Hypophosphorylated neurofilament subunits undergo axonal transport more rapidly than more extensively phosphorylated subunits in situ

Cell Motility and the Cytoskeleton

Volumn 47, Issue 2, 2000, Pages 120-129

  Stephens, R E ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Axonal transport; Neurofilaments (NFs); Phosphorylation

Indexed keywords

NEUROFILAMENT PROTEIN; PROTEIN SUBUNIT;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CYTOSKELETON; DENSITOMETRY; DEPHOSPHORYLATION; MOUSE; NERVE FIBER TRANSPORT; NEUROFILAMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION;

ANIMAL; AXONAL TRANSPORT; AXONS; BLOTTING, WESTERN; MICE; MOLECULAR WEIGHT; NEUROFILAMENT PROTEINS; PEPTIDES; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PROTEIN ISOFORMS; PROTEIN SUBUNITS; RETINAL GANGLION CELLS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

ANIMALIA;

EID: 0033810408     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0169(200010)47:2<120::AID-CM3>3.0.CO;2-6     Document Type: Article

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