Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Noel D. Lazo"'
Publikováno v:
ACS Omega, Vol 3, Iss 10, Pp 13275-13282 (2018)
Externí odkaz:
https://doaj.org/article/6265c891d84e4abfa1539af4786b0543
Autor:
Qiuchen Zheng, Micheal T. Kebede, Bethany Lee, Claire A. Krasinski, Saadman Islam, Liliana A. Wurfl, Merc M. Kemeh, Valerie A. Ivancic, Charles E. Jakobsche, Donald E. Spratt, Noel D. Lazo
Publikováno v:
Antioxidants, Vol 10, Iss 9, p 1342 (2021)
The insulin-degrading enzyme (IDE) possesses a strong ability to degrade insulin and Aβ42 that has been linked to the neurodegeneration in Alzheimer’s disease (AD). Given this, an attractive IDE-centric strategy for the development of therapeutics
Externí odkaz:
https://doaj.org/article/a25d395273c14b41b4557b7a706bbf1a
Autor:
Qiuchen Zheng, Micheal T. Kebede, Merc M. Kemeh, Saadman Islam, Bethany Lee, Stuart D. Bleck, Liliana A. Wurfl, Noel D. Lazo
Publikováno v:
Molecules, Vol 24, Iss 12, p 2316 (2019)
The amyloid-β (Aβ) peptide and tau protein are thought to play key neuropathogenic roles in Alzheimer’s disease (AD). Both Aβ and tau self-assemble to form the two major pathological hallmarks of AD: amyloid plaques and neurofibrillary tangles,
Externí odkaz:
https://doaj.org/article/3ddb5dfa912c4ce083e42c48eb0be1fe
Autor:
Merc M Kemeh, Noel D Lazo
Publikováno v:
Neural Regeneration Research, Vol 19, Iss 9, Pp 1871-1872 (2024)
Externí odkaz:
https://doaj.org/article/6114bcf327f7437298bdb5c4df3064f4
Autor:
Qiuchen Zheng, Bethany Lee, Micheal T. Kebede, Valerie A. Ivancic, Merc M. Kemeh, Henrique Lemos Brito, Donald E. Spratt, Noel D. Lazo
Publikováno v:
ACS Omega. 7:24757-24765
Insulin-degrading enzyme (IDE) is an evolutionarily conserved ubiquitous zinc metalloprotease implicated in the efficient degradation of insulin monomer. However, IDE also degrades monomers of amyloidogenic peptides associated with disease, complicat
Autor:
Bocach Dd, Jillian E. Smith-Carpenter, Jones Kl, Bell Jm, Benjamin J. Alper, Noel D. Lazo, Zheng Q
Here we report proteolysis of synthetic acylated human ghrelin by recombinant human insulin-degrading enzyme (IDE). Kinetic parameters and sites of proteolytic cleavage were evaluated. Ghrelin proteolysis by IDE was inhibited by ethylenediaminetetraa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74d7b94763613848f06e651fec321a6a
https://doi.org/10.1101/2021.06.10.447714
https://doi.org/10.1101/2021.06.10.447714
Publikováno v:
Langmuir
The self-assembly of amyloidogenic peptides on membrane surfaces is associated with the death of neurons and β-cells in Alzheimer’s disease and type 2 diabetes, respectively. The early events of self-assembly in vivo are not known, but there is in
Publikováno v:
ACS Omega, Vol 3, Iss 10, Pp 13275-13282 (2018)
ACS Omega
ACS Omega
Alzheimer's disease (AD), the most common cause of dementia in the elderly, is the sixth leading cause of death in the United States. We hypothesize that the impaired clearance of Aβ42 from the brain is partly responsible for the onset of sporadic A
Autor:
Noel D. Lazo, Charles E. Jakobsche, Qiuchen Zheng, Donald E. Spratt, Claire A. Krasinski, Bethany Lee, Saadman Islam, Merc M. Kemeh, Micheal T. Kebede, Valerie A. Ivancic, Liliana A. Wurfl
Publikováno v:
Antioxidants
Volume 10
Issue 9
Antioxidants, Vol 10, Iss 1342, p 1342 (2021)
Volume 10
Issue 9
Antioxidants, Vol 10, Iss 1342, p 1342 (2021)
The insulin-degrading enzyme (IDE) possesses a strong ability to degrade insulin and Aβ42 that has been linked to the neurodegeneration in Alzheimer’s disease (AD). Given this, an attractive IDE-centric strategy for the development of therapeutics
Autor:
Noel D. Lazo, Merc M. Kemeh, Liliana A. Wurfl, Micheal T. Kebede, Saadman Islam, Bethany Lee, Qiuchen Zheng, Stuart D. Bleck
Publikováno v:
Molecules
Molecules, Vol 24, Iss 12, p 2316 (2019)
Molecules, Vol 24, Iss 12, p 2316 (2019)
The amyloid-β (Aβ) peptide and tau protein are thought to play key neuropathogenic roles in Alzheimer’s disease (AD). Both Aβ and tau self-assemble to form the two major pathological hallmarks of AD: amyloid plaques and neurofibrillary tangles,