Author

O. R. Davies

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· 8 Cell Biology· 5 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 14 Research Focus:chromatin & epigenetic regulation· 8 Organism:mouse· 7 Assay:structural biology· 5 Research Focus:cell signaling & trafficking· 4 Approach:biophysical modeling· 3 Research Focus:cell type annotation· 3 Research Focus:protein folding & dynamics· 3

Frequent Co-Authors

J. M. Dunce· 4 shared L. J. Salmon· 3 shared M. Gurusaran· 3 shared O. M. Dunne· 3 shared I. R. Adams· 2 shared J. H. Crichton· 2 shared A. A. Jeyaprakash· 1 shared A. M. Pendas· 1 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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4 shared papersBiochemistry

J. M. Dunce

Mutual co-authors in cluster

Author profile →

14 papers

Recent·Most cited

BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode

J. M. Dunce, O. R. Davies

This study reports the structural basis of how BRCA2's PhePP motifs stabilize RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode.

bioRxiv · Nov 20, 2023Biochemistry

MEILB2-BRME1 forms a V-shaped DNA clamp upon BRCA2-binding in meiotic recombination

M. Gurusaran, J. Zhang, K. Zhang, H. Shibuya, O. R. Davies

The paper reports the crystal structure of MEILB2-BRME1 complex and shows how BRCA2 binding causes it to form a V-shaped DNA clamp to facilitate meiotic recombination.

bioRxiv · Jul 4, 2023 · PreprintBiochemistry

Crystal structure of SUN1-KASH6 reveals an asymmetric LINC complex architecture compatible with nuclear membrane insertion

M. Gurusaran, B. S. Erlandsen, O. R. Davies

The paper reports the crystal structure of the SUN1-KASH6 complex, revealing an asymmetric arrangement that explains how KASH proteins can insert into the outer nuclear membrane.

bioRxiv · Jun 5, 2023Biochemistry

Parallel recruitment pathways contribute to synaptonemal complex assembly during mammalian meiosis

J. H. Crichton, J. M. Dunce, W. M. Baarends, O. R. Davies, I. R. Adams

This study shows that SYCE2 is recruited to recombination sites early in SC assembly, independent of SYCP1, suggesting parallel recruitment pathways in mammalian meiosis.

bioRxiv · Apr 14, 2022 · PreprintCell Biology

The meiotic LINC complex component KASH5 is an activating adaptor for cytoplasmic dynein

K. E. L. GARNER, A. Salter, C. K. Lau, G. Manickam, C. Villemant, E. P. Granger, G. McNee, P. G. Woodman, O. R. Davies, B. E. Burke, V. J. Allan

This study identifies KASH5 as an activating adaptor for cytoplasmic dynein during meiosis, showing its role in dynein motility and complex assembly.

bioRxiv · Apr 13, 2022 · PreprintCell Biology

Structural maturation of SYCP1-mediated meiotic chromosome synapsis through conformational remodelling by molecular adapter SYCE3

J. H. Crichton, J. M. Dunce, O. M. Dunne, L. J. Salmon, P. S. Devenney, J. Lawson, I. R. Adams, O. R. Davies

The paper reveals that SYCE3 remodels the SYCP1 lattice during meiotic synapsis, enabling long-range synapsis by forming an integrated SYCP1-SYCE3 lattice.

bioRxiv · Mar 6, 2022 · PreprintBiochemistry

Structural Basis for Mis18 Complex Assembly: Implications for Centromere Maintenance

R. Thamkachy, B. Medina-Pritchard, S. H. Park, C. G. Chiodi, J. Zou, M. de la Torre-Barranco, K. Shimanaka, M. A. Abad, C. Gallego Paramo, R. Feederle, E. Ruksenaite, P. Heun, O. R. Davies, J. Rappsilber, D. Schneidman-Duhovny, , A. A. Jeyaprakash

This study characterizes the structure of the Mis18 complex and identifies structural determinants essential for its assembly and centromere maintenance.

bioRxiv · Nov 8, 2021 · PreprintCell Biology

Structural basis for the coiled-coil architecture of human CtIP

C. R. Morton, N. J. Rzechorzek, J. D. Maman, M. Kuramochi, H. Sekiguchi, R. P. Rambo, Y. C. Sasaki, O. R. Davies, L. Pellegrini

This study presents an atomic model of human CtIP's structure, revealing its extended dimer-of-dimers architecture and dynamic zinc-binding motif involved in DNA repair.

bioRxiv · Mar 5, 2021Biophysics

Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12

J. M. Dunce, L. J. Salmon, O. R. Davies

The paper reports the structural basis of SYCE2-TEX12 assembly in the meiotic synaptonemal complex, revealing a hierarchical fibrous mechanism similar to cytoskeletal proteins.

bioRxiv · Dec 30, 2020Biochemistry

A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies

M. Gurusaran, O. R. Davies

This study reveals that SUN-KASH forms a 6:6 complex rather than the canonical 3:3 model, leading to a branched LINC complex network for force distribution.

bioRxiv · Mar 21, 2020Biochemistry

Meiotic chromosome synapsis depends on multivalent SYCE1-SIX6OS1 interactions that are disrupted in cases of human infertility

F. Sanchez-Saez, L. Gomez-H, O. M. Dunne, C. Gallego-Paramo, N. Felipe-Medina, M. A. Sanchez-Martin, E. Llano, A. M. Pendas, O. R. Davies

This study identifies SYCE1-SIX6OS1 interactions critical for meiotic synapsis, showing that mutations disrupting these interactions cause human infertility.

bioRxiv · Feb 4, 2020Biochemistry

Synchronous chromosome segregation in mouse oocytes is ensured by biphasic securin destruction and cyclin B1-Cdk1

C. Thomas, M. D. Levasseur, R. J. Harris, O. R. Davies, S. Madgwick

This study identifies a novel mechanism in mouse oocytes that ensures synchronous chromosome segregation through biphasic securin destruction and cyclin B1-Cdk1 inhibition of separase.

bioRxiv · Oct 30, 2019 · PreprintCell Biology

A molecular model for self-assembly of synaptonemal complex protein SYCE3

O. M. Dunne, O. R. Davies

This study identifies a self-assembly mechanism for SYCE3, a synaptonemal complex protein, using biophysical techniques and structural analysis.

bioRxiv · Mar 1, 2019Biochemistry

A pseudo-meiotic centrosomal function of TEX12 in cancer

S. Sandhu, L. J. Salmon, J. E. Hunter, C. L. Wilson, N. D. Perkins, N. Hunter, O. R. Davies, U. L. McClurg

The paper identifies TEX12 as a meiosis-specific gene aberrantly expressed in cancer, showing its role in centrosome dysfunction and oncogenesis.

bioRxiv · Jan 8, 2019 · PreprintCell Biology