Author

S. Pyrpassopoulos

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Approach:microscopy & imaging analysis· 2 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Organism:yeast· 1

Frequent Co-Authors

E. M. Ostap· 4 shared A. M. Gicking· 1 shared A. Snoberger· 1 shared B. M. Bensel· 1 shared D. G. Drubin· 1 shared D. Safer· 1 shared H. Shuman· 1 shared M. S. Woody· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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4 shared papersBiophysics

E. M. Ostap

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4 papers

Recent·Most cited

Endocytic myosin-1 is a force-insensitive, power-generating motor

R. T. Pedersen, A. Snoberger, S. Pyrpassopoulos, D. Safer, D. G. Drubin, E. M. Ostap

The paper measures the force-sensitivity of yeast endocytic myosin Myo5 and finds it generates power rather than acting as a force-sensitive anchor during endocytosis.

bioRxiv · Mar 21, 2023 · PreprintCell Biology

KIF1A is kinetically tuned to be a super-engaging motor under hindering loads

S. Pyrpassopoulos, A. M. Gicking, T. M. Zaniewski, W. O. Hancock, E. M. Ostap

This study uses optical tweezers to show KIF1A generates higher force and sustains longer attachment under hindering loads compared to KIF5B, with rapid microtubule reengagement.

bioRxiv · May 16, 2022 · PreprintBiophysics

Strain-Dependent Kinetic Properties of KIF3A and KIF3C Tune the Mechanochemistry of the KIF3AC Heterodimer

B. M. Bensel, M. S. Woody, S. Pyrpassopoulos, Y. E. Goldman, S. P. Gilbert, E. M. Ostap

This study investigates the kinetic properties of KIF3A and KIF3C in KIF3AC heterodimers, showing strain-dependent mechanochemistry and force sensitivity.

Proceedings of the National Academy of Sciences · Jun 22, 2020Peer-reviewedBiophysics

Modulation of kinesin’s load-bearing capacity by force geometry and the microtubule track

S. Pyrpassopoulos, H. Shuman, E. M. Ostap

This study shows that kinesin's attachment duration to microtubules varies significantly based on force geometry, with parallel forces increasing attachment time up to 10-fold compared to vertical forces.

bioRxiv · Aug 21, 2019Biophysics