Structural basis for the enzymatic resistance of the GM2 ganglioside.
Department of Biochemistry, Tulane University Health Sciences Center, School of Medicine, 1430 Tulane Avenue, New Orleans, Louisiana 70112, USA.
Yu-Teh
YT
Li
Su-Chen
SC
Li
Hideharu
H
Ishida
Makoto
M
Kiso
Laura
L
Raimondi
Anna
A
Bernardi
Sandro
S
Sonnino
D002240:Carbohydrate Sequence; D003013:Clostridium / Q000201:enzymology; D003198:Computer Simulation; D049289:G(M2) Activator Protein; D005678:G(M2) Ganglioside / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009439:Neuraminidase / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D013816:Thermodynamics; D001619:beta-N-Acetylhexosaminidases / Q000378:metabolism
D049289:G(M2) Activator Protein; D009844:Oligosaccharides; D011506:Proteins; D005678:G(M2) Ganglioside; D009439:Neuraminidase; D001619:beta-N-Acetylhexosaminidases