Author

L. Lesanpezeshki

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Cell Biology· 2 Physiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:C. elegans· 3 Approach:experimental assay· 3 Research Focus:development & morphogenesis· 2 Research Focus:cell type annotation· 1 Assay:imaging· 1

Frequent Co-Authors

S. A. Vanapalli· 3 shared H. Qadota· 2 shared A. F. Oberhauser· 1 shared C. M. Lacerda· 1 shared C. V. Yingling· 1 shared D. Kitzler· 1 shared D. Pruyne· 1 shared G. Benian· 1 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersCell Biology

S. A. Vanapalli

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

FHOD-1/profilin-mediated actin assembly protects sarcomeres against contraction-induced deformation in C. elegans

M. J. Kimmich, S. Sundaramurthy, M. A. Geary, L. Lesanpezeshki, C. V. Yingling, S. A. Vanapalli, R. S. Littlefield, D. Pruyne

This study shows FHOD-1 and profilin cooperate to stabilize sarcomere Z-lines in C. elegans by promoting actin assembly and preventing muscle deformation during contraction.

bioRxiv · Feb 29, 2024 · PreprintCell Biology

Investigating the correlation of muscle function tests and sarcomere organization in C. elegans

L. Lesanpezeshki, H. Qadota, M. Norouzi Darabad, K. Kashyap, C. M. Lacerda, N. J. Szewczyk, G. Benian, S. A. Vanapalli

This study investigates the relationship between muscle function and sarcomere organization in C. elegans using two assays, finding that mutants with sarcomere defects show reduced muscle strength and that combined assays improve phenotyping.

bioRxiv · Apr 13, 2021Physiology

A Region of UNC-89 (obscurin) Lying Between Two Protein Kinase Domains is a Highly Elastic Spring Required for Proper Sarcomere Assembly

H. Qadota, J. C. Moody, L. Lesanpezeshki, T. Moncrief, D. Kitzler, P. D. Bhat, S. A. Vanapalli, A. F. Oberhauser, G. M. Benian

This paper identifies a highly elastic interkinase region in UNC-89 essential for sarcomere assembly, showing that its deletion causes sarcomere disorganization and locomotion defects in C. elegans.

bioRxiv · Apr 3, 2020Cell Biology