The University of Queensland

Early activation of cellular stress and death pathways caused by cytoplasmic TDP-43 in the rNLS8 mouse model of ALS and FTD

Luan, Wei, Wright, Amanda L., Brown-Wright, Heledd, Le, Sheng, San Gil, Rebecca, Madrid San Martin, Lidia, Ling, Karen, Jafar-Nejad, Paymaan, Rigo, Frank and Walker, Adam K. (2023). Early activation of cellular stress and death pathways caused by cytoplasmic TDP-43 in the rNLS8 mouse model of ALS and FTD. Molecular Psychiatry, 28 (6), 2445-2461. doi: 10.1038/s41380-023-02036-9

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Keating, Sean S., Bademosi, Adekunle T., San Gil, Rebecca and Walker, Adam K. (2023). Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43. Cellular and Molecular Life Sciences, 80 (4) 95, 1-23. doi: 10.1007/s00018-023-04739-2

TDP-43 pathology: from noxious assembly to therapeutic removal

Keating, Sean S., San Gil, Rebecca, Swanson, Molly E.V., Scotter, Emma L. and Walker, Adam K. (2022). TDP-43 pathology: from noxious assembly to therapeutic removal. Progress in Neurobiology, 211 102229, 102229. doi: 10.1016/j.pneurobio.2022.102229

Application of WGCNA and PloGO2 in the analysis of complex proteomic data

Wu, Jemma X., Pascovici, Dana, Wu, Yunqi, Walker, Adam K. and Mirzaei, Mehdi (2023). Application of WGCNA and PloGO2 in the analysis of complex proteomic data. Statistical analysis of proteomic data: methods and tools. (pp. 375-390) edited by Thomas Burger. New York, NY, United States: Humana Press. doi: 10.1007/978-1-0716-1967-4_17

Endoplasmic reticulum stress and protein misfolding in amyotrophic lateral sclerosis

Walker, A. K., Turner, B. J. and Atkin, J. D. (2009). Endoplasmic reticulum stress and protein misfolding in amyotrophic lateral sclerosis. Protein Misfolding Disorders: A Trip into the ER. (pp. 56-76) edited by K. Walker, A., J. Turner, B. and D. Atkin, J.. Bentham Science Publishers Ltd.. doi: 10.2174/978160805013010901010056

A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration

San Gil, Rebecca, Pascovici, Dana, Venturato, Juliana, Brown-Wright, Heledd, Mehta, Prachi, Madrid San Martin, Lidia, Wu, Jemma, Luan, Wei, Chui, Yi Kit, Bademosi, Adekunle T., Swaminathan, Shilpa, Naidoo, Serey, Berning, Britt A., Wright, Amanda L., Keating, Sean S., Curtis, Maurice A., Faull, Richard L. M., Lee, John D., Ngo, Shyuan T., Lee, Albert, Morsch, Marco, Chung, Roger S., Scotter, Emma, Lisowski, Leszek, Mirzaei, Mehdi and Walker, Adam K. (2024). A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration. Nature Communications, 15 (1) 1508. doi: 10.1038/s41467-024-45646-9

UndERACting ion channels in neurodegeneration

Jacobs, Matisse T., San Gil, Rebecca and Walker, Adam K. (2023). UndERACting ion channels in neurodegeneration. Trends in Neurosciences, 47 (2), 87-89. doi: 10.1016/j.tins.2023.11.002

Microglial CD68 and L-ferritin upregulation in response to phosphorylated-TDP-43 pathology in the amyotrophic lateral sclerosis brain

Swanson, Molly E.V., Mrkela, Miran, Murray, Helen C., Cao, Maize C., Turner, Clinton, Curtis, Maurice A., Faull, Richard L.M., Walker, Adam K. and Scotter, Emma L. (2023). Microglial CD68 and L-ferritin upregulation in response to phosphorylated-TDP-43 pathology in the amyotrophic lateral sclerosis brain. Acta Neuropathologica Communications, 11 (1) 69, 1-22. doi: 10.1186/s40478-023-01561-6

Early activation of cellular stress and death pathways caused by cytoplasmic TDP-43 in the rNLS8 mouse model of ALS and FTD

Luan, Wei, Wright, Amanda L., Brown-Wright, Heledd, Le, Sheng, San Gil, Rebecca, Madrid San Martin, Lidia, Ling, Karen, Jafar-Nejad, Paymaan, Rigo, Frank and Walker, Adam K. (2023). Early activation of cellular stress and death pathways caused by cytoplasmic TDP-43 in the rNLS8 mouse model of ALS and FTD. Molecular Psychiatry, 28 (6), 2445-2461. doi: 10.1038/s41380-023-02036-9

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Keating, Sean S., Bademosi, Adekunle T., San Gil, Rebecca and Walker, Adam K. (2023). Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43. Cellular and Molecular Life Sciences, 80 (4) 95, 1-23. doi: 10.1007/s00018-023-04739-2

Cryptic inclusions UNCover losses driving neurodegeneration

Bademosi, Adekunle T. and Walker, Adam K. (2022). Cryptic inclusions UNCover losses driving neurodegeneration. Trends in Genetics, 38 (9), 889-891. doi: 10.1016/j.tig.2022.06.004

TDP-43 pathology: from noxious assembly to therapeutic removal

Keating, Sean S., San Gil, Rebecca, Swanson, Molly E.V., Scotter, Emma L. and Walker, Adam K. (2022). TDP-43 pathology: from noxious assembly to therapeutic removal. Progress in Neurobiology, 211 102229, 102229. doi: 10.1016/j.pneurobio.2022.102229

Impaired glymphatic function in the early stages of disease in a TDP-43 mouse model of amyotrophic lateral sclerosis

Zamani, Akram, Walker, Adam K., Rollo, Ben, Ayers, Katie L., Farah, Raysha, O’Brien, Terence J. and Wright, David K. (2022). Impaired glymphatic function in the early stages of disease in a TDP-43 mouse model of amyotrophic lateral sclerosis. Translational Neurodegeneration, 11 (1) 17, 1-11. doi: 10.1186/s40035-022-00291-4

Early and progressive dysfunction revealed by in vivo neurite imaging in the rNLS8 TDP-43 mouse model of ALS

Zamani, Akram, Walker, Adam K., Rollo, Ben, Ayers, Katie L., Farah, Raysha, O'Brien, Terence J. and Wright, David K. (2022). Early and progressive dysfunction revealed by in vivo neurite imaging in the rNLS8 TDP-43 mouse model of ALS. NeuroImage: Clinical, 34 103016, 103016. doi: 10.1016/j.nicl.2022.103016

miR-23a suppression accelerates functional decline in the rNLS8 mouse model of TDP-43 proteinopathy

Tsitkanou, Stavroula, Della Gatta, Paul A., Abbott, Gavin, Wallace, Marita A., Lindsay, Angus, Gerlinger-Romero, Frederico, Walker, Adam K., Foletta, Victoria C. and Russell, Aaron P. (2022). miR-23a suppression accelerates functional decline in the rNLS8 mouse model of TDP-43 proteinopathy. Neurobiology of Disease, 162 105559, 105559. doi: 10.1016/j.nbd.2021.105559

Riluzole does not ameliorate disease caused by cytoplasmic TDP‐43 in a mouse model of amyotrophic lateral sclerosis

Wright, Amanda L., Della Gatta, Paul A., Le, Sheng, Berning, Britt A., Mehta, Prachi, Jacobs, Kelly R., Gul, Hossai, San Gil, Rebecca, Hedl, Thomas J., Riddell, Winonah R., Watson, Owen, Keating, Sean S., Venturato, Juliana, Chung, Roger S., Atkin, Julie D., Lee, Albert, Shi, Bingyang, Blizzard, Catherine A., Morsch, Marco and Walker, Adam K. (2021). Riluzole does not ameliorate disease caused by cytoplasmic TDP‐43 in a mouse model of amyotrophic lateral sclerosis. European Journal of Neuroscience, 54 (6) ejn.15422, 6237-6255. doi: 10.1111/ejn.15422

Mislocalisation of TDP-43 to the cytoplasm causes cortical hyperexcitability and reduced excitatory neurotransmission in the motor cortex

Dyer, Marcus S., Reale, Laura A., Lewis, Katherine E., Walker, Adam K., Dickson, Tracey C., Woodhouse, Adele and Blizzard, Catherine A. (2021). Mislocalisation of TDP-43 to the cytoplasm causes cortical hyperexcitability and reduced excitatory neurotransmission in the motor cortex. Journal of Neurochemistry, 157 (4), 1300-1315. doi: 10.1111/jnc.15214

Unbiased label-free quantitative proteomics of cells expressing Amyotrophic Lateral Sclerosis (ALS) mutations in CCNF reveals activation of the apoptosis pathway: a workflow to screen pathogenic gene mutations

Cheng, Flora, De Luca, Alana, Hogan, Alison L., Rayner, Stephanie L., Davidson, Jennilee M., Watchon, Maxinne, Stevens, Claire H., Muñoz, Sonia Sanz, Ooi, Lezanne, Yerbury, Justin J., Don, Emily K., Fifita, Jennifer A., Villalva, Maria D., Suddull, Hannah, Chapman, Tyler R., Hedl, Thomas J., Walker, Adam K., Yang, Shu, Morsch, Marco, Shi, Bingyang, Blair, Ian P., Laird, Angela S., Chung, Roger S. and Lee, Albert (2021). Unbiased label-free quantitative proteomics of cells expressing Amyotrophic Lateral Sclerosis (ALS) mutations in CCNF reveals activation of the apoptosis pathway: a workflow to screen pathogenic gene mutations. Frontiers in Molecular Neuroscience, 14 627740, 1-18. doi: 10.3389/fnmol.2021.627740

Impaired NHEJ repair in amyotrophic lateral sclerosis is associated with TDP-43 mutations

Konopka, Anna, Whelan, Donna R., Jamali, Md Shafi, Perri, Emma, Shahheydari, Hamideh, Toth, Reka P., Parakh, Sonam, Robinson, Tina, Cheong, Alison, Mehta, Prachi, Vidal, Marta, Ragagnin, Audrey M G, Khizhnyak, Ivan, Jagaraj, Cyril J., Galper, Jasmin, Grima, Natalie, Deva, Anand, Shadfar, Sina, Nicholson, Garth A., Yang, Shu, Cutts, Suzanne M., Horejsi, Zuzana, Bell, Toby D M, Walker, Adam K., Blair, Ian P. and Atkin, Julie D. (2020). Impaired NHEJ repair in amyotrophic lateral sclerosis is associated with TDP-43 mutations. Molecular neurodegeneration, 15 (1) 51, 51. doi: 10.1186/s13024-020-00386-4

Neurodegenerative disease-associated protein aggregates are poor inducers of the heat shock response in neuronal cells

Gil, R. San, Cox, D., McAlary, L., Berg, T., Walker, A. K., Yerbury, J. J., Ooi, L. and Ecroyd, H. (2020). Neurodegenerative disease-associated protein aggregates are poor inducers of the heat shock response in neuronal cells. Journal of Cell Science, 133 (15), 1-15. doi: 10.1242/jcs.243709

Workflow for rapidly extracting biological insights from complex, multicondition proteomics experiments with WGCNA and PloGO2

Wu, Jemma X., Pascovici, Dana, Wu, Yunqi, Walker, Adam K. and Mirzaei, Mehdi (2020). Workflow for rapidly extracting biological insights from complex, multicondition proteomics experiments with WGCNA and PloGO2. Journal of Proteome Research, 19 (7), 2898-2906. doi: 10.1021/acs.jproteome.0c00198

Correction: The cysteine (Cys) residues Cys-6 and Cys-111 in mutant superoxide dismutase 1 (SOD1) A4V are required for induction of endoplasmic reticulum stress in amyotrophic lateral sclerosis

Perri, Emma R., Parakh, Sonam, Vidal, Marta, Mehta, Prachi, Ma, Yi, Walker, Adam K. and Atkin, Julie D. (2020). Correction: The cysteine (Cys) residues Cys-6 and Cys-111 in mutant superoxide dismutase 1 (SOD1) A4V are required for induction of endoplasmic reticulum stress in amyotrophic lateral sclerosis. Journal of Molecular Neuroscience, 70 (9), 1369-1369. doi: 10.1007/s12031-020-01617-5

The cysteine (Cys) residues Cys-6 and Cys-111 in mutant superoxide dismutase 1 (SOD1) A4V are required for induction of endoplasmic reticulum stress in amyotrophic lateral sclerosis

Perri, Emma R., Parakh, Sonam, Vidal, Marta, Mehta, Prachi, Ma, Yi, Walker, Adam K. and Atkin, Julie D. (2020). The cysteine (Cys) residues Cys-6 and Cys-111 in mutant superoxide dismutase 1 (SOD1) A4V are required for induction of endoplasmic reticulum stress in amyotrophic lateral sclerosis. Journal of Molecular Neuroscience, 70 (9), 1357-1368. doi: 10.1007/s12031-020-01551-6

Proteomics approaches for biomarker and drug target discovery in ALS and FTD

Hedl, Thomas J., San Gil, Rebecca, Cheng, Flora, Rayner, Stephanie L., Davidson, Jennilee M., De Luca, Alana, Villalva, Maria D., Ecroyd, Heath, Walker, Adam K. and Lee, Albert (2019). Proteomics approaches for biomarker and drug target discovery in ALS and FTD. Frontiers in Neuroscience, 13 (JUN) 548, 548. doi: 10.3389/fnins.2019.00548

Label-free fluorescent poly(amidoamine) dendrimer for traceable and controlled drug delivery

Wang, Guoying, Fu, Libing, Walker, Adam, Chen, Xianfeng, Lovejoy, David B., Hao, Mingcong, Lee, Albert, Chung, Roger, Rizos, Helen, Irvine, Mal, Zheng, Meng, Liu, Xiuhua, Lu, Yiqing and Shi, Bingyang (2019). Label-free fluorescent poly(amidoamine) dendrimer for traceable and controlled drug delivery. Biomacromolecules, 20 (5), 2148-2158. doi: 10.1021/acs.biomac.9b00494

The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD

Berning, Britt A. and Walker, Adam K. (2019). The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD. Frontiers in Neuroscience, 13 (APR) 335, 335. doi: 10.3389/fnins.2019.00335

Genetic and immunopathological analysis of CHCHD10 in Australian amyotrophic lateral sclerosis and frontotemporal dementia and transgenic TDP-43 mice

McCann, Emily P., Fifita, Jennifer A., Grima, Natalie, Galper, Jasmin, Mehta, Prachi, Freckleton, Sarah E., Zhang, Katharine Y., Henden, Lyndal, Hogan, Alison L., Chan Moi Fat, Sandrine, Wu, Sharlynn S.L., Jagaraj, Cyril J., Berning, Britt A., Williams, Kelly Louise, Twine, Natalie A., Bauer, Denis, Piguet, Olivier, Hodges, John, Kwok, John B.J., Halliday, Glenda M., Kiernan, Matthew C., Atkin, Julie, Rowe, Dominic B., Nicholson, Garth A., Walker, Adam K., Blair, Ian P. and Yang, Shu (2019). Genetic and immunopathological analysis of CHCHD10 in Australian amyotrophic lateral sclerosis and frontotemporal dementia and transgenic TDP-43 mice. Journal of Neurology, Neurosurgery and Psychiatry, 91 (2), 162-2019. doi: 10.1136/jnnp-2019-321790

Stilbenes from Veratrum maackii Regel protect against ethanol-induced DNA damage in mouse cerebellum and cerebral cortex

Wu, Yantong, Li, Shasha, Liu, Jinjin, Liu, Xiping, Ruan, Weimin, Lu, Jengwei, Liu, Yong, Lawson, Tom, Shimoni, Olga, Lovejoy, David B., Walker, Adam K., Cong, Yue and Shi, Bingyang (2018). Stilbenes from Veratrum maackii Regel protect against ethanol-induced DNA damage in mouse cerebellum and cerebral cortex. ACS Chemical Neuroscience, 9 (7), 1616-1624. doi: 10.1021/acschemneuro.8b00006

ERp57 is protective against mutant SOD1-induced cellular pathology in amyotrophic lateral sclerosis

Parakh, Sonam, Jagaraj, Cyril J., Vidal, Marta, Ragagnin, Audrey M. G., Perri, Emma R., Konopka, Anna, Toth, Reka P., Galper, Jasmin, Blair, Ian P., Thomas, Colleen J., Walker, Adam K., Yang, Shu, Spencer, Damian M. and Atkin, Julie D. (2018). ERp57 is protective against mutant SOD1-induced cellular pathology in amyotrophic lateral sclerosis. Human Molecular Genetics, 27 (8), 1311-1331. doi: 10.1093/hmg/ddy041

Casein kinase II phosphorylation of cyclin F at serine 621 regulates the Lys48-ubiquitylation E3 ligase activity of the SCF(cyclin F) complex

Lee, Albert, Rayner, Stephanie L., De Luca, Alana, Gwee, Serene S. L., Morsch, Marco, Sundaramoorthy, Vinod, Shahheydari, Hamideh, Ragagnin, Audrey, Shi, Bingyang, Yang, Shu, Williams, Kelly L., Don, Emily K., Walker, Adam K., Zhang, Katharine Y., Yerbury, Justin J., Cole, Nicholas J., Atkin, Julie D., Blair, Ian P., Molloy, Mark P. and Chung, Roger S. (2017). Casein kinase II phosphorylation of cyclin F at serine 621 regulates the Lys48-ubiquitylation E3 ligase activity of the SCF(cyclin F) complex. Open Biology, 7 (10) 170058, 170058. doi: 10.1098/rsob.170058

Erratum: Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis (Human molecular genetics (2015) 24 13 (3830-3846))

Sundaramoorthy, Vinod, Walker, Adam K., Tan, Vanessa, Fifita, Jennifer A., Mccann, Emily P., Williams, Kelly L., Blair, Ian P., Guillemin, Gilles J., Farg, Manal A. and Atkin, Julie D. (2017). Erratum: Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis (Human molecular genetics (2015) 24 13 (3830-3846)). Human Molecular Genetics, 26 (17), 3452-3452. doi: 10.1093/hmg/ddx268

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

Lee, Albert, Rayner, Stephanie L., Gwee, Serene S. L., De Luca, Alana, Shahheydari, Hamideh, Sundaramoorthy, Vinod, Ragagnin, Audrey, Morsch, Marco, Radford, Rowan, Galper, Jasmin, Freckleton, Sarah, Shi, Bingyang, Walker, Adam K., Don, Emily K., Cole, Nicholas J., Yang, Shu, Williams, Kelly L., Yerbury, Justin J., Blair, Ian P., Atkin, Julie D., Molloy, Mark P. and Chung, Roger S. (2017). Pathogenic mutation in the ALS/FTD gene, CCNF, causes elevated Lys48-linked ubiquitylation and defective autophagy. Cellular and Molecular Life Sciences, 75 (2), 335-354. doi: 10.1007/s00018-017-2632-8

Protein quality control and the amyotrophic lateral sclerosis/frontotemporal dementia continuum

Shahheydari, Hamideh, Ragagnin, Audrey, Walker, Adam K., Toth, Reka P., Vidal, Marta, Jagaraj, Cyril J., Perri, Emma R., Konopka, Anna, Sultana, Jessica M. and Atkin, Julie D. (2017). Protein quality control and the amyotrophic lateral sclerosis/frontotemporal dementia continuum. Frontiers in Molecular Neuroscience, 10 119, 1-25. doi: 10.3389/fnmol.2017.00119

An insoluble frontotemporal lobar degeneration-associated TDP-43 C-terminal fragment causes neurodegeneration and hippocampus pathology in transgenic mice

Walker, Adam K., Tripathy, Kalyan, Restrepo, Clark R., Ge, Guanghui, Xu, Yan, Kwong, Linda K., Trojanowski, John Q. and Lee, Virginia M. -Y. (2015). An insoluble frontotemporal lobar degeneration-associated TDP-43 C-terminal fragment causes neurodegeneration and hippocampus pathology in transgenic mice. Human Molecular Genetics, 24 (25), 7241-7254. doi: 10.1093/hmg/ddv424

Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43

Walker, Adam K., Spiller, Krista J., Ge, Guanghui, Zheng, Allen, Xu, Yan, Zhou, Melissa, Tripathy, Kalyan, Kwong, Linda K., Trojanowski, John Q. and Lee, Virginia M. -Y. (2015). Functional recovery in new mouse models of ALS/FTLD after clearance of pathological cytoplasmic TDP-43. Acta Neuropathologica, 130 (5), 643-660. doi: 10.1007/s00401-015-1460-x

Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis

Sundaramoorthy, Vinod, Walker, Adam K., Tan, Vanessa, Fifita, Jennifer A., Mccann, Emily P., Williams, Kelly L., Blair, Ian P., Guillemin, Gilles J., Farg, Manal A. and Atkin, Julie D. (2015). Defects in optineurin- and myosin VI-mediated cellular trafficking in amyotrophic lateral sclerosis. Human Molecular Genetics, 24 (13), 3830-3846. doi: 10.1093/hmg/ddv126

Astrocytic TDP-43 pathology in Alexander disease

Walker, Adam K., Daniels, Christine M. LaPash, Goldman, James E., Trojanowski, John Q., Lee, Virginia M. -Y. and Messing, Albee (2014). Astrocytic TDP-43 pathology in Alexander disease. Journal of Neuroscience, 34 (19), 6448-6458. doi: 10.1523/JNEUROSCI.0248-14.2014

Mutant SOD1 inhibits ER-Golgi transport in amyotrophic lateral sclerosis

Atkin, Julie D., Farg, Manal A., Soo, Kai Ying, Walker, Adam K., Halloran, Mark, Turner, Bradley J., Nagley, Phillip and Horne, Malcolm K. (2014). Mutant SOD1 inhibits ER-Golgi transport in amyotrophic lateral sclerosis. Journal of Neurochemistry, 129 (1), 190-204. doi: 10.1111/jnc.12493

Novel monoclonal antibodies to normal and pathologically altered human TDP-43 proteins

Kwong, Linda K., Irwin, David J., Walker, Adam K., Xu, Yan, Riddle, Dawn M, Trojanowski, John Q. and Lee, Virginia M. Y. (2014). Novel monoclonal antibodies to normal and pathologically altered human TDP-43 proteins. Acta Neuropathologica Communications, 2 (1) 33. doi: 10.1186/2051-5960-2-33

ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation

Walker, Adam K., Soo, Kai Y., Sundaramoorthy, Vinod, Parakh, Sonam, Ma, Yi, Farg, Manal A., Wallace, Robyn H., Crouch, Peter J., Turner, Bradley J., Horne, Malcolm K. and Atkin, Julie D. (2013). ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS One, 8 (11) e81170, e81170.1-e81170.12. doi: 10.1371/journal.pone.0081170

Extracellular wildtype and mutant SOD1 induces ER-Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells

Sundaramoorthy, Vinod, Walker, Adam K., Yerbury, Justin, Soo, Kai Ying, Farg, Manal A., Hoang, Vy, Zeineddine, Rafaa, Spencer, Damian and Atkin, Julie D. (2013). Extracellular wildtype and mutant SOD1 induces ER-Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells. Cellular and Molecular Life Sciences, 70 (21), 4181-4195. doi: 10.1007/s00018-013-1385-2

N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2)

Walker, Adam K., Soo, Kai Ying, Levina, Vita, Talbo, Gert H. and Atkin, Julie D. (2013). N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2). FEBS Journal, 280 (1), 233-243. doi: 10.1111/febs.12063

Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase

Farg, Manal A., Soo, Kai Y., Walker, Adam K., Pham, Hong, Orian, Jacqueline, Horne, Malcolm K., Warraich, Sadaf T., Williams, Kelly L., Blair, Ian P. and Atkin, Julie D. (2012). Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiology of Aging, 33 (12), 2855-2868. doi: 10.1016/j.neurobiolaging.2012.02.009

Bim links ER stress and apoptosis in cells expressing mutant SOD1 associated with amyotrophic lateral sclerosis

Soo, Kai Y., Atkin, Julie D., Farg, Manal, Walker, Adam K., Horne, Malcolm K. and Nagley, Phillip (2012). Bim links ER stress and apoptosis in cells expressing mutant SOD1 associated with amyotrophic lateral sclerosis. PLoS One, 7 (4) e35413, e35413. doi: 10.1371/journal.pone.0035413

Stress signaling from the endoplasmic reticulum: a central player in the pathogenesis of amyotrophic lateral sclerosis

Walker, Adam K. and Atkin, Julie D. (2011). Stress signaling from the endoplasmic reticulum: a central player in the pathogenesis of amyotrophic lateral sclerosis. IUBMB Life, 63 (9), 754-763. doi: 10.1002/iub.520

Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis

Walker, Adam K. and Atkin, Julie D. (2011). Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis. Neurology Research International, 2011 317340. doi: 10.1155/2011/317340

Protein disulfide isomerase and the endoplasmic reticulum in amyotrophic lateral sclerosis

Walker, Adam K. (2010). Protein disulfide isomerase and the endoplasmic reticulum in amyotrophic lateral sclerosis. Journal of Neuroscience, 30 (11), 3865-3867. doi: 10.1523/JNEUROSCI.0408-10.2010

Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis

Walker, Adam K., Farg, Manal A., Bye, Chris R., McLean, Catriona A., Horne, Malcolm K. and Atkin, Julie D. (2010). Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis. Brain, 133 (1), 105-116. doi: 10.1093/brain/awp267

Redefining the role of metallothionein within the injured brain: Extracellular metallothioneins play an important role in the astrocyte-neuron response to injury

Chung, Roger S., Penkowa, Milena, Dittmann, Justin, King, Carolyn E., Bartlett, Carole, Asmussen, Johanne W., Hidalgo, Juan, Carrasco, Javier, Leung, Yee Kee J., Walker, Adam K., Fung, Samantha J., Dunlop, Sarah A., Fitzgerald, Melinda, Beazley, Lyn D., Chuah, Meng I., Vickers, James C. and West, Adrian K. (2008). Redefining the role of metallothionein within the injured brain: Extracellular metallothioneins play an important role in the astrocyte-neuron response to injury. Journal of Biological Chemistry, 283 (22), 15349-15358. doi: 10.1074/jbc.M708446200

Metallothionein expression by NG2 glial cells following CNS injury

Chung, R. S., Fung, S. J., Leung, Y. K., Walker, A. K., McCormack, G. H., Chuah, M. I., Vickers, J. C. and West, A. K. (2007). Metallothionein expression by NG2 glial cells following CNS injury. Cellular and Molecular Life Sciences, 64 (19-20), 2716-2722. doi: 10.1007/s00018-007-7267-8

Applying novel human iPSC-derived neuronal models to investigate modulators of TDP-43 pathology

Jacobs, Matisse, Gil, Rebecca San and Walker, Adam K. (2023). Applying novel human iPSC-derived neuronal models to investigate modulators of TDP-43 pathology. HOBOKEN: WILEY.