Author

G. Stan

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· 5

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:protein folding & dynamics· 5 Approach:mechanistic / dynamical model· 4 Assay:protein structure· 2 Assay:structural biology· 2 Organism:bacteria (other)· 1 Approach:experimental assay· 1 Assay:fluorescence / live-cell microscopy· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Dayananda· 3 shared A. Javidi· 2 shared H. Y. Y. Fonseka· 2 shared M. Damre· 2 shared R. A. Varikoti· 2 shared R. I. Dima· 2 shared C. M. Gonzales· 1 shared C. Micheletti· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 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

3 shared papersBiophysics

A. Dayananda

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Allosteric Communication in the Gating Mechanism for Controlled Protein Degradation by the Bacterial ClpP Peptidase

A. Dayananda, H. T. S. Dennison, H. Y. H. Fonseka, M. S. Avestan, Q. Wang, R. Tehver, G. Stan

This study investigates allosteric communication in the ClpP peptidase gating mechanism by analyzing conformational changes and network rewiring during pore opening.

bioRxiv · Mar 1, 2023Biophysics

Single-molecule FRET probes allosteric effects on protein-translocating pore loops of a AAA+ machine

M. Iljina, H. Mazal, A. Dayananda, Z. Zhang, G. Stan, I. Riven, G. Haran

This study uses single-molecule FRET to show that ATP hydrolysis in ClpB's nucleotide binding domains allosterically controls pore loop dynamics, revealing long-range conformational changes essential for substrate translocation.

bioRxiv · Feb 2, 2023Biophysics

Exploring the effect of mechanical anisotropy of protein structures in the unfoldase mechanism of AAA+ molecular machines

R. A. Varikoti, H. Y. Y. Fonseka, M. S. Kelly, A. Javidi, M. Damre, S. Mullen, J. L. Nugent, C. M. Gonzales, G. Stan, R. I. Dima

This study investigates how mechanical anisotropy in protein structures influences the unfolding mechanisms of AAA+ molecular machines like spastin and ClpY.

bioRxiv · Apr 6, 2022Biophysics

Unfolding and Translocation of Knotted Proteins by Clp Biological Nanomachines: Synergistic Contribution of Primary Sequence and Topology Revealed by Molecular Dynamics Simulations

H. Y. Y. Fonseka, A. Javidi, L. F. L. Oliveira, C. Micheletti, G. Stan

The paper uses molecular dynamics simulations to study how knotted proteins are unfolded by ClpY ATPase, showing that primary sequence and topology both influence translocation.

bioRxiv · Apr 30, 2021Biophysics

Factors Underlying Asymmetric Dynamics of Disaggregase and Microtubule Severing AAA+ Machines

M. Damre, A. Dayananda, R. A. Varikoti, G. Stan, R. I. Dima

This study uses molecular dynamics simulations to analyze the asymmetric dynamics of AAA+ disaggregase and microtubule-severing proteins, revealing differences in inter-protomer coupling and substrate processing mechanisms.

bioRxiv · Nov 25, 2020Biophysics