Author

M. Gur

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 4 Immunology· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:biophysical modeling· 4 Research Focus:protein folding & dynamics· 4 Research Focus:cell signaling & trafficking· 3 Organism:human· 3 Approach:experimental assay· 2 Assay:protein structure· 2 Assay:structural biology· 2 Assay:cryo-EM· 1

Frequent Co-Authors

M. Golcuk· 8 shared A. Yildiz· 7 shared S. Z. Yilmaz· 3 shared A. P. Carter· 2 shared C. Kilinc· 2 shared E. Taka· 2 shared U. Aktas· 2 shared A. Hacisuleyman· 1 shared

Activity by Year

2020-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

8 shared papersBiophysics

M. Golcuk

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Stepping dynamics of dynein characterized by MINFLUX

J. Slivka, E. Gleave, M. Golcuk, D. P. Wijewardena, J. T. Canty, P. R. Selvin, M. Gur, A. P. Carter, A. Yildiz

This study uses MINFLUX to track yeast dynein stepping dynamics at high resolution, revealing ATP hydrolysis per step and 8 nm steps with transient plus-end movements.

bioRxiv · Jul 16, 2024 · PreprintBiophysics

A force-sensitive mutation reveals a spindle assembly checkpoint-independent role for dynein in anaphase progression

D. Salvador-Garcia, L. Jin, A. Hensley, M. Golcuk, E. Gallaud, S. Chaaban, F. Port, A. Vagnoni, V. J. Planelles-Herrero, M. A. McClintock, E. Derivery, A. P. Carter, R. Giet, M. Gur, A. Yildiz, S. L. Bullock

This study identifies a mutation in dynein that causes mitotic spindle arrest independent of the spindle assembly checkpoint, revealing a load-dependent role in anaphase progression.

bioRxiv · Aug 3, 2023 · PreprintCell Biology

The Mechanism and Energetics of the Dynein Priming Stroke

M. Golcuk, S. Z. Yilmaz, A. Yildiz, M. Gur

This study uses molecular dynamics simulations to analyze the conformational changes and energy dynamics of the dynein linker during the power stroke.

bioRxiv · Jun 10, 2023Biophysics

Omicron BA.1 and BA.2 Variants Increase the Interactions of SARS-CoV-2 Spike Glycoprotein with ACE2

M. Golcuk, A. Yildiz, M. Gur

This study uses molecular dynamics simulations to show that Omicron BA.1 and BA.2 variants have stronger RBD-ACE2 binding due to increased salt bridges and hydrophobic interactions.

bioRxiv · Dec 6, 2021Immunology

Binding mechanism of neutralizing Nanobodies targeting SARS-CoV-2 Spike Glycoprotein

M. Golcuk, A. Hacisuleyman, B. Erman, A. Yildiz, M. Gur

This study uses molecular dynamics simulations to analyze how three nanobodies bind to SARS-CoV-2 Spike RBD and affect ACE2 binding, revealing differences in their neutralizing mechanisms against variants.

bioRxiv · Apr 23, 2021Immunology

The mechanism of motor inhibition by microtubule-associated proteins

L. S. Ferro, L. Eshun-Wilson, M. Golcuk, J. Fernandes, T. Huijben, E. Gerber, A. Jack, K. Costa, M. Gur, Q. Feng, E. Nogales, A. Yildiz

This study investigates how microtubule-associated proteins (MAPs) regulate motor protein interactions, finding that MAPs inhibit motors without blocking their binding sites and that motors must interact with MAPs to move on MAP-coated microtubules.

bioRxiv · Oct 22, 2020 · PreprintBiophysics

Critical Interactions Between the SARS-CoV-2 Spike Glycoprotein and the Human ACE2 Receptor

E. Taka, S. Z. Yilmaz, M. Golcuk, C. Kilinc, U. Aktas, A. Yildiz, M. Gur

This study identifies key interactions between SARS-CoV-2 spike protein and ACE2 receptor using MD simulations and suggests targeting hydrophobic residues for therapeutic strategies.

bioRxiv · Sep 21, 2020Immunology

Exploring Conformational Transition of 2019 Novel Coronavirus Spike Glycoprotein Between Its Closed and Open States Using Molecular Dynamics Simulations

M. Gur, E. Taka, S. Z. Yilmaz, C. Kilinc, U. Aktas, M. Golcuk

This study uses molecular dynamics simulations to explore the conformational transitions of the SARS-CoV-2 spike glycoprotein between closed and open states, identifying key structural changes and energy pathways.

bioRxiv · Apr 17, 2020Biophysics