Author

C. R. Bramham

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· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:protein folding & dynamics· 3 Organism:human· 2 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:Drosophila· 1 Assay:protein structure· 1

Frequent Co-Authors

E. I. Hallin· 4 shared P. Kursula· 4 shared M. S. Eriksen· 2 shared O. Nikolaienko· 2 shared T. Hosokawa· 2 shared Y. Hayashi· 2 shared A. E. Torda· 1 shared A. Martinez· 1 shared

Activity by Year

2018-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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4 shared papersBiochemistry

E. I. Hallin

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Author profile →

4 papers

Recent·Most cited

Structural properties and peptide ligand binding of the capsid homology domains of human Arc

E. I. Hallin, C. R. Bramham, P. Kursula

This study identifies conserved interactions in the Arc protein's peptide binding site and characterizes its structural properties and potential functional roles in synaptic processes.

bioRxiv · Dec 17, 2020Biochemistry

Crystal and solution structures reveal oligomerization of individual capsid homology domains of Drosophila Arc

E. I. Hallin, S. Markusson, L. Bottger, A. E. Torda, C. R. Bramham, P. Kursula

This study compares the structural properties of dArc lobes to mammalian Arc, showing dArc forms oligomers while mammalian Arc is monomeric, suggesting different capsid assembly mechanisms.

bioRxiv · Nov 18, 2020Biochemistry

Molecular determinants of Arc oligomerization and formation of virus-like capsids

M. S. Eriksen, O. Nikolaienko, E. I. Hallin, S. Grodem, H. J. Bustad, M. I. Flydal, R. O'Connell, T. Hosokawa, D. Lascu, S. Akerkar, J. Cuellar, J. J. Chambers, I. Merski, G. Muruganandam, R. Loris, , C. R. Bramham

This paper identifies a 28-amino-acid region in Arc critical for oligomerization and virus-like capsid formation, showing that exogenous RNA enhances assembly.

bioRxiv · Nov 22, 2019 · PreprintBiochemistry

Structure of monomeric full-length ARC sheds light on molecular flexibility, protein interactions, and functional modalities

E. I. Hallin, M. S. Eriksen, S. Baryshnikov, O. Nikolaienko, S. Groedem, T. Hosokawa, Y. Hayashi, C. R. Bramham, P. Kursula

This study determines the structure of monomeric full-length ARC, revealing its compact conformation and interaction sites for postsynaptic proteins and phospholipid membranes.

bioRxiv · May 26, 2018Biophysics