Author

M. M. Morck

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· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Research Focus:differential expression· 1 Research Focus:host-pathogen & immune response· 1 Assay:imaging· 1 Assay:proteomics· 1

Frequent Co-Authors

J. A. Spudich· 2 shared K. M. Ruppel· 2 shared A. Dawood· 1 shared A. Jhingran· 1 shared A. S. Adhikari· 1 shared A. S. Vander Roest· 1 shared B. Pruitt· 1 shared C. Liu· 1 shared

Activity by Year

2019-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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2 shared papersBiophysics

J. A. Spudich

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2 papers

Recent·Most cited

Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super-relaxed state: multiscale measurements and computational modeling

A. S. Vander Roest, C. Liu, M. M. Morck, K. B. Kooiker, G. Jung, D. Song, A. Dawood, A. Jhingran, G. Pardon, S. Ranjbarvaziri, G. Fajardo, M. Zhao, K. S. Campbell, B. Pruitt, J. A. Spudich, , D. Bernstein

This study investigates the P710R mutation in β-cardiac myosin, showing it causes hypercontractility by disrupting the super-relaxed state, using multiscale experiments and modeling.

bioRxiv · Nov 10, 2020 · PreprintBiophysics

The molecular basis of hypercontractility caused by the hypertrophic cardiomyopathy mutations R403Q and R663H

S. S. Sarkar, D. V. Trivedi, M. M. Morck, A. S. Adhikari, S. N. Pasha, K. M. Ruppel, J. A. Spudich

This study investigates how HCM mutations R403Q and R663H in myosin cause hypercontractility by increasing functionally-accessible myosin heads and affecting MyBP-C binding.

bioRxiv · Feb 7, 2019 · PreprintBiochemistry