Dr Blagojce Jovcevski

Blagojce Jovcevski
Postdoctoral Fellow
School of Physical Sciences
Faculty of Sciences

Blagojce Jovcevski completed his PhD at the Illawarra Health and Medical Research Institute and the University of Wollongong in 2017, under the supervision of Assoc. Prof. Heath Ecroyd and Dr. Andrew Aquilina. His PhD project focused on studying the structure-function relationship of small heat-shock proteins, which are associated with numerous degenerative diseases, using native mass spectrometry.

Recently, I have joined the Pukala research group to utilise similar techniques to understand the aggregation dynamics of aggregation-prone proteins that are associated with neurodegenerative diseases.

Connect With Me

External Profiles

Dr Blagojce Jovcevski

Blagojce Jovcevski completed his PhD at the Illawarra Health and Medical Research Institute and the University of Wollongong in 2017, under the supervision of Assoc. Prof. Heath Ecroyd and Dr. Andrew Aquilina. His PhD project focused on studying the structure-function relationship of small heat-shock proteins, which are associated with numerous degenerative diseases, using native mass spectrometry.

Recently, I have joined the Pukala research group to utilise similar techniques to understand the aggregation dynamics of aggregation-prone proteins that are associated with neurodegenerative diseases.

Investigating the structure of amyloidogenic proteins using mass spectrometry-based approaches

The pathogenesis of neurodegenerative diseases, such as Alzheimer’s disease, Parkinson's disease and amyotrophic lateral sclerosis, is believed to be caused by the aggregation of non-native proteins. One such protein that forms fibril (amyloid) aggregates is alpha-synuclein, which is heavily associated with Parkinson's disease. My current focus is on understanding the role lipids play in the aggregation dynamics of alpha-synuclein using a range of mass spectrometry-based approaches. Native MS is a high-resolution tool utilised in structural biology which can define a range of structural features within proteins, such as oligomeric distribution and polydispersity, unfolded/unstructured states, assembly stability and quaternary conformation of proteins. Using these techniques, in conjunction with other biophysical tools, can provide a structural rationale for protein function/dysfunction. 

Appointments

Date Position Institution name
2017 Postdoctoral Fellow University of Adelaide

Education

Date Institution name Country Title
2012 - 2017 University of Wollongong Australia PhD
2007 - 2011 University of Wollongong Australia Bachelor of Science (Honours) (Biological Sciences)

Research Interests

Journals

Year Citation
2018 Jovcevski, B., Andrew Aquilina, J., Benesch, J., & Ecroyd, H. (2018). The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin. Cell stress & chaperones, Online, 1-10.
DOI
2017 Jovcevski, B., Kelly, M., Aquilina, J., Benesch, J., & Ecroyd, H. (2017). Evaluating the effect of phosphorylation on the structure and dynamics of Hsp27 dimers by means of ion mobility mass spectrometry. Analytical Chemistry, 89(24), 13275-13282.
DOI
2015 Jovcevski, B., Kelly, M., Rote, A., Berg, T., Gastall, H., Benesch, J., . . . Ecroyd, H. (2015). Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity. Chemistry and Biology, 22(2), 186-195.
DOI Scopus25 WoS22 Europe PMC16
2015 Cork, A., Ericsson, D., Law, R., Casey, L., Valkov, E., Bertozzi, C., . . . Kobe, B. (2015). Stability of the octameric structure affects plasminogen-binding capacity of streptococcal enolase. PLoS ONE, 10(3), e0121764-1-e0121764-18.
DOI Scopus2 WoS3 Europe PMC2
2013 Henningham, A., Ericsson, D., Langer, K., Casey, L., Jovcevski, B., Singh Chhatwal, G., . . . Walker, M. (2013). Structure-informed design of an enzymatically inactive vaccine component for group A Streptococcus. mBio, 4(4), e00509-13-1-e00509-13-9.
DOI Scopus9 WoS6 Europe PMC6
Position
Postdoctoral Fellow
Phone
83132540
Fax
8313 4380
Campus
North Terrace
Building
Badger, floor 2
Room Number
2 13
Org Unit
Chemistry

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