Turnover of oxidatively damaged nuclear proteins in BV-2 microglial cells is linked to their activation state by poly-ADP-ribose polymerase.
Ullrich
O
O
Department of Cell and Neurobiology, Institute of Anatomy, Medical Faculty (Charité), Humboldt-University Berlin, 10098 Berlin, Germany. oliver.ulrich@charite.de
Diestel
A
A
Bechmann
I
I
Homberg
M
M
Grune
T
T
Hass
R
R
Nitsch
R
R
D003374:Coumarins / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D017628:Microglia / Q000378:metabolism*; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism; D010084:Oxidation-Reduction; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex
D003374:Coumarins; D009097:Multienzyme Complexes; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D009842:Oligopeptides; C046582:succinyl-leucyl-leucyl-valyl-tyrosyl-methylcoumarinamide; D011065:Poly(ADP-ribose) Polymerases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex