Author

A. Baldwin

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· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 4 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Approach:deep learning· 1

Frequent Co-Authors

T. R. Alderson· 2 shared A. Giliberti· 1 shared A. Khan· 1 shared A. Lakshminarayanan· 1 shared A. Le Bas· 1 shared A. M. Giltrap· 1 shared A. M. J. J. Bonvin· 1 shared A. Renieri· 1 shared

Activity by Year

2018-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersBiochemistry

T. R. Alderson

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Cryptic pathogen-sugar interactions revealed by universal saturation transfer analysis

C. J. Buchanan, B. Gaunt, P. J. Harrison, Y. Yang, J. Liu, A. Khan, A. M. Giltrap, A. Le Bas, P. N. Ward, K. Gupta, M. Dumoux, S. Daga, N. Picchiotti, M. Baldassarri, E. Benetti, , B. G. Davis

This paper introduces uSTA, an NMR method to analyze protein-ligand interactions, revealing SARS-CoV-2 spike binds sialoside sugars via the NTD and showing variants-of-concern lose this binding.

bioRxiv · Apr 14, 2021Biophysics

αB-crystallin affects the morphology of Aβ(1-40) aggregates

H. Muller, D. M. Dias, A. van der Zalm, A. Baldwin

This paper introduces a protocol for producing native Aβ(1-40) with high reproducibility and shows that αB-crystallin inhibits amyloid fibril formation, favoring disordered aggregates.

bioRxiv · Mar 7, 2021 · PreprintBiochemistry

Local frustration determines loop opening during the catalytic cycle of an oxidoreductase

L. S. Stelzl, D. A. I. Mavridou, E. Saridakis, D. Gonzalez, A. Baldwin, S. J. Ferguson, M. Sansom, C. Redfield

This study shows how oxidation of cysteine thiols to a disulfide bond in DsbD introduces local frustration, disrupting the cap-loop structure and enabling loop opening during its catalytic cycle.

bioRxiv · Jun 14, 2020Biophysics

Dysregulated interactions triggered by a neuropathy-causing mutation in the IPV motif of HSP27

T. R. Alderson, E. Adriaenssens, B. Asselbergh, I. Pritisanac, H. Y. Gastall, M. A. Walti, J. M. Louis, V. Timmerman, A. Baldwin, J. L. P. Benesch

This study investigates how the P182L mutation in HSP27's IxI/V motif disrupts protein interactions, leading to aggregation and disease.

bioRxiv · Sep 10, 2019 · PreprintBiochemistry

Phosphorylation of HspB1 regulates its mechanosensitive molecular chaperone interaction with native filamin C

M. Collier, T. R. Alderson, C. de Villiers, D. Nicholls, H. Gastall, T. Allison, M. Degiacomi, D. Fuerst, P. van de Ven, K. Djinovic-Carugo, A. Baldwin, H. Watkins, K. Gehmlich, J. L. Benesch

This study shows phosphorylation of HspB1 enhances its interaction with filamin C under mechanical stress, stabilizing its structure and protecting it from over-extension.

bioRxiv · May 18, 2018Biophysics