Author

G. M. Benian

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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Cell Biology· 3 Biophysics· 1

Signature Assays, Organisms & Methods

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Organism:C. elegans· 4 Research Focus:cell type annotation· 3 Research Focus:development & morphogenesis· 3 Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Assay:fluorescence / live-cell microscopy· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

H. Qadota· 4 shared A. F. Oberhauser· 2 shared J. C. Moody· 2 shared B. Franke· 1 shared D. Kitzler· 1 shared D. Porto· 1 shared H. Lu· 1 shared J. Hardin· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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4 shared papersCell Biology

H. Qadota

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

FARL-11 (STRIP1/2) is Required for Sarcomere and Sarcoplasmic Reticulum Organization in C. elegans

S. C. T. Martin, H. Qadota, A. F. Oberhauser, J. Hardin, G. M. Benian

This study shows that STRIP1 is essential for sarcoplasmic reticulum and sarcomere organization in C. elegans muscle.

bioRxiv · Mar 5, 2023Cell Biology

The Rho GAP RRC-1 is required for the assembly or stability of integrin adhesion complexes and is a member of the PIX pathway in muscle

J. C. Moody, H. Qadota, G. M. Benian

The paper identifies RRC-1 as a Rho GAP in the PIX pathway required for integrin adhesion complex assembly and stability in C. elegans muscle.

bioRxiv · Jul 2, 2022 · PreprintCell Biology

Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely moving C. elegans

D. Porto, Y. Matsunaga, B. Franke, R. Williams, H. Qadota, O. Mayans, G. M. Benian, H. Lu

This study uses FRET imaging in C. elegans to show stretch-induced conformational changes in twitchin kinase during muscle activity.

bioRxiv · Mar 1, 2021Biophysics

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