Author

A. F. Oberhauser

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 Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Research Focus:development & morphogenesis· 2 Assay:proteomics· 2

Frequent Co-Authors

H. Qadota· 4 shared G. Benian· 2 shared G. M. Benian· 2 shared T. Moncrief· 2 shared A. O. Bailey· 1 shared C. J. Christian· 1 shared C. J. Matheny· 1 shared D. Kitzler· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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4 shared papersCell Biology

H. Qadota

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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

UNC-45 has a crucial role in maintaining muscle sarcomeres during aging in C. elegans

C. J. Matheny, H. Qadota, M. Kimelman, A. O. Bailey, A. F. Oberhauser, G. Benian

This study shows that UNC-45 is essential for maintaining muscle sarcomeres in C. elegans during aging, with its loss leading to sarcopenia through myosin degradation.

bioRxiv · Jun 4, 2022 · PreprintCell Biology

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

Mutational analysis of the structure and function of the chaperone domain of UNC-45B

I. Gaziova, T. Moncrief, C. J. Christian, M. A. White, M. A. Villarreal, S. Powell, H. Qadota, G. Benian, A. F. Oberhauser

This paper investigates the chaperone function of UNC-45B's UCS domain by engineering mutations and analyzing their effects on structure, stability, and sarcomere organization in C. elegans and human cataract.

bioRxiv · Jan 3, 2020Biophysics