N-acetyl-D-glucosamine kinase binds dynein light chain roadblock 1 and promotes protein aggregate clearance
EDIT: please see PB comment below
nature.com/articles/s41419-...
michaeljfox.org/grant/glyco...
These results suggest that O-GlcNAc may be a cellular strategy to prevent protein aggregation, which could potentially be exploited for treatment.
pnas.org/doi/10.1073/pnas.1...
I’m not sure if this is the same or similar enough to reap the claimed benefits.
Regarding the first reference, N-acetyl-glucosamine kinase is not the same as N-acetyl-glucosamine: en.wikipedia.org/wiki/N-ace...
The third reference is favorable. However, here is a study that finds N-acetyl-glucosamine unfavorable: faseb.onlinelibrary.wiley.c...
Increased O-GlcNAcylation Attenuates Autophagic Flux, Induces Mitochondrial Dysfunction and Leads to Accumulation of Alpha-Synuclein in Neurons
" found significantly increased O-GlcNAcylation levels in PD brains compared to control. Whether increased O-GlcNAcylation affects neuronal function and survival was then tested in rat primary cortical neurons. We found that thiamet G... significantly increased protein O-GlcNAcylation, decreased autophagic flux, decreased mitochondrial complex IV activities, increased accumulation of mitochondrial peroxynitrite, and led to an increased α-synuclein accumulation. To confirm our results in vivo, ... We found that dnOGA synaptosomes exhibited increased O-GlcNAcylation, decreased mitochondrial function, increased α-synuclein, and accumulation of autophagosomes. Taken together we proposed that a significant increase of O-GlcNAcylation levels in PD brains may contribute to impairment of neuronal bioenergetics and attenuation of autophagic activities and accumulation of α-synuclein."
what about the MJFF link?
Alpha-synuclein is a sticky protein that clumps in the brains of people with Parkinson's disease (PD). N-acetyl-glucosamine (O-GlcNAc), a sugar-like molecule, can modify (become attached to) alpha-synuclein in a process called glycosylation. This raises the possibility that the number of modifications -- O-GlcNAc molecules attached to a single alpha-synuclein protein -- may, in turn, affect alpha-synuclein clumping. We have used chemical methods to produce alpha-synuclein with one O-GlcNAc modification. We found that this modification can completely block clumping, making alpha-synuclein less toxic in vitro. Finally, we discovered that O-GlcNAc prevents clumping by blocking the entry of new individual alpha-synuclein proteins into a growing clump. Together, these findings indicate that drugs that increase the number of O-GlcNAc modifications could slow the progression of PD.”
The one you linked to is post mortem and rats and mice. MJFF was just a test tube.
The third I posted which was “favorable” is the most recent, Stanford 2018.
Not sure if this deserves further research
It is okay for what it is but it does not carry the same level of confidence as a study published in a peer-reviewed journal. Be that as it may, we have got conflicting information here. I am in no position to judge which parties have it right. Under these circumstances I could not recommend taking this substance.
Among the many PD fighting effects of melatonin, reducing Asyn excretion and aggregation is on the list :
assets.researchsquare.com/f...
ncbi.nlm.nih.gov/pmc/articl...
Perhaps Melatonin + NAG, may have synergy toward this end.
Art
Why exercise slows progression of PD: reduces α-synuclein aggregation
Same Mistake in Parkinson's Research as in Alzheimer's Research?
Whey Protein vs Vegetable Protein 
protein v Sinemet….
