Author

A. M. Gicking

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· 4 Cell Biology· 3

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Research Focus:cell signaling & trafficking· 5 Approach:microscopy & imaging analysis· 4 Approach:experimental assay· 3 Assay:fluorescence / live-cell microscopy· 2 Research Focus:protein folding & dynamics· 2 Organism:Arabidopsis· 1 Research Focus:cell type annotation· 1 Research Focus:clustering· 1

Frequent Co-Authors

W. O. Hancock· 6 shared Q. Feng· 3 shared L. Guo· 2 shared P. Wang· 2 shared T. M. Zaniewski· 2 shared T.-C. Ma· 2 shared W. Qiu· 2 shared B. Liu· 1 shared

Activity by Year

2017-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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6 shared papersBiophysics

W. O. Hancock

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Author profile →

7 papers

Recent·Most cited

Simulations suggest robust microtubule attachment of kinesin and dynein in antagonistic pairs

T.-C. Ma, A. M. Gicking, Q. Feng, W. O. Hancock

The paper uses simulations to study kinesin and dynein motor dynamics in bidirectional transport, finding that matched stall forces and independent detachment rates best replicate experimental velocity distributions.

bioRxiv · Aug 9, 2022Biophysics

Kinesin-1, -2 and -3 motors use family-specific mechanochemical strategies to effectively compete with dynein during bidirectional transport

A. M. Gicking, T.-C. Ma, Q. Feng, R. Jiang, S. Badieyan, M. A. Cianfrocco, W. O. Hancock

The paper investigates how kinesin-1, -2, and -3 motors compete with dynein during bidirectional transport and finds that all three families can withstand hindering loads through distinct kinetic strategies.

bioRxiv · Aug 4, 2022Cell 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

The fast and superprocessive KIF1A predominately resides in a vulnerable one-head-bound state during its chemomechanical cycle

T. M. Zaniewski, A. M. Gicking, J. Fricks, W. O. Hancock

This study elucidates the chemomechanical cycle of KIF1A, revealing that it predominantly resides in a one-head-bound state during its cycle, with fast rear head detachment and tethered head attachment as key rate-limiting steps.

bioRxiv · Jun 28, 2020Cell Biology

Dynactin p150 promotes processive motility of DDB complexes by minimizing diffusional behavior of dynein

Q. Feng, A. M. Gicking, W. O. Hancock

The paper uses iSCAT microscopy to analyze dynein-dynactin-BicD2 motility, finding that p150 reduces diffusive behavior and enhances processive movement.

bioRxiv · Sep 10, 2019Cell Biology

The Orphan Kinesin PAKRP2 Achieves Processive Motility Via Noncanonical Stepping

A. M. Gicking, P. Wang, C. Liu, K. J. Mickolajczyk, L. Guo, W. O. Hancock, W. Qiu

This study shows that PAKRP2, an orphan kinesin in Arabidopsis, moves processively along microtubules using a noncanonical stepping mechanism with small steps and lateral movements.

bioRxiv · Sep 29, 2018Biophysics

The preprophase band-associated kinesin-14 OsKCH2 is a processive minus-end-directed microtubule motor

K.-F. Tseng, P. Wang, Y.-R. J. Lee, J. Bowen, A. M. Gicking, L. Guo, B. Liu, W. Qiu

This study identifies OsKCH2 as a processive minus-end-directed kinesin-14 in plants, compensating for the absence of cytoplasmic dynein.

bioRxiv · Dec 11, 2017Biophysics