Reactions of Hydrogen Peroxide with Familial Amyotrophic Lateral Sclerosis Mutant Human Copper-Zinc Superoxide Dismutases Studied by Pulse Radiolysis

Pulse Radiolysis ◽

Superoxide Dismutases ◽

Copper Zinc ◽

Loss of in Vitro Metal Ion Binding Specificity in Mutant Copper-Zinc Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis

Journal of Biological Chemistry ◽

10.1074/jbc.275.2.1007 ◽

2000 ◽

Vol 275 (2) ◽

pp. 1007-1014 ◽

Cited By ~ 120

Author(s):

Joy J. Goto ◽

Haining Zhu ◽

Raylene J. Sanchez ◽

Aram Nersissian ◽

Edith Butler Gralla ◽

...

Keyword(s):

Metal Ion ◽

Superoxide Dismutases ◽

Ion Binding ◽

Metal Ion Binding ◽

Copper Zinc ◽

Nonamyloid Aggregates Arising from Mature Copper/Zinc Superoxide Dismutases Resemble Those Observed in Amyotrophic Lateral Sclerosis

Journal of Biological Chemistry ◽

10.1074/jbc.m110.113696 ◽

2010 ◽

Vol 285 (53) ◽

pp. 41701-41711 ◽

Cited By ~ 39

Author(s):

Young-Mi Hwang ◽

Peter B. Stathopulos ◽

Kristin Dimmick ◽

Hong Yang ◽

Hamid R. Badiei ◽

...

Keyword(s):

Superoxide Dismutases ◽

Copper Zinc ◽

Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni2+- and other metal-ion-substituted wild-type copper–zinc superoxide dismutases

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-014-1126-5 ◽

2014 ◽

Vol 19 (4-5) ◽

pp. 647-657 ◽

Cited By ~ 6

Author(s):

Li-June Ming ◽

Joan Selverstone Valentine

Keyword(s):

Metal Ion ◽

Superoxide Dismutases ◽

Wild Type ◽

Nmr Studies ◽

Copper Zinc ◽

Dysregulation of intracellular copper trafficking pathway in a mouse model of mutant copper/zinc superoxide dismutase-linked familial amyotrophic lateral sclerosis

Journal of Neurochemistry ◽

10.1111/j.1471-4159.2009.06310.x ◽

2009 ◽

Vol 111 (1) ◽

pp. 181-191 ◽

Cited By ~ 38

Author(s):

Eiichi Tokuda ◽

Eriko Okawa ◽

Shin-ichi Ono

Keyword(s):

Superoxide Dismutase ◽

Copper Trafficking ◽

Trafficking Pathway ◽

Copper Zinc ◽

Lateral Sclerosis ◽

Intracellular Copper

Human Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis

Protein Misfolding, Aggregation, and Conformational Diseases - Protein Reviews ◽

10.1007/978-0-387-36534-3_16 ◽

2007 ◽

pp. 327-344 ◽

Cited By ~ 1

Author(s):

Ahmad Galaleldeen ◽

P. John Hart

Keyword(s):

Superoxide Dismutase ◽

Copper Zinc ◽

Gain in functions of mutant Cu,Zn-superoxide dismutases as a causative factor in familial amyotrophic lateral sclerosis: Less reactive oxidant formation but high spontaneous aggregation and precipitation

Free Radical Research ◽

10.1080/10715760000300621 ◽

2000 ◽

Vol 33 (1) ◽

pp. 65-73 ◽

Cited By ~ 19

Author(s):

Ayako Okado-Matsumoto ◽

Theingi Myint ◽

Junichi Fujii ◽

Naoyuki Taniguchi

Keyword(s):

Causative Factor ◽

Superoxide Dismutases ◽

Spontaneous Aggregation ◽

Reactive Oxidant ◽

Neuroprotective effects of copper/zinc-dependent superoxide dismutase against a wide variety of death-inducing stimuli and proapoptotic effect of familial amyotrophic lateral sclerosis mutations

Molecular Brain Research ◽

10.1016/s0169-328x(02)00560-0 ◽

2002 ◽

Vol 109 (1-2) ◽

pp. 189-197 ◽

Cited By ~ 5

Author(s):

Yogesh Patel ◽

Yolanda Collaco Moraes ◽

David Latchman ◽

Robert Coffin ◽

Jacqueline de Belleroche

Keyword(s):

Superoxide Dismutase ◽

Neuroprotective Effects ◽

Copper Zinc ◽

Reduced net charge and heterogeneity of pIisoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase

Electrophoresis ◽

10.1002/elps.201500187 ◽

2015 ◽

Vol 36 (19) ◽

pp. 2482-2488 ◽

Cited By ~ 9

Author(s):

Stéphane Roudeau ◽

Sylviane Chevreux ◽

Asuncion Carmona ◽

Richard Ortega

Keyword(s):

Superoxide Dismutase ◽

Net Charge ◽

Copper Zinc ◽

Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis

Neurodegenerative Diseases and Metal Ions ◽

10.1002/0470028114.ch8 ◽

2006 ◽

pp. 179-205

Author(s):

Lisa J. Whitson ◽

P. John Hart

Keyword(s):

Superoxide Dismutase ◽

Copper Zinc ◽

Faculty Opinions recommendation of Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1012344.185335 ◽

2003 ◽

Author(s):

Elizabeth Theil

Keyword(s):

Superoxide Dismutase ◽

Nmr Spectroscopy ◽

Dynamic Properties ◽

Copper Zinc ◽