Results 11 to 20 of about 72,088 (314)

The Neuronal Adaptor Protein X11α Interacts with the Copper Chaperone for SOD1 and Regulates SOD1 Activity [PDF]

Journal of Biological Chemistry, 2001
The neuronal adaptor protein X11alpha participates in the formation of multiprotein complexes and intracellular trafficking. It contains a series of discrete protein-protein interaction domains including two contiguous C-terminal PDZ domains. We used the yeast two-hybrid system to screen for proteins that interact with the PDZ domains of human X11alpha,
Declan M. McLoughlin, Claire L. Standen, Kwok‐Fai Lau, Steven Ackerley, Thomas P. Bartnikas, Jonathan D. Gitlin, Christopher C.J. Miller   +6 more
openalex   +7 more sources

Specific analysis of SOD1 enzymatic activity in CSF from ALS patients with and without SOD1 mutations

Neurobiology of Disease
Mutations in superoxide dismutase-1 (SOD1) are a cause of hereditary amyotrophic lateral sclerosis (ALS) through a gain-of-function mechanism involving unfolded mutant SOD1.
Laura Leykam, Karin M.E. Forsberg, Ulrika Nordström, Karin Hjertkvist, Agneta Öberg, Eva Jonsson, Peter M. Andersen, Stefan L. Marklund, Per Zetterström   +8 more
doaj   +4 more sources

Copper Sources for Sod1 Activation [PDF]

Antioxidants, 2020
Copper ions (i.e., copper) are a critical part of several cellular processes, but tight regulation of copper levels and trafficking are required to keep the cell protected from this highly reactive transition metal. Cu, Zn superoxide dismutase (Sod1) protects the cell from the accumulation of radical oxygen species by way of the redox cycling activity ...
Stefanie D. Boyd, Morgan S. Ullrich, Amelie Skopp, Duane D. Winkler   +3 more
openaire   +4 more sources

Cancer grows on SOD1 [PDF]

Science-Business eXchange, 2008
Researchers from Attenuon have found that SOD1 is a master regulatory switch for kinase phosphorylation involved in angiogenesis and cell proliferation. SOD1 thus is a potential target for a variety of cancers and might have some utility in degenerative diseases as well.
Michael J. Haas
openalex   +3 more sources

Tryptophan residues in TDP-43 and SOD1 mediate the cross-seeding and toxicity of SOD1 [PDF]

Journal of Biological Chemistry, 2020
ABSTRACTAmyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease of motor neurons. Neuronal superoxide dismutase-1 (SOD1) inclusion bodies are characteristic of familial ALS with SOD1 mutations, while a hallmark of sporadic ALS is inclusions containing aggregated wild-type TAR DNA-binding protein 43 (TDP-43).
Edward Pokrishevsky, Michèle G. DuVal, Luke McAlary, Sarah Louadi, Silvia Pozzi, Andrei Roman, Steven S Plotkin, Anke Dijkstra, Jean-Pierre Julien, W. Ted Allison, Neil R. Cashman   +10 more
openaire   +3 more sources

Structures of mouse SOD1 and human/mouse SOD1 chimeras [PDF]

Archives of Biochemistry and Biophysics, 2010
Mutations in human copper-zinc superoxide dismutase (SOD1) cause an inherited form of amyotrophic lateral sclerosis (ALS). Inclusions enriched in pathogenic SOD1 accumulate in the spinal cords of transgenic mice expressing these proteins, but endogenous mouse SOD1 is not found as a component of these aggregates.
Alexander B. Taylor, S.V. Seetharaman, P. John Hart, P. John Hart, Stephen P. Holloway   +4 more
openaire   +3 more sources

Dorfin Ubiquitylates Mutant SOD1 and Prevents Mutant SOD1-mediated Neurotoxicity [PDF]

Journal of Biological Chemistry, 2002
Amyotrophic lateral sclerosis (ALS) is a progressive paralytic disorder resulting from the degeneration of motor neurons in the cerebral cortex, brainstem, and spinal cord. The cytopathological hallmark in the remaining motor neurons of ALS is the presence of ubiquitylated inclusions consisting of insoluble protein aggregates.
Keiji Tanaka, Jun-ichi Niwa, Shinsuke Ishigaki, Shigeo Murata, Naoyuki Taniguchi, Gen Sobue, Nozomi Hishikawa, Masahiko Yamamoto, Manabu Doyu   +8 more
openaire   +3 more sources

Adherent Monomer-Misfolded SOD1

PLoS ONE, 2008
Multiple cellular functions are compromised in amyotrophic lateral sclerosis (ALS). In familial ALS (FALS) with Cu/Zn superoxide dismutase (SOD1) mutations, the mechanisms by which the mutation in SOD1 leads to such a wide range of abnormalities remains elusive.To investigate underlying cellular conditions caused by the SOD1 mutation, we explored ...
Yasuhiro Watanabe, Eri Morita, Yasuyo Fukada, Koji Doi, Kenichi Yasui, Michio Kitayama, Toshiya Nakano, Kenji Nakashima   +7 more
openalex   +6 more sources

Anti-SOD1 Nanobodies That Stabilize Misfolded SOD1 Proteins Also Promote Neurite Outgrowth in Mutant SOD1 Human Neurons

International Journal of Molecular Sciences, 2022
ALS-linked mutations induce aberrant conformations within the SOD1 protein that are thought to underlie the pathogenic mechanism of SOD1-mediated ALS. Although clinical trials are underway for gene silencing of SOD1, these approaches reduce both wild-type and mutated forms of SOD1.
Meenakshi Sundaram Kumar, Megan E. Fowler-Magaw, Daniel Kulick, Sivakumar Boopathy, Del Hayden Gadd, Melissa Rotunno, Catherine Douthwright, Diane Golebiowski, Issa Yusuf, Zuoshang Xu, Robert H. Brown, Miguel Sena-Esteves, Alison L. O'Neil, Daryl A. Bosco   +13 more
openaire   +3 more sources

Molecular and pharmacological chaperones for SOD1 [PDF]

Biochemical Society Transactions, 2020
The efficacy of superoxide dismutase-1 (SOD1) folding impacts neuronal loss in motor system neurodegenerative diseases. Mutations can prevent SOD1 post-translational processing leading to misfolding and cytoplasmic aggregation in familial amyotrophic lateral sclerosis (ALS).
openaire   +2 more sources