Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 14, 1997, Pages 7606-7611

  Bruijn, L I ^a   Beal, M F ^c   Becher, M W ^b   Schulz, J B ^c   Wong, P C ^b   Price, D L ^b   Cleveland, D W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c MASSACHUSETTS GENERAL HOSPITAL   (United States)

Author keywords

Nitration; Peroxidation

Indexed keywords

HYDROXYL RADICAL; NITRO DERIVATIVE; SUPEROXIDE DISMUTASE; TYROSINE DERIVATIVE;

ADOLESCENT; AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; FAMILIAL DISEASE; GENE MUTATION; MOTOR NEURON DISEASE; MOUSE; NITRATION; NONHUMAN; PEROXIDATION; PRIORITY JOURNAL; SPINAL CORD; TRANSGENIC MOUSE;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; FREE RADICALS; HUMANS; MICE; MICE, TRANSGENIC; MUTATION; PROTEIN BINDING; SUPEROXIDE DISMUTASE; TYROSINE;

ANIMALIA; MUS MUSCULUS;

EID: 0030806228     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.14.7606     Document Type: Article

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