Author

S. M. Hamdan

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· 3 Biophysics· 3

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:experimental assay· 4 Organism:human· 3 Research Focus:protein structure prediction· 3 Approach:microscopy & imaging analysis· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

A. De Biasio· 4 shared M. Tehseen· 4 shared C. G. Savva· 3 shared A. Shirbini· 2 shared A. Al-Amodi· 1 shared A. Cubbon· 1 shared A. Horton· 1 shared A. M. van Oijen· 1 shared

Activity by Year

2019-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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4 shared papersBiochemistry

A. De Biasio

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Structure of the human CTF18-RFC clamp loader bound to PCNA

G. Briola, M. Tehseen, A. Al-Amodi, G. Young, A. U. Danazumi, P. Q. Nguyen, C. G. Savva, M. Hedglin, S. M. Hamdan, A. De Biasio

This study presents a cryo-EM structure of the human CTF18-RFC complex bound to PCNA, revealing structural features important for PCNA loading and Pol ε-mediated leading strand synthesis.

bioRxiv · May 8, 2024 · PreprintBiochemistry

Structural visualisation of the dynamics of DNA unwinding by a replicative helicase

T. Shahid, M. Tehseen, L. Alhudhali, A. R. Clark, C. G. Savva, S. M. Hamdan, A. De Biasio

This study uses cryo-EM to visualize the dynamics of DNA unwinding by the SV40 Large Tumor Antigen helicase, revealing how ATP hydrolysis drives translocation and strand separation.

bioRxiv · Apr 19, 2024 · PreprintBiophysics

Structure of Aquifex aeolicus Lumazine Synthase by Cryo-Electron Microscopy to 1.42 Angstrom Resolution

C. G. Savva, M. A. Sobhy, A. De Biasio, S. M. Hamdan

The paper uses Cryo-EM to determine the structure of Aquifex aeolicus lumazine synthase at 1.42 Angstrom resolution, revealing hydrogen atoms and confirming near-atomic resolution for protein complexes.

bioRxiv · Mar 21, 2024 · PreprintBiophysics

Human HelQ and DNA polymerase δ interact to halt DNA synthesis and stimulate DNA single-strand annealing

L. He, R. Lever, A. Cubbon, M. Tehseen, A. O. Nottingham, A. Horton, H. Betts, M. Fisher, S. M. Hamdan, P. Soultanas, E. L. Bolt

This study shows HelQ interacts with DNA polymerase δ to stop DNA synthesis and enhance DNA single-strand annealing during repair.

bioRxiv · Oct 2, 2022Biochemistry

Rapid single-molecule characterisation of nucleic-acid enzymes

S. H. Mueller, L. J. Fitschen, A. Shirbini, S. M. Hamdan, L. M. Spenkelink, A. M. van Oijen

This paper introduces a single-molecule assay to rapidly characterize DNA metabolism enzymes by measuring fluorescence intensity changes during DNA synthesis, unwinding, or digestion.

bioRxiv · Mar 3, 2022Biophysics

Structure of the processive human Pol δ holoenzyme

C. Lancey, M. Tehseen, V.-S. Raducanu, F. Rashid, N. Merino, T. J. Ragan, C. Savva, M. S. Zaher, A. Shirbini, F. J. Blanco, S. M. Hamdan, A. De Biasio

This study presents the high-resolution cryo-EM structure of the human Pol δ-DNA-PCNA complex with and without FEN1, revealing its structural basis for DNA replication.

bioRxiv · Dec 11, 2019Biochemistry