Publications

• Balachandra V, Shrestha RL, Hammond CM#, Lin S, Hendriks IA, Sethi SC, Chen L, Sevilla S, Caplen NJ, Chari R, Karpova TS, McKinnon K, Todd MAM, Koparde V, Cheng KCC, Nielsen ML, Groth A, Basrai MA#, “DNAJC9 prevents CENP-A mislocalization and chromosomal instability by maintaining the fidelity of histone supply chains” EMBO J. accepted (2024). 10.1038/s44318-024-00093-6. Identified DNAJC9 as a factor restricting CENP-A mislocalisation and chromasomal instability highlighting that maintaining H3–H4 supply to chromatin ensures proper centromere targeting of CENP-A.

• Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, Goloubinoff P, Gestwicki J, Hammond CM, Hines JK, Ishikawa K, Joachimiak LA, Kirstein J, Liberek K, Mokranjac D, Nillegoda N, Ramos CHI, Rebeaud M, Ron D, Rospert S, Sahi C, Shalgi R, Tomiczek B, Ushioda R, Ustyantseva E, Ye Y, Zylicz M, Kampinga HH. “J-domain proteins: From molecular mechanisms to diseases” Cell Stress Chaperones. 29(1):21-33 (2023). 10.1016/j.cstres.2023.12.002. Meeting report from a conference with group leaders in the heat shock community that work of J domain proteins, a particular honour to have been invited to when I was still a postdoc. Cell Stress Society International “J-domain proteins from molecular mechanisms to diseases” (2023; Invited Speaker)

• Carraro M*, Hendriks IA*, Hammond CM*,#, Solis V, Völker-Albert M, Elsborg JD, Weisser MB, Spanos C, Montoya G, Rappsilber J, Imhof A, Nielsen ML#, Groth A#, “DAXX adds a de novo H3.3K9me3 Deposition Pathway to the Histone Chaperone Network” Mol Cell. 83(7):1075-1092 (2023). Demonstrated that the heterochromatin mark H3K9me3 can be established on soluble histones prior to nucleosome assembly. Previewed in Nat Struct Mol Biol by Dmitris Typas and in Mol Cell by Zhiming Li and Zhiguo Zhang; Presented at Cell Stress Society International “J-domain proteins from molecular mechanisms to diseases” (2023; Invited Speaker), ASBMB “Epigenetic Regulation and Genome Stability” (2022; Invited Speaker). 

• Hammond CM*, Bao H*, Hendriks IA, Carraro M, García-Nieto A, Liu Y, Reverón-Gómez N, Spanos C, Chen L, Rappsilber J, Nielsen ML, Patel DJ, Huang H, Groth A, “DNAJC9 Integrates Heat Shock Molecular Chaperones into the Histone Chaperone Network” Mol Cell. 81(12):2533-2548 (2021). Demonstrated that molecular chaperones combine with histone chaperones during histone supply. Previewed in Molecular Cell by Jan Dreyer and Francesca Mattiroli; Recommended in Faculty Opinions by Sofie Polo; Poster prize award at FEBS 45th Congress 2021; Presented at the Fragile Nucleosome Seminar Series (2021, Selected abstract) and Protein Homeostasis virtual seminar (2022, Invited speaker), Presented at Cell Stress Society International “J-domain proteins from molecular mechanisms to diseases” (2023; Invited Speaker).

• Hammond CM*, Strømme CB*, Huang H, Patel DJ, Groth A, "Histone Chaperone Networks Shaping Chromatin Function" Nat Rev Mol Cell Biol. 18(3):141-158 (2017). Introduced the histone chaperone network concept that built on my previous publications and led to the identification of the role of DNAJC9 and DAXX in the histone chaperone network. 

• Saredi G*, Huang H*, Hammond CM, Alabert C, Bekker-Jensen S, Forne I, Reverón-Gómez N, Foster BM, Mlejnkova L, Bartke T, Cejka P, Mailand N, Imhof A, Patel DJ, Groth A, "H4K20me0 Marks Post-replicative Chromatin and Recruits the TONSL–MMS22L DNA Repair Complex." Nature 534(7609):14-8 (2016). Demonstrated that new histones mark regions of the genome that have been replicated and are competant for repair via homologous recombination.

• Hammond CM*, Sundaramoorthy R, Larance M, El-Mkami H, Lamond A, Norman DG, Owen-Hughes T. “The Histone Chaperone Vps75 Forms Multiple Oligomeric Assemblies Capable of Mediating Exchange Between Histone H3-H4 Tetramers and Asf1-H3-H4 Complexes.” Nucleic Acids Res. 44(13):6157-72 (2016). Demonstrated that histone chaperones Asf1 and Vps75 form a histone dependent interaction - this was a key discovery that helped conceptualise the histone chaperone network theory. My second biomolecular crystal structure - the Vps75 tetramer.

• Hammond CM*, Owen-Hughes T, Norman DG, “Modelling Multi-protein Complexes Using PELDOR Distance Measurements for Rigid Body Minimisation Experiments Using XPLOR-NIH.” Methods 70(2-3):139-53 (2014). A computational biology pipeline for using PELDOR and cross-linking MS experimentally derived distance restraints to dock different protein structures together. 

• Bowman A*, Hammond CM*, Stirling A, Ward R, Shang W, El-Mkami H, Robinson DA, Svergun DI, Norman DG, Owen-Hughes T. “The Histone Chaperones Vps75 and Nap1 Form Ring-like, Tetrameric Structures in Solution” Nucleic Acids Res. 42(9):6038-51 (2014). Demonstrated for the first time that histone chaperones can self-chaperone, i.e. form oligomers that shield their histone binding surfaces.

• Daldrop P*, Reyes FE, Robinson DA, Hammond CM, Lilley DM, Batey RT, Brenk R. “Novel Ligands for a Purine Riboswitch Discovered by RNA-ligand Docking.” Chem Biol. 18(3): 324-35 (2011). My first biomolecular x-ray crystal structure - an RNA riboswitch (Figure 1), solved in a rotation project in the first year of my PhD - before I started my PhD with Tom Owen-Hughes.

• Bellabarba RM*, Hammond C, Forman GS, Tooze RP, Slawin AM. “1,8-Dimethylnaphthalene-bridged Diphosphine Ligands: Synthesis and Structural Comparison of their Palladium Complexes.” Dalton Trans. (20):2444-9 (2006). During my undergraduate year in industry at Sasol Technology (UK) Ltd I synthesised and characterised all of the ligands and paladium complexes in this paper.

(* indicates first authorship, # indicates corresponding authorship)