Sonam Parakh

Dr

  • 335 Citations
  • 7 h-Index
20132019
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Research Outputs 2013 2019

  • 335 Citations
  • 7 h-Index
  • 8 Article
  • 5 Review article
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Article
2019

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., 4 Dec 2019, In : Cellular and Molecular Life Sciences. 15 p.

Research output: Contribution to journalArticleResearchpeer-review

Endoplasmic Reticulum Stress
Amyotrophic Lateral Sclerosis
Endoplasmic Reticulum
Protein Transport
Endoplasmic Reticulum-Associated Degradation

Protein disulphide isomerase is associated with mutant SOD1 in canine degenerative myelopathy

Chang, R. C., Parakh, S., Coates, J. R., Long, S. & Atkin, J. D., 2 Jan 2019, In : NeuroReport. 30, 1, p. 8-13 6 p.

Research output: Contribution to journalArticleResearchpeer-review

Protein Disulfide-Isomerases
Spinal Cord Diseases
Canidae
Amyotrophic Lateral Sclerosis
Endoplasmic Reticulum Stress
2018

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

Parakh, S., Jagaraj, C. J., Vidal, M., Ragagnin, A. M. G., Perri, E. R., Konopka, A., Toth, R. P., Galper, J., Blair, I. P., Thomas, C. J., Walker, A. K., Yang, S., Spencer, D. M. & Atkin, J. D., 15 Apr 2018, In : Human molecular genetics. 27, 8, p. 1311-1331 21 p.

Research output: Contribution to journalArticleResearchpeer-review

Amyotrophic Lateral Sclerosis
Endoplasmic Reticulum Stress
Pathology
Apoptosis
DNA-Binding Proteins
2016

Efficacy of peptide nucleic acid and selected conjugates against specific cellular pathologies of amyotrophic lateral sclerosis

Browne, E. C., Parakh, S., Duncan, L. F., Langford, S. J., Atkin, J. D. & Abbott, B. M., 1 Apr 2016, In : Bioorganic and Medicinal Chemistry. 24, 7, p. 1520-1527 8 p.

Research output: Contribution to journalArticleResearchpeer-review

Peptide Nucleic Acids
Amyotrophic Lateral Sclerosis
Pathology
Superoxide Dismutase
Nucleic acid sequences
2015

Novel roles for protein disulphide isomerase in disease states: a double edged sword?

Parakh, S. & Atkin, J. D., 2015, In : Frontiers in cell and developmental biology. 3, p. 1-11 11 p., 30.

Research output: Contribution to journalArticleResearchpeer-review

Open Access
File
Protein Disulfide-Isomerases
Post Translational Protein Processing
Endoplasmic Reticulum
Oxidation-Reduction

Rab1-dependent ER-Golgi transport dysfunction is a common pathogenic mechanism in SOD1, TDP-43 and FUS-associated ALS

Soo, K. Y., Halloran, M., Sundaramoorthy, V., Parakh, S., Toth, R. P., Southam, K. A., McLean, C. A., Lock, P., King, A., Farg, M. A. & Atkin, J. D., 1 Nov 2015, In : Acta Neuropathologica. 130, 5, p. 679-697 19 p.

Research output: Contribution to journalArticleResearchpeer-review

Amyotrophic Lateral Sclerosis
Endoplasmic Reticulum
Protein Transport
Motor Neurons
Endoplasmic Reticulum Stress

The unfolded protein response and the role of Protein Disulfide Isomerase in neurodegeneration

Perri, E. R., Thomas, C. J., Parakh, S., Spencer, D. M. & Atkin, J. D., 2015, In : Frontiers in cell and developmental biology. 3, p. 1-17 17 p., 80.

Research output: Contribution to journalArticleResearchpeer-review

Open Access
File
Protein Disulfide-Isomerases
Unfolded Protein Response
Endoplasmic Reticulum Stress
Endoplasmic Reticulum
Neurodegenerative Diseases
2013

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

Walker, A. K., Soo, K. Y., Sundaramoorthy, V., Parakh, S., Ma, Y., Farg, M. A., Wallace, R. H., Crouch, P. J., Turner, B. J., Horne, M. K. & Atkin, J. D., 29 Nov 2013, In : PLoS ONE. 8, 11, p. 1-12 12 p., e81170.

Research output: Contribution to journalArticleResearchpeer-review

Open Access
File
Endoplasmic Reticulum Stress
DNA-binding proteins
Amyotrophic Lateral Sclerosis
DNA-Binding Proteins
endoplasmic reticulum