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ProMIS Neurosciences Inc PMN

ProMIS Neurosciences Inc. is a development stage biotechnology company. The Company is focused on generating and developing antibody therapeutics selectively targeting toxic misfolded proteins in neurodegenerative diseases such as Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS) and multiple system atrophy (MSA), an alpha-synucleinopathy. Its proprietary target discovery engine applies a thermodynamic, computational discovery platform - ProMIS and Collective Coordinates - to predict novel targets known as Disease Specific Epitopes on the molecular surface of misfolded proteins. Using this approach, the Company is developing novel antibody therapeutics for AD, ALS and MSA. Its product portfolio includes PMN310 / Amyloid-beta, PMN267 / TDP-43, and PMN442 / Alpha-synuclein. The Company plans to investigate additional synucleinopathies, including Parkinson's disease (PD) and dementia with Lewy bodies (DLB). Its wholly owned subsidiary is ProMIS Neurosciences (US) Inc.


NDAQ:PMN - Post by User

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Post by retiredcopon May 09, 2018 11:51pm
80 Views
Post# 28009276

Who is Dr. Neil. Cashman ....

Who is Dr. Neil. Cashman ....
It’s a bit dated ( possibly 2006) but gives you a peek into the amazing person...you can probabaly add a few pages to his bio at this point in time....


Dr. Neil Cashman 
University of British Columbia

Position:
Professor
Division:
Neurology

I have made many contributions to understanding of prion diseases for over 20 years, significantly including the discovery that the normal cellular isoform of the prion protein participates in cell activation (Cashman et al, Cell 1990) and lymphoid differentiation (Dodelet and Cashman, Blood 1998). These and other papers have been considered foundational in the new science of prion neuroimmunology, and have also been cited by scientists and policy makers as evidence for the prion infectablity of peripheral lymphoid and bone marrow cells.  More recently, I have identified an immunological epitope unique to the disease-associated isoform of the prion protein, with potential for use in non-invasive diagnosis and treatment of the prion disorders (Paramithiotis et al, Nature Medicine 2003; Cashman and Caughey, Nature Reviews in Drug Discovery 2004; Griffin and Cashman Expert Opinion on Biological Therapeutics 2006). Other recent prion work includes the identification of a cell surface receptor for these proteins (patent pending), copolymer-based therapies for prion disease (patent awarded), a prion peptide experimental system for studying amyloid formation (Zou et al, Europ Biochem 2001), an enhanced in vitro prion protein conversion system (Zou and Cashman, J Biol Chem 2002; patent pending), and the development of a novel method for detecting aggregated misfolded proteins, including prions, named Epitope Protection (patent pending). As a clinical neurologist concerned with the public health impact of newly emerging prion diseases, I have published numerous well-cited medical articles on this subject (e.g., Cashman CMAJ 1997; Coulthart and Cashman CMAJ 2001). I co-founded in 1998 the Canadian CJD Surveillance System, and I have I have made many contributions to understanding of prion diseases for over 20 years, significantly including the discovery that the normal cellular isoform of the prion protein participates in cell activation (Cashman et al, Cell 1990) and lymphoid differentiation (Dodelet and Cashman, Blood 1998). These and other papers have been considered foundational in the new science of prion neuroimmunology, and have also been cited by scientists and policy makers as evidence for the prion infectablity of peripheral lymphoid and bone marrow cells.  More recently, I have identified an immunological epitope unique to the disease-associated isoform of the prion protein, with potential for use in non-invasive diagnosis and treatment of the prion disorders (Paramithiotis et al, Nature Medicine 2003; Cashman and Caughey, Nature Reviews in Drug Discovery 2004; Griffin and Cashman Expert Opinion on Biological Therapeutics 2006). Other recent prion work includes the identification of a cell surface receptor for these proteins (patent pending), copolymer-based therapies for prion disease (patent awarded), a prion peptide experimental system for studying amyloid formation (Zou et al, Europ Biochem 2001), an enhanced in vitro prion protein conversion system (Zou and Cashman, J Biol Chem 2002; patent pending), and the development of a novel method for detecting aggregated misfolded proteins, including prions, named Epitope Protection (patent pending). As a clinical neurologist concerned with the public health impact of newly emerging prion diseases, I have published numerous well-cited medical articles on this subject (e.g., Cashman CMAJ 1997; Coulthart and Cashman CMAJ 2001). I co-founded in 1998 the Canadian CJD Surveillance System, and I have served as an expert for the Canadian government and international industry on these diseases (e.g., the “”Cashman Report”” on risks of transmission of prion disease through blood and blood products for Health Canada 1999, McDonald’s Corporation Scientific Advisory Committee since 2001).  I am the Scientific Director of PrioNet Canada, a Network of Centres of Excellence awarded in November 2005. Caprion Pharmaceuticals in Montreal was initially founded in 1998 to commercialize my prion discoveries. Amorfix Life Sciences was founded in 2004 to commercialize my work in detection and treatment of protein misfolding diseases, including prion disorders and other neurodegenerative diseases. I am Chief Scientific Officer of Amorfix, which became public on the TSX-V exchange in October 2005, and now has a market capitalization of ~CAD 50 M. Both Caprion and Amorfix technology emerged from programs originally funded by CIHR.

 

 






 


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