Author

S. Newstead

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· 6 Biochemistry· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 4 Assay:structural biology· 4 Research Focus:protein folding & dynamics· 3 Research Focus:protein structure prediction· 3 Approach:statistical model· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:drug response / drug discovery· 2

Frequent Co-Authors

J. L. Parker· 3 shared Z. Wu· 3 shared M. Schewe· 2 shared P. Biggin· 2 shared P. C. Biggin· 2 shared P. Proks· 2 shared S. J. Tucker· 2 shared T. Baukrowitz· 2 shared

Activity by Year

2018-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

J. L. Parker

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Author profile →

9 papers

Recent·Most cited

CryoEM Structure of the human THIK-1 K2P K+ Channel Reveals a Lower 'Y-gate' Regulated by Lipids and Anaesthetics

K. E. Rodstrom, B. Eymsh, P. Proks, M. S. Hayre, C. Madry, A. Rowland, S. Newstead, T. Baukrowitz, M. Schewe, S. J. Tucker

The paper presents a cryoEM structure of the human THIK-1 K2P K+ channel, revealing structural features and regulatory mechanisms involving lipids and anaesthetics.

bioRxiv · Jun 26, 2024 · PreprintBiophysics

The mechanism of mammalian proton-coupled peptide transporters

S. M. Lichtinger, J. L. Parker, S. Newstead, P. Biggin

This study uses molecular dynamics simulations to elucidate the conformational mechanism and proton-substrate coupling in mammalian POTs, revealing key structural differences and functional insights.

bioRxiv · Feb 4, 2024Biophysics

Extracellular modulation of TREK-2 activity with nanobodies provides insight into the mechanisms of K2P channel regulation

K. E. J. Rodstrom, A. Cloake, J. Sormann, A. Baronina, K. H. M. Smith, A. C. W. Pike, J. Ang, P. Proks, M. Schewe, I. Holland-Kaye, S. R. Bushell, J. Elliott, E. Pardon, T. Baukrowitz, R. J. Owens, , S. J. Tucker

The paper identifies nanobodies that selectively modulate TREK-2 channel activity and reveals their binding mechanisms through structural analysis.

bioRxiv · Oct 19, 2023Biophysics

Proton Coupling and the Multiscale Kinetic Mechanism of a Peptide Transporter

C. Li, Z. Yue, S. Newstead, G. A. Voth

This study uses multiscale modeling to show how proton flux drives the conformational changes and ligand transport in proton-coupled peptide transporters.

bioRxiv · Sep 10, 2021Biophysics

Molecular basis for redox control by the human cystine/glutamate antiporter System xc-.

J. L. Parker, J. C. Deme, D. Kolokouris, G. Kuteyi, S. M. Lea, S. Newstead

The paper determines the cryo-EM structure of System xc- in apo and glutamate-bound states, revealing an allosteric mechanism for ligand discrimination and cystine transport.

bioRxiv · Aug 9, 2021Biochemistry

A baton-relay mechanism for ER retrieval signal capture and proofreading by the KDEL receptor

A. Gerondopoulos, P. Bräuer, T. Sobajima, Z. Wu, J. L. Parker, P. Biggin, F. A. Barr, S. Newstead

The paper investigates the KDEL receptor's mechanism for capturing and proofreading ER retrieval signals, revealing a baton-relay mechanism and selective proofreading steps.

bioRxiv · Mar 21, 2021Cell Biology

The KDEL Trafficking Receptor Exploits pH to Tune the Strength of an Unusual Short Hydrogen Bond.

Z. Wu, S. Newstead, P. C. Biggin

The paper shows that the KDEL receptor uses pH to strengthen a short hydrogen bond, enhancing peptide binding and enabling COPI-mediated retrieval of ER proteins.

Scientific Reports · Oct 9, 2020Peer-reviewedBiophysics

Proton-control of transitions in an amino-acid transporter

Z. Wu, I. Alibay, S. Newstead, P. C. Biggin

The paper uses molecular dynamics simulations to study proton-coupled amino acid transport in GkApcT, showing that deprotonation of E115 facilitates the transition from inward-occluded to inward-open states.

bioRxiv · Apr 11, 2019Biophysics

Structural basis for prodrug recognition by the SLC15 family of proton coupled peptide transporters

G. S. Minhas, S. Newstead

The paper presents crystal structures of prokaryotic SLC15 transporter homologues complexed with prodrugs, revealing structural insights into prodrug recognition mechanisms.

bioRxiv · Oct 26, 2018Biochemistry