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of 12
pro vyhledávání: '"Helen R. Broom"'
Autor:
Ashok Sekhar, Jessica AO Rumfeldt, Helen R Broom, Colleen M Doyle, Guillaume Bouvignies, Elizabeth M Meiering, Lewis E Kay
Publikováno v:
eLife, Vol 4 (2015)
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease involving cytotoxic conformations of Cu, Zn superoxide dismutase (SOD1). A major challenge in understanding ALS disease pathology has been the identification and atomic-le
Externí odkaz:
https://doaj.org/article/3e6f47c6b96f48569f57e0bce025c0fc
Autor:
Harmeen K, Deol, Helen R, Broom, Bruna, Siebeneichler, Brenda, Lee, Zoya, Leonenko, Elizabeth M, Meiering
Publikováno v:
Biophysical Chemistry. 288:106844
Protein misfolding and aggregation are hallmarks of many diseases, including amyotrophic lateral sclerosis (ALS). In familial ALS, aberrant self-association of mutant Cu,Zn-superoxide dismutase (SOD1) is implicated as a key contributor to disease. Mu
Autor:
Elizabeth M. Meiering, Ashok Sekhar, Colleen M. Doyle, Jessica A.O. Rumfeldt, Helen R. Broom, Lewis E. Kay
Publikováno v:
Biochemistry. 55:1346-1361
The chemical shifts of backbone amide protons in proteins are sensitive reporters of local structural stability and conformational heterogeneity, which can be determined from their readily measured linear and nonlinear temperature-dependences, respec
Publikováno v:
Protein Science. 24:2081-2089
Neurotoxic misfolding of Cu, Zn‐superoxide dismutase (SOD1) is implicated in causing amyotrophic lateral sclerosis, a devastating and incurable neurodegenerative disease. Disease‐linked mutations in SOD1 have been proposed to promote misfolding a
Publikováno v:
Essays in Biochemistry. 56:149-165
ALS (amyotrophic lateral sclerosis) is a fatal neurodegenerative syndrome characterized by progressive paralysis and motor neuron death. Although the pathological mechanisms that cause ALS remain unclear, accumulating evidence supports that ALS is a
Autor:
Jessica A.O. Rumfeldt, Johnathan J. Almey, Helen R. Broom, Elizabeth M. Meiering, Peter B. Stathopulos, Colleen M. Doyle, Kenrick A. Vassall, Aron Broom
Publikováno v:
Archives of Biochemistry and Biophysics. 531:44-64
In nature, proteins most often exist as complexes, with many of these consisting of identical subunits. Understanding of the energetics governing the folding and misfolding of such homooligomeric proteins is central to understanding their function an
Autor:
Elizabeth M. Meiering, Lewis E. Kay, Ashok Sekhar, Jessica A.O. Rumfeldt, Ryan E. Sobering, Colleen M. Doyle, Helen R. Broom
Publikováno v:
Proceedings of the National Academy of Sciences. 113
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that, in some cases, has been linked with mutations to the antioxidant metalloenzyme superoxide dismutase (SOD1). Although the mature form of this enzyme is highly stable and resistan
Autor:
Laurine Legroux, Helen R. Broom, Neil R. Cashman, Elizabeth M. Meiering, Sabrina Semmler, Laurie Destroismaisons, Christine Vande Velde, Sarah Pickles, Nathalie Arbour
Publikováno v:
Acta Neuropathologica Communications
Approximately 20 % of familial Amyotrophic Lateral Sclerosis (ALS) is caused by mutations in superoxide dismutase (SOD1), which leads to misfolding of the SOD1 protein, resulting in a toxic gain of function. Several conformation-restricted antibodies
Autor:
Kenrick A. Vassall, Ming Sze Tong, Helen R. Broom, Colleen M. Doyle, Elizabeth M. Meiering, Jessica A.O. Rumfeldt, Julia Maeve Bonner
Publikováno v:
Biochemistry. 55(3)
Many proteins are naturally homooligomers, homodimers most frequently. The overall stability of oligomeric proteins may be described in terms of the stability of the constituent monomers and the stability of their association; together, these stabili
Autor:
Lewis E. Kay, Ashok Sekhar, Helen R. Broom, Colleen M. Doyle, Jessica A.O. Rumfeldt, Elizabeth M. Meiering, Guillaume Bouvignies
Publikováno v:
eLife, Vol 4 (2015)
eLife
eLife, 2015, 4, pp.e08679. ⟨10.7554/eLife.07296⟩
eLife, eLife Sciences Publication, 2015, 4, pp.e08679. ⟨10.7554/eLife.07296⟩
eLife
eLife, 2015, 4, pp.e08679. ⟨10.7554/eLife.07296⟩
eLife, eLife Sciences Publication, 2015, 4, pp.e08679. ⟨10.7554/eLife.07296⟩
International audience; Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease involving cytotoxic conformations of Cu, Zn superoxide dismutase (SOD1). A major challenge in understanding ALS disease pathology has been the iden