Author

D. J. Scott

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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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 3 Assay:protein structure· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Assay:proteomics· 1

Frequent Co-Authors

P. R. Gooley· 4 shared F. Yan· 3 shared R. A. D. Bathgate· 3 shared A. Inoue· 2 shared F. Bumbak· 2 shared H. Wu· 2 shared J. C. Paniagua· 2 shared J. J. Ziarek· 2 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiochemistry

P. R. Gooley

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Author profile →

5 papers

Recent·Most cited

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

Structural insights into the modes of relaxin-binding and tethered-agonist activation of RXFP1 and RXFP2

A. Sethi, S. Bruell, T. Ryan, F. Yan, M. H. Tanipour, Y. F. Mok, C. D. Joyce, Y. Khandokar, R. D. Metcalfe, M. D. W. Griffin, D. J. Scott, M. A. Hossain, E. J. Petrie, R. A. D. Bathgate, P. R. Gooley

The paper identifies a conserved motif critical for RXFP1 and RXFP2 activation, showing distinct structural roles in receptor activity.

bioRxiv · Jun 6, 2021Biophysics

α1A-adrenoceptor inverse agonists and agonists modulate receptor signalling through a conformational selection mechanism

P. R. Gooley, F. Wu, L. M. Williams, A. Abdul-Ridha, A. Gunatilaka, T. M. Vaid, M. Kocan, A. R. Whitehead, M. Griffin, R. A. D. Bathgate, D. J. Scott

This study shows how different ligands modulate the conformational states of the α1A-adrenoceptor through a conformational selection mechanism, as revealed by NMR analysis of labeled receptor mutants.

bioRxiv · Dec 7, 2019 · PreprintBiochemistry

Structure-guided enhancement of selectivity of chemical probe inhibitors targeting bacterial seryl-tRNA synthetase

R. Cain, R. Salimaraj, A. S. Punekar, D. Bellini, C. W. G. Fishwisk, L. Czapleski, D. J. Scott, G. Harris, C. G. Dowson, A. J. Lloyd, D. I. Roper

The paper identifies small molecule inhibitors that selectively target bacterial seryl-tRNA synthetases over human homologues using structure-based drug discovery.

bioRxiv · Mar 22, 2019Biochemistry