Author

B. W. Hoogenboom

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· 4 Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Approach:microscopy & imaging analysis· 3 Research Focus:chromatin & epigenetic regulation· 2 Assay:DNA methylation· 2 Research Focus:protein folding & dynamics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

A. L. B. Pyne· 3 shared A. W. Hodel· 2 shared J. G. Beton· 2 shared A. D. Bates· 1 shared A. J. Roberts· 1 shared A. Maxwell· 1 shared A. Menny· 1 shared A. Noy· 1 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersBiophysics

A. L. B. Pyne

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Author profile →

7 papers

Recent·Most cited

Complement-mediated killing of bacteria by mechanical destabilization of the cell envelope

G. Benn, C. Bortolini, D. M. Roberts, A. L. B. Pyne, S. Holden, B. W. Hoogenboom

The paper uses atomic force microscopy to study how MAC pores in E. coli lead to mechanical destabilization of the cell envelope, causing lysis through inner membrane permeation.

bioRxiv · Dec 10, 2023Microbiology

Cooperative Amyloid Fibre Binding and Disassembly by the Hsp70 disaggregase

J. G. Beton, J. Monistrol, A. Wentink, E. C. Johnston, A. J. Roberts, B. Bukau, B. W. Hoogenboom, H. R. Saibil

The paper shows that Hsc70 and DNAJB1, with Apg2, cooperatively bind and disassemble amyloid fibrils, with Apg2 enhancing Hsc70 recruitment and disassembly rate.

bioRxiv · Aug 29, 2021Biochemistry

Crowding-induced phase separation of nuclear transport receptors in FG nucleoporin assemblies

L. K. Davis, I. J. Ford, B. W. Hoogenboom

This study uses a physical model to predict how different nuclear transport receptors (NTRs) modulate each other's penetration through FG nucleoporin assemblies, revealing phase separation at physiologically relevant concentrations.

bioRxiv · Jul 24, 2021Biophysics

Base-pair resolution analysis of the effect of supercoiling on DNA flexibility and major groove recognition by triplex-forming oligonucleotides

A. L. B. Pyne, A. Noy, K. Main, V. Velasco-Berrelleza, M. M. Piperakis, L. A. Mitchenhall, F. M. Cugliandolo, J. G. Beton, C. E. M. Stevenson, B. W. Hoogenboom, A. D. Bates, A. Maxwell, S. A. Harris

This study uses AFM and MD simulations to analyze how DNA supercoiling affects structure and triplex-forming oligonucleotide binding at base-pair resolution.

bioRxiv · Jan 7, 2021Biophysics

Single-molecule measurements reveal that PARP1 condenses DNA by loop formation

N. A. W. Bell, P. J. Haynes, K. Brunner, T. Maia de Oliveira, M. Flocco, B. W. Hoogenboom, J. E. Molloy

This study shows PARP1 condenses undamaged DNA through loop formation using single-molecule techniques, revealing a mechanism for chromatin organization.

bioRxiv · Sep 15, 2020Biophysics

The structure of Macrophage Expressed Gene-1, a phagolysosome immune effector that is activated upon acidification.

S. S. Pang, C. Bayly-Jones, M. Radjainia, B. A. Spicer, R. H. P. Law, A. W. Hodel, S. M. Ekkel, P. J. Conroy, G. Ramm, H. Venugopal, P. I. Bird, B. W. Hoogenboom, I. Voskoboinik, Y. Gambin, E. Sierecki, , J. C. Whisstock

This paper determines the structure of MPEG-1, showing it forms a pre-pore complex and can perforate membranes under acidic conditions.

bioRxiv · Mar 17, 2019 · PreprintBiochemistry

Single-molecule kinetics of pore assembly by the membrane attack complex

E. S. Parsons, G. J. Stanley, A. L. B. Pyne, A. W. Hodel, A. P. Nievergelt, A. Menny, A. R. Yon, A. Rowley, R. P. Richter, G. E. Fantner, D. Bubeck, B. W. Hoogenboom

This study uses AFM to analyze MAC assembly kinetics, finding that C9 incorporation is the rate-limiting step in pore formation.

bioRxiv · Nov 16, 2018Biophysics