Author

J. L. Benesch

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 Assay:proteomics· 5 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1

Frequent Co-Authors

M. Degiacomi· 2 shared P. Kukura· 2 shared W. B. Struwe· 2 shared A. Baldwin· 1 shared A. Croft· 1 shared A. Elofsson· 1 shared A. Maxwell· 1 shared A. Olerinyova· 1 shared

Activity by Year

2018-2023 · peak 5/yr

Co-Author Collaboration Network

10 top collaborators · 10 mutual co-author links

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2 shared papersBiophysics

M. Degiacomi

Mutual co-authors in cluster

Author profile →

9 papers

Recent·Most cited

Cooperativity and induced oligomerisation control the interaction of SARS- CoV-2 with its cellular receptor and patient-derived antibodies

R. Asor, A. Olerinyova, S. A. Burnap, M. S. Kushwah, F. Soltermann, L. P. Rudden, M. Hensen, S. Vasiljevic, J. Brun, M. Hill, L. Chang, W. Dejnirattisai, P. Supasa, J. Mongkolsapaya, D. Zhou, , P. Kukura

The paper investigates how multivalent interactions between SARS-CoV-2 spike protein, ACE2 receptor, and patient-derived antibodies influence viral entry and antibody inhibition.

bioRxiv · Sep 14, 2023 · PreprintBiophysics

Regulation of inositol 5-phosphatase activity by the C2 domain of SHIP1 and SHIP2

W. J. Bradshaw, E. C. Kennedy, T. Moreira, L. A. Smith, R. Chalk, V. L. Katis, J. L. Benesch, P. E. Brennan, E. J. Murphy, O. Gileadi

The paper determines structures of SHIP1 and SHIP2 phosphatase and C2 domains, showing the C2 domain modulates phosphatase activity more in SHIP2 than SHIP1, providing insights for drug development.

bioRxiv · Jul 31, 2023Biochemistry

Development of a PNGase Rc column for online deglycosylation of complex glycoproteins during HDX-MS

T. O. T. Lambert, M. Gramlich, L. S. Stutzke, L. Smith, D. Deng, P. D. Kaiser, U. Rothbauer, J. L. Benesch, C. Wagner, M. Koenig, P. Pompach, P. Novak, A. Zeck, K. D. Rand

The paper develops a PNGase Rc column for online deglycosylation during HDX-MS, enabling efficient analysis of glycoproteins and mapping of mAb binding epitopes.

bioRxiv · Jul 28, 2023Biochemistry

Dimerisation of European robin cryptochrome 4a

M. Hanic, L. M. Antill, A. S. Gehrckens, J. Schmidt, K. Gortemaker, R. Bartolke, T. J. El-Baba, J. Xu, K. W. Koch, H. Mouritsen, J. L. Benesch, P. J. Hore, I. A. Solov'yov

The paper investigates dimerisation of European robin Cry4a through experimental and computational methods, identifying disulphide-linked dimers and proposing their relevance to magnetoreception.

bioRxiv · Apr 11, 2023 · PreprintBiochemistry

The adaptability of the ion binding site by the Ag(I)/Cu(I) periplasmic chaperone SilF.

R. Lithgo, M. Hanzevacki, G. Harris, J. Kamps, E. Holden, J. L. Benesch, C. Jager, A. Croft, J. Hobman, A. Orville, A. Quigley, S. Carr, D. Scott

This study shows SilF, a periplasmic chaperone, binds both Ag(I) and Cu(I) with similar affinities, suggesting Gram-negative bacteria use an existing Cu(I) detox system for Ag(I) resistance.

bioRxiv · Mar 31, 2023Biophysics

Rapid, DNA-induced interface swapping by DNA gyrase

T. Germe, N. G. Bush, V. Baskerville, D. Saman, J. L. Benesch, A. Maxwell

This paper demonstrates DNA gyrase can swap DNA-cleaving interfaces between heterotetramers, enabling DNA passage without ATP and raising new mechanistic possibilities.

bioRxiv · Sep 8, 2022Biochemistry

Complementing machine learning-based structure predictions with native mass spectrometry

T. M. Allison, M. T. Degiacomi, E. G. Marklund, L. Jovine, A. Elofsson, J. L. Benesch, M. Landreh

This study shows that native mass spectrometry can reveal structural features not detectable by AlphaFold2, improving the accuracy of protein structure models.

bioRxiv · Mar 17, 2022Biophysics

Quantifying the heterogeneity of macromolecular machines by mass photometry

A. Sonn Segev, K. Belacic, T. Bodrug, G. Young, R. T. VanderLinden, B. Schulman, J. Schimpf, T. Friedrich, P. Vinh Dip, T. Schwartz, B. Bauer, J.-M. Peters, W. B. Struwe, J. L. Benesch, N. G. Brown, , P. Kukura

This paper demonstrates that mass photometry accurately quantifies sample heterogeneity with high resolution and minimal volume, outperforming negative stain electron microscopy in detecting proteasome assemblies.

bioRxiv · Dec 4, 2019Biophysics

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