Author

J. J. Ziarek

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· 5 Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:protein folding & dynamics· 5 Organism:human· 2 Assay:protein structure· 2 Assay:proteomics· 2 Approach:statistical model· 2 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

S. A. Robson· 6 shared A. Inoue· 3 shared F. Bumbak· 3 shared H. Wu· 3 shared C. Dag· 2 shared D. J. Scott· 2 shared F. Yan· 2 shared J. C. Paniagua· 2 shared

Activity by Year

2019-2025 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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6 shared papersBiophysics

S. A. Robson

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Author profile →

9 papers

Recent·Most cited

Chemically induced partial unfolding of the multifunctional Apurinic/apyrimidinic endonuclease 1

R. Rai, O. Dawodu, J. Meng, S. M. Johnson, J. Z. Vilseck, M. R. Kelley, J. J. Ziarek, M. M. Georgiadis

This study investigates how the redox inhibitor APX3330 induces reversible partial unfolding of APE1, revealing structural changes relevant to its redox function.

Protein Science · May 15, 2025Peer-reviewedBiochemistry

Insights on the GPCR helix 8 solution structure and orientation using a neurotensin receptor 1 peptide

J. B. Bower, S. A. Robson, J. J. Ziarek

This study investigates the structural stability and orientation of the neurotensin receptor 1 H8-Ctail using NMR in detergent and lipid environments, revealing its sensitivity to membrane conditions.

bioRxiv · Jan 31, 2024 · PreprintBiophysics

Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study

K. Kahraman, S. A. Robson, O. Gocenler, C. M. Yenici, C. D. Tozkoparan, J. M. Klein, V. Dötsch, E. S. Elgin, A. L. Haas, J. J. Ziarek, C. Dag

This study uses SAXS and NMR to show UbcH8 exists in a concentration-dependent monomer-dimer equilibrium with dimerization affecting E1 and E3 interfaces.

bioRxiv · Apr 13, 2023Biochemistry

The dynamic nature of neurotensin receptor 1 (NTS1) allostery and signaling bias

F. Bumbak, A. Inoue, M. Pons, J. C. Paniagua, F. Yan, H. Wu, S. A. ROBSON, R. A. D. Bathgate, D. J. Scott, P. R. Gooley, J. J. Ziarek

This study investigates NTS1 allostery and signaling bias using NMR, showing PIP2 enhances transducer complexation through allosteric connections and β-arrestin modulates receptor conformation.

bioRxiv · Nov 25, 2022Biochemistry

Ligands tune the local and global motions of neurotensin receptor 1 (NTS1): a DFT-guided solution NMR analysis

F. Bumbak, M. Pons, A. Inoue, J. C. Paniagua, F. Yan, H. Wu, S. A. ROBSON, R. Bathgate, D. J. Scott, P. R. Gooley, J. J. Ziarek

This study uses NMR and DFT to analyze sub-nanosecond motions of NTS1, showing ligands affect conformational entropy and dynamics.

bioRxiv · Aug 9, 2022Biophysics

A Method for Selective 19F-Labeling Absent of Probe Sequestration (SLAPS)

A. Dixon, J. Trinidad, J. J. Ziarek

The paper introduces a method to prevent offsite 19F-labeling by detergent micelles, improving NMR spectral quality for membrane protein studies.

bioRxiv · Jun 17, 2022Biophysics

The Effect of Ligands and Transducers on the Neurotensin Recep-tor 1 (NTS1) Conformational Ensemble

A. D. Dixon, A. Inoue, S. A. ROBSON, K. Culhane, J. Trinidad, S. Sivaramakrishnan, F. Bumbak, J. J. Ziarek

This study uses 19F-NMR to show ligands and transducers modulate NTS1 conformational substates, revealing dynamic behavior not captured by static structures.

bioRxiv · Dec 8, 2021Biophysics

TRACT revisited: an algebraic solution for determining overall rotational correlation times from cross-correlated relaxation rates

S. A. ROBSON, C. Dag, H. Wu, J. J. Ziarek

The paper develops algebraic solutions to improve the accuracy of rotational correlation time estimation using TRACT experiments by addressing limitations in existing methods.

bioRxiv · Jan 16, 2021Biophysics

Molecular Basis for the Evolved Instability of a Human G-Protein Coupled Receptor

L. M. Chamness, N. B. Zelt, C. P. Kuntz, B. J. Bender, W. D. Penn, J. J. Ziarek, J. P. Meiler, J. P. Schlebach

The paper identifies a C-terminal truncation and increased TM domain polarity in GnRHR as evolutionary adaptations that reduce receptor stability and activity.

bioRxiv · Dec 20, 2019Biochemistry