Author

C. Harms

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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Biophysics· 3 Physiology· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 3 Approach:experimental assay· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Assay:fluorescence / live-cell microscopy· 1 Organism:human· 1 Assay:imaging· 1

Frequent Co-Authors

D. Wright· 3 shared J. Klein-Seetharaman· 3 shared L. Kumar· 3 shared S. K. SARKAR· 3 shared A. Nash· 2 shared S. Kamboj· 2 shared A. V. P. Vinje· 1 shared D. Houser· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersBiophysics

D. Wright

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Capture and Release of Minke Whales Offers New Research Opportunities Including Measurements of Mysticete Hearing

L. Kleivane, P. H. Kvadsheim, A. V. P. Vinje, J. Mulsow, R. A. Olberg, J. Teilmann, C. Harms, D. Houser

The paper describes a catch-and-release method to safely handle minke whales for hearing measurements and other research, with successful initial hearing tests and normal post-release behavior.

bioRxiv · Feb 2, 2024Physiology

Quantification of allosteric communications in matrix metalloprotease-1 on alpha-synuclein aggregates and substrate-dependent virtual screening

S. Kamboj, C. Harms, D. Wright, A. Nash, L. Kumar, J. Klein-Seetharaman, S. K. SARKAR

This paper quantifies allosteric communications in MMP1 on alpha-synuclein aggregates using FRET and virtual screening, showing substrate-dependent changes in ligand-binding sites.

bioRxiv · Jan 11, 2021 · PreprintBiophysics

Inter-domain dynamics and fibrinolytic activity of matrix metalloprotease-1

L. Kumar, J. Planas-Iglesias, C. Harms, S. Kamboj, D. Wright, J. Klein-Seetharaman, S. K. Sarkar

This study investigates how inter-domain dynamics of MMP1 correlate with its fibrinolytic activity using single-molecule FRET and kinetic modeling.

bioRxiv · Jul 6, 2020Biophysics

Allosteric communications between domains modulate activity of matrix metalloprotease-1

L. Kumar, A. Nash, C. Harms, J. Planas, D. Wright, J. Klein-Seetharaman, S. K. Sarkar

This paper identifies functionally relevant inter-domain dynamics in MMP1 on collagen fibrils, showing that open conformations correlate with activity and can be modulated by mutations and ligands.

Biophysical Journal · Jul 1, 2020Peer-reviewedBiophysics