthal· 1 shared B. Doray· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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5 shared papersBiophysics

N. J. Schnicker

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Author profile →

6 papers

Recent·Most cited

Conformational landscape of soluble α-klotho revealed by cryogenic electron microscopy

N. J. Schnicker, Z. Xu, M. Amir, L. Gakhar, C.-L. Huang

This study reveals the conformational landscape of soluble α-klotho using cryo-EM, showing flexibility and multiple forms that support its FGFR-independent functions.

bioRxiv · Mar 2, 2024 · PreprintBiophysics

A double-ring of human RAD52 remodels replication forks restricting fork reversal

M. Honda, M. Razzaghi, P. Gaur, E. Malacaria, G. Marozzi, L. Di Biagi, F. A. Aiello, E. A. Paintsil, A. Stanfield, B. J. Deppe, L. Gakhar, N. J. Schnicker, M. A. Spies, P. Pichierri, M. Spies

The paper shows human RAD52 forms a double-ring structure around stalled replication forks, remodeling them via DNA strand exchange to prevent reversal by SMARCAL1.

bioRxiv · Nov 14, 2023 · PreprintBiochemistry

A single C-terminal residue controls SARS-CoV-2 spike trafficking and virion assembly

D. Dey, E. Qing, Y. He, Y. Chen, B. Jennings, W. Cohn, S. Singh, L. Gakhar, N. J. Schnicker, B. G. Pierce, J. P. Whitelegge, B. Doray, J. P. Orban, T. Gallagher, S. S. Hasan

This study identifies a C-terminal residue critical for SARS-CoV-2 spike protein trafficking and virion assembly, offering insights for vaccine design.

bioRxiv · Mar 9, 2023 · PreprintBiophysics

Structural basis for APE1 processing DNA damage in the nucleosome

T. M. Weaver, N. M. Hoitsma, J. J. Spencer, L. Gakhar, N. J. Schnicker, B. D. Freudenthal

This study reveals how APE1 processes DNA damage in nucleosomes by bending DNA to access AP sites, with efficiency depending on site exposure.

bioRxiv · Mar 9, 2022Biochemistry

ANTH domains within CALM, HIP1R, and Sla2 recognize ubiquitin internalization signals.

N. Pashkova, L. Gakhar, S. Winistorfer, A. Y. Minard, N. J. Schnicker, L. Yu, I. E. Johnson, R. C. Piper

The paper identifies ANTH domains in CALM, HIP1R, and Sla2 that bind ubiquitin, contributing to clathrin-mediated endocytosis of ubiquitinated membrane proteins.

eLife · Nov 25, 2021Peer-reviewedCell Biology

An Extended Motif in the SARS-CoV-2 Spike Modulates Binding and Release of Host Coatomer in Retrograde Trafficking

D. Dey, S. Singh, S. Khan, M. Martin, N. Schnicker, L. Gakhar, B. Pierce, S. S. Hasan

The paper identifies an extended COPI binding motif in the SARS-CoV-2 spike protein that modulates its interaction with COPI subunits and is critical for retrograde trafficking.

bioRxiv · Sep 3, 2021Biochemistry