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chromosome 22q deletion

Parkinson's chromosome deletion linked to other genetic disorders

Researchers, led by BRC-supported Professor Nicholas Wood, UCL Institute of Neurology, have made a breakthrough in their understanding of Parkinson’s disease after they discovered a chromosome deletion linked to Parkinson’s disease and other genetic disorders. More...

Prof John Hardy

Prof John Hardy is the first UK winner of $3m Breakthrough Prize in Life Sciences

Professor John Hardy (UCL Institute of Neurology) has been awarded the $3 million Breakthrough Prize in Life Sciences for his pioneering research into the genetic causes of Alzheimer’s disease, other forms of dementia and Parkinson’s disease. More...

John Hardy, PhD, right, accepted the 2015 Robert A. Pritzker Prize from MJFF VP Brian Fiske, PhD, and Michael J. Fox on April 15.

John Hardy awarded 2015 Robert A. Pritzker Prize for Leadership in Parkinson's Research

One of the UK Parkinson's Disease Consortium Principal Investigators, Prof John Hardy, has been awarded the 2015 Robert A. Pritzker Prize for his leadership in Parkinson's genetics research. The award was presented by Michael J. Fox at a ceremony in New York on April 15. From the Michael J. Fox Foundation website: More...

Webcast - Prof Nicholas Wood - Advances in Genetic Understanding of Parkinson's Disease.

Video: Advances in Genetic Understanding of Parkinson's Disease

Webcast of the presentation entitled ‘Advances in Genetic Understanding of Parkinson's Disease’ given by Nicholas Wood (University College London, United Kingdom) presented at the Biochemical Society Hot Topic event, PINK1-Parkin Signalling in Parkinson’s Disease and Beyond, held in December 2014. More...

Pedigrees and I-FP-CIT SPECT scan images of the four families with GCH1 mutations involved in this study.

GCH1 gene and Parkinson's risk

A study published in Brain, led by researchers at UCL Institute of Neurology, has shown that genetic mutations which cause a decrease in dopamine production in the brain and lead to a form of childhood-onset Dystonia, also play a role in the development of Parkinson’s disease.

Adamantios Mamais

(Research Associate)

Adamantios Mamais

I hold a multi-disciplinary research background having had the opportunity to study and investigate many aspects of cell biology leading to human disease. Having completed a BSc in Molecular Biology at University College London in 2001, I pursued an MSc in Molecular Medicine, at the same university, that equipped me with a deeper understanding of the underlying mechanisms and consequences that give rise to pathology, when the blue-prints of nature go wrong.

My academic studies cultivated my enthusiasm on the molecular events of human disease, while I had the chance to work on proteins involved in gastrulation and synaptic neurotransmission, and also tumour targeting drugs, during my BSc/MSc research projects respectively. During a summer placement at the UCL Institute of Neurology I was involved in a project investigating the mechanistics of filopodia formation in developing neurons. I then joined the Institute of Cancer Research for two years as a Scientific Officer to investigate nucleosomal positioning and chromatin remodelling mechanisms in V(D)J recombination. In 2005 I focused my research skills and experience in pursuing a PhD at the UCL Institute of Neurology, in the lab of Prof Louis Lim and Dr Christine Hall, investigating novel mechanisms of interplay between cytoskeletal remodelling factors involved in neuronal differentiation and mRNA binding factors involved in local translation in axons and formation of Stress Granules.

In 2010, I joined the team of Dr Rina Bandopadhyay and Dr Patrick Lewis at the Reta Lila Weston Institute, UCL Institute of Neurology, as a post-doc Research Associate, and I am currently investigating the molecular events that underlie LRRK2 associated Parkinson’s disease. My research utilises the invaluable resource of post-mortem human brain tissue from Parkinson’s cases, provided by the Queen Square Brain Bank. We are focusing on the post-translational modifications and neuropathological features of two LRRK2 putative partners in disease, a-Synuclein and 4E-BP1. Furthermore, I have initiated a novel project investigating the role of mutated LRRK2 in mRNA Stress Granule formation, recently involved in pathologic protein aggregation in neurodegenerative diseases.

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Number of items: 15.


Dusonchet, J; Li, H; Guillily, M; Liu, M; Stafa, K; Derada Troletti, C; Boon, JY; (2014) A Parkinson's disease gene regulatory network identifies the signaling protein RGS2 as a modulator of LRRK2 activity and neuronal toxicity. Hum Mol Genet , 23 (18) 4887 - 4905. 10.1093/hmg/ddu202.


Brelstaff, J; Mamais, A; Lashley, T; Holton, JL; Revesz, T; Bandopadhyay, R; (2013) The aggregate proteins of FTLD-FUS are re-localised to stress granules upon oxidative stress. In: (Proceedings) 114th Meeting of the British-Neuropathological-Society / Symposium on Advances in Motor Neuron Diseases. (pp. pp. 46-47). WILEY-BLACKWELL

Manzoni, C; Mamais, A; Dihanich, S; Tooze, S; Bandopadhyay, R; Lewis, PA; (2013) LRRK2 regulates autophagy. In: (Proceedings) 114th Meeting of the British-Neuropathological-Society / Symposium on Advances in Motor Neuron Diseases. (pp. p. 10). WILEY-BLACKWELL


Devine, MJ; Kaganovich, A; Ryten, M; Mamais, A; Trabzuni, D; Manzoni, C; McGoldrick, P; (2012) Correction: Pathogenic LRRK2 Mutations Do Not Alter Gene Expression in Cell Model Systems or Human Brain Tissue. PLOS ONE , 7 (1) , Article e22489. 10.1371/annotation/c12e4f9e-5aae-424b-a69f-fddf16976dc5. Green open access

Trancikova, A; Mamais, A; Webber, PJ; Stafa, K; Tsika, E; Glauser, L; West, AB; (2012) Phosphorylation of 4E-BP1 in the mammalian brain is not altered by LRRK2 expression or pathogenic mutations. PLoS One , 7 (10) , Article e47784. 10.1371/journal.pone.0047784. Green open access



Ahmed, Z; Doherty, KM; Silveira-Moriyama, L; Bandopadhyay, R; Lashley, T; Mamais, A; Hondhamuni, G; (2011) Globular glial tauopathies (GGT) presenting with motor neuron disease or frontotemporal dementia: an emerging group of 4-repeat tauopathies. ACTA NEUROPATHOL , 122 (4) 415 - 428. 10.1007/s00401-011-0857-4.

Bandopadhyay, R; Mamais, A; Lashley, T; Griffiths, C; Goswami, N; Holton, JL; Revesz, T; (2011) The role of 4E-BP1, a putative LRRK2 interactor in the pathology of IPD and in G2019S LRRK2 mutation cases. In: NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY. (pp. 21 - 21). WILEY-BLACKWELL PUBLISHING, INC

Devine, MJ; Kaganovich, A; Ryten, M; Mamais, A; Trabzuni, D; Manzoni, C; McGoldrick, P; (2011) Pathogenic LRRK2 Mutations Do Not Alter Gene Expression in Cell Model Systems or Human Brain Tissue. PLOS ONE , 6 (7) , Article e22489. 10.1371/journal.pone.0022489. Green open access


Bandopadhyay, R; Phan, B; Mamais, A; Lashley, T; Lees, A; (2010) Validation of 4E-BP1 as a Putative LRRK2 Substrate: In Vivo Evidence. In: MOVEMENT DISORD. (pp. S629 - S629). WILEY-LISS

Mamais, A.; (2010) Investigation of an N5-glutamine methyltranferase, a novel partner of α2-chimaerin. Doctoral thesis, UCL (University College London). Green open access


Heckman, CA; Demuth, JG; Deters, D; Malwade, SR; Cayer, ML; Monfries, C; Mamais, A; (2009) Relationship of p21-Activated Kinase (PAK) and Filopodia to Persistence and Oncogenic Transformation. J CELL PHYSIOL , 220 (3) 576 - 585. 10.1002/jcp.21788.


Nightingale, KP; Baumann, M; Eberharter, A; Mamais, A; Becker, PB; Boyes, J; (2007) Acetylation increases access of remodelling complexes to their nucleosome targets to enhance initiation of V(D)J recombination. NUCLEIC ACIDS RES , 35 (18) 6311 - 6321. 10.1093/nar/gkm650. Gold open access


Baumann, M; Mamais, A; McBlane, F; Xiao, H; Boyes, J; (2003) Regulation of V(D)J recombination by nucleosome positioning at recombination signal sequences. EMBO J , 22 (19) 5197 - 5207.


Cowan, DA; Russell, NJ; Mamais, A; Sheppard, DM; (2002) Antarctic Dry Valley mineral soils contain unexpectedly high levels of microbial biomass. EXTREMOPHILES , 6 (5) 431 - 436. 10.1007/s00792-002-002-0276-5.

This list was generated on Sun Oct 23 17:12:47 2016 BST.