Julie Atkin

Professor

Former affiliations

Associate Professor, Department of Biomedical Sciences
Associate Professor, Department of Biomedical Sciences

Macquarie University

https://orcid.org/0000-0003-2427-499X

Emailjulie.atkin@mq.edu.au

Source: Scopus
Calculated based on no. of publications stored in Pure and citations from Scopus

Research activity per year

If you made any changes in Pure these will be visible here soon.

Personal profile

Biography

Julie is interested in the basic cellular and molecular singalling mechanisms involved in neurons as well as other cells. She is particularly interested in processes that trigger neurodegeneration in amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND), and related condition frontotemporal dementia (FTD). This includes the role of cellular trafficking and the DNA damage response, as well as the protein disulphide isomerase family of chaperones.

Fingerprint

Dive into the research topics where Julie Atkin is active. These topic labels come from the works of this person. Together they form a unique fingerprint.

12 Similar Profiles

Network

Recent external collaboration on country level. Dive into details by clicking on the dots or

2 Article
1 Abstract

Amyotrophic lateral sclerosis-linked UBQLN2 mutants inhibit endoplasmic reticulum to Golgi transport, leading to Golgi fragmentation and ER stress
Halloran, M., Ragagnin, A. M. G., Vidal, M., Parakh, S., Yang, S., Heng, B., Grima, N., Shahheydari, H., Soo, K-Y., Blair, I., Guillemin, G. J., Sundaramoorthy, V. & Atkin, J. D., Oct 2020, In: Cellular and Molecular Life Sciences. 77, 19, p. 3859-3873 15 p.
Macquarie University
Research output: Contribution to journal › Article › Research › peer-review
The redox activity of protein disulfide isomerase inhibits ALS phenotypes in cellular and zebrafish models
Parakh, S., Shadfar, S., Perri, E. R., Ragagnin, A. M. G., Piattoni, C. V., Fogolín, M. B., Yuan, K. C., Shahheydari, H., Don, E. K., Thomas, C. J., Hong, Y., Comini, M. A., Laird, A. S., Spencer, D. M. & Atkin, J. D., 22 May 2020, In: iScience. 23, 5, p. 1-27 44 p., 101097.
Macquarie University
Research output: Contribution to journal › Article › Research › peer-review

Open Access
Pathogenic mutation in the ALS/FTD gene, CCNF, causes elevated Lys48-linked ubiquitylation and defective autophagy.
Lee, A., Rayner, S. L., Gwee, S. S. L., De Luca, A., Shahheydari, H., Sundaramoorthy, V., Morsch, M., Hogan, A., Don, E., Williams, K., Yerbury, J. J., Blair, I., Atkin, J. D., Molloy, M. P. & Chung, R. S., 8 Feb 2019. 1 p.
Macquarie University
Research output: Contribution to conference › Abstract › Research › peer-review

Biography

Amyotrophic lateral sclerosis-linked UBQLN2 mutants inhibit endoplasmic reticulum to Golgi transport, leading to Golgi fragmentation and ER stress

The redox activity of protein disulfide isomerase inhibits ALS phenotypes in cellular and zebrafish models

Pathogenic mutation in the ALS/FTD gene, CCNF, causes elevated Lys48-linked ubiquitylation and defective autophagy.