How to build a bone: PHOSPHO1, biomineralization and beyond
Journal Article
Dillon, S., Staines, K. A., Millán, J. L., & Farquharson, C. (2019)
How to build a bone: PHOSPHO1, biomineralization and beyond. Journal of Bone and Mineral Research Plus, 3(7), https://doi.org/10.1002/jbm4.10202
Since its characterization two decades ago, the phosphatase PHOSPHO1 has been the subject of an increasing focus of research. This work has elucidated PHOSPHO1’s central role ...
The Ex Vivo Organ Culture of Bone
Book Chapter
Staines, K. A., Brown, G., & Farquharson, C. (2019)
The Ex Vivo Organ Culture of Bone. In Bone Research Protocols (199-215). New york, USA: Humana Press. https://doi.org/10.1007/978-1-4939-8997-3_10
The ex vivo organ culture of bone provides many of the advantages of both the whole organism and isolated cell strategies and can deliver valuable insight into the network of ...
Silver nanoparticles promote the emergence of heterogeneic human neutrophil sub-populations
Journal Article
Kemp, S., Young, L., Ross, M., Prach, M., Hutchison, G. R., Malone, E., & Fraser, J. A. (2018)
Silver nanoparticles promote the emergence of heterogeneic human neutrophil sub-populations. Scientific Reports, 8(1), https://doi.org/10.1038/s41598-018-25854-2
Neutrophil surveillance is central to nanoparticle clearance. Silver nanoparticles (AgNP) have numerous uses, however conflicting evidence exists as to their impact on neutrop...
Overexpression of TIMP-3 in Chondrocytes Produces Transient Reduction in Growth Plate Length but Permanently Reduces Adult Bone Quality and Quantity
Journal Article
Poulet, B., Liu, K., Plumb, D., Vo, P., Shah, M., Staines, K., …Bou-Gharios, G. (2016)
Overexpression of TIMP-3 in Chondrocytes Produces Transient Reduction in Growth Plate Length but Permanently Reduces Adult Bone Quality and Quantity. PLOS ONE, 11(12), https://doi.org/10.1371/journal.pone.0167971
Bone development and length relies on the growth plate formation, which is dependent on degradative enzymes such as MMPs. Indeed, deletion of specific members of this enzyme f...
Phosphomimetic Mutation of the N-Terminal Lid of MDM2 Enhances the Polyubiquitination of p53 through Stimulation of E2-Ubiquitin Thioester Hydrolysis
Journal Article
Fraser, J. A., Worrall, E. G., Lin, Y., Landre, V., Pettersson, S., Blackburn, E., …Hupp, T. R. (2015)
Phosphomimetic Mutation of the N-Terminal Lid of MDM2 Enhances the Polyubiquitination of p53 through Stimulation of E2-Ubiquitin Thioester Hydrolysis. Journal of Molecular Biology, 427(8), 1728-1747. https://doi.org/10.1016/j.jmb.2014.12.011
Mouse double minute 2 (MDM2) has a phosphorylation site within a lid motif at Ser17 whose phosphomimetic
mutation to Asp17 stimulates MDM2-mediated polyubiquitination of p53. ...
Regulation and Function of the Original p53- Inducible p21 Gene
Book Chapter
Fraser, J. A. (2010)
Regulation and Function of the Original p53- Inducible p21 Gene. In p53; Molecular Biology Intelligence Unit, 100-116. Springer Science + Business Media. https://doi.org/10.1007/978-1-4419-8231-5_7
P21 is a well known regulator of cell cycle progression through its inhibitory actions on Cyclin dependent kinases, (Cdk)/cyclin complexes, and DNA replication via its binding...
A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: II. A MODEL IN WHICH PHOSPHORYLATION AT SER269 INDUCES A MUTANT CONFORMATION TO p53.
Journal Article
Fraser, J. A., Madhumalar, A., Blackburn, E., Bramham, J., Walkinshaw, M. D., Verma, C., & Hupp, T. R. (2010)
A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: II. A MODEL IN WHICH PHOSPHORYLATION AT SER269 INDUCES A MUTANT CONFORMATION TO p53. Journal of Biological Chemistry, 285, 37773-37786. https://doi.org/10.1074/jbc.M110.143107
The p53 DNA-binding domain harbors a conformationally flexible multiprotein binding site that regulates p53 ubiquitination. A novel phosphorylation site exists within this reg...
A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: I. PHOSPHORYLATION AT SER269 IN VIVO IS LINKED TO INACTIVATION OF p53 FUNCTION.
Journal Article
Fraser, J. A., Vojtesek, B., & Hupp, T. R. (2010)
A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: I. PHOSPHORYLATION AT SER269 IN VIVO IS LINKED TO INACTIVATION OF p53 FUNCTION. Journal of Biological Chemistry, 285, 37762-37772. https://doi.org/10.1074/jbc.M110.143099
p53 is a thermodynamically unstable protein containing a conformationally flexible multiprotein docking site within the DNA-binding domain. A combinatorial peptide chip used t...
A Central Role for CK1 in Catalyzing Phosphorylation of the p53 Transactivation Domain at Serine 20 after HHV-6B Viral Infection
Journal Article
MacLaine, N. J., Øster, B., Bundgaard, B., Fraser, J. A., Buckner, C., Lazo, P. A., …Hupp, T. R. (2008)
A Central Role for CK1 in Catalyzing Phosphorylation of the p53 Transactivation Domain at Serine 20 after HHV-6B Viral Infection. Journal of Biological Chemistry, 283, 28563-28573. https://doi.org/10.1074/jbc.M804433200
The tumor suppressor protein p53 is activated by distinct cellular stresses including radiation, hypoxia, type I interferon, and DNA/RNA virus infection. The transactivation d...
The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members
Journal Article
Craig, A. L., Chrystal, J. A., Fraser, J. A., Sphyris, N., Lin, Y., Harrison, B. J., …Hupp, T. R. (2007)
The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members. Molecular and Cellular Biology, 27(9), 3542-3555. https://doi.org/10.1128/mcb.01595-06
Genetic and biochemical studies have shown that Ser20 phosphorylation in the transactivation domain of p53 mediates p300-catalyzed DNA-dependent p53 acetylation and B-cell tum...