Author

H. R. Saibil

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· 4 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:cryo-EM· 4 Organism:mouse· 3 Research Focus:host-pathogen & immune response· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Organism:bacteria (other)· 1

Frequent Co-Authors

A. Wenborn· 2 shared J. Betts· 2 shared J. Collinge· 2 shared N. Lukoyanova· 2 shared S. Joiner· 2 shared S. W. Manka· 2 shared A. J. Roberts· 1 shared A. Wentink· 1 shared

Activity by Year

2021-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiochemistry

A. Wenborn

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6 papers

Recent·Most cited

Structural basis of substrate progression through the chaperonin cycle

S. Gardner, M. C. Darrow, N. Lukoyanova, K. Thalassinos, H. R. Saibil

The paper uses cryoEM to determine structures of GroEL-GroES complexes with Rubisco, revealing conformational changes and interactions during the chaperonin cycle.

bioRxiv · May 29, 2023 · PreprintBiophysics

Sequential roles for red blood cell binding proteins enable phased commitment to invasion for malaria parasites

M. N. Hart, F. Mohring, S. M. Donvito, J. A. Thomas, N. Muller-Sienerth, G. J. Wright, E. Knuepfer, H. R. Saibil, R. W. Moon

This study identifies the sequential roles of DBP and NBPXa in P. knowlesi merozoite invasion of human RBCs, revealing a phased commitment mechanism that can be targeted with antibodies.

bioRxiv · Aug 9, 2022Cell Biology

A structural basis for prion strain diversity

S. W. Manka, A. Wenborn, J. Betts, S. Joiner, H. R. Saibil, J. Collinge, J. D. Wadsworth

This paper determines the cryo-EM structure of ME7 prion fibrils and compares it to RML fibrils, revealing structural differences that explain prion strain diversity within the same species.

bioRxiv · May 17, 2022 · PreprintBiochemistry

2.7 A cryo-EM structure of ex vivo RML prion fibrils

S. W. Manka, W. Zhang, A. Wenborn, J. Betts, S. Joiner, H. R. Saibil, J. Collinge, J. D. F. Wadsworth

The paper presents a cryo-EM structure of prion fibrils from RML prion-infected mice, revealing structural features and conformational variations that may influence prion strain diversity and propagation.

bioRxiv · Dec 13, 2021Biochemistry

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

The pore conformation of lymphocyte perforin

M. Ivanova, N. Lukoyanova, S. Malhotra, M. Topf, J. A. Trapani, I. Voskoboinik, H. R. Saibil

This study presents a high-resolution cryo-EM structure of the perforin pore, revealing conformational changes and interactions that explain its function and pathogenic mutations.

bioRxiv · Jul 3, 2021Biochemistry