Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Sujan Devkota"'
Autor:
Sujan Devkota, Rui Zhou, Vaishnavi Nagarajan, Masato Maesako, Hung Do, Arshad Noorani, Caitlin Overmeyer, Sanjay Bhattarai, Justin T. Douglas, Anita Saraf, Yinglong Miao, Brian D. Ackley, Yigong Shi, Michael S. Wolfe
Publikováno v:
Cell Reports, Vol 43, Iss 2, Pp 113761- (2024)
Summary: Mutations that cause familial Alzheimer’s disease (FAD) are found in amyloid precursor protein (APP) and presenilin, the catalytic component of γ-secretase, that together produce amyloid β-peptide (Aβ). Nevertheless, whether Aβ is the
Externí odkaz:
https://doaj.org/article/946405b54cfb4ca6ae682b16e8ead2ff
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-14 (2023)
Gaussian accelerated molecular dynamics (GaMD) simulations and biochemical experiments in E.Coli provide mechanistic insight into how Presenilin-1 familial Alzheimer’s disease mutations affect structural dynamics and enzyme-substrate interactions o
Externí odkaz:
https://doaj.org/article/662f47a2fd4549069b6a0b27e86c9dd0
Publikováno v:
ACS Central Science, Vol 6, Iss 6, Pp 969-983 (2020)
Externí odkaz:
https://doaj.org/article/bbbf83652e3240fc89040e3623db3a1f
Autor:
Apurba Bhattarai, Sujan Devkota, Hung Nguyen Do, Jinan Wang, Sanjay Bhattarai, Michael S. Wolfe, Yinglong Miao
Publikováno v:
J Am Chem Soc
The membrane-embedded γ-secretase complex processively cleaves within the transmembrane domain of amyloid precursor protein (APP) to produce 37-to-43-residue amyloid β-peptides (Aβ) of Alzheimer’s disease (AD). Despite its importance in pathogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8975fe7e7e76c8a2d349d0c983986029
https://pubmed.ncbi.nlm.nih.gov/35544328
https://pubmed.ncbi.nlm.nih.gov/35544328
Autor:
Sameer Gautam, Sujan Devkota
Publikováno v:
Journal of Business and Social Sciences. 3:111-120
Most of the banks and financial institutions of Nepal have been moving towards the e-Banking system as all of them want to increase customer satisfaction and relationship (especially in terms of time), scope, and transaction facilities. The scope of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1258315a071cde880fbf6a5653378d55
https://doi.org/10.3126/jbss.v3i1.40859
https://doi.org/10.3126/jbss.v3i1.40859
Autor:
Michael S. Wolfe, Minli Xing, Kathleen M. Meneely, Justin T. Douglas, Sujan Devkota, Sanjay Bhattarai
Publikováno v:
J Am Chem Soc
γ-Secretase is a membrane-embedded aspartyl protease complex central in biology and medicine. How this enzyme recognizes transmembrane substrates and catalyzes hydrolysis in the lipid bilayer is unclear. Inhibitors that mimic the entire substrate tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad1e6a05d0f7d44041cdd4a617830765
https://doi.org/10.1021/jacs.9b13405
https://doi.org/10.1021/jacs.9b13405
Publikováno v:
Biophysical Journal. 122:507a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60b7b8aa06fa797aae4f38cba973f78b
https://doi.org/10.1016/j.bpj.2022.11.2701
https://doi.org/10.1016/j.bpj.2022.11.2701
Publikováno v:
J Med Chem
γ-Secretase, a membrane-embedded aspartyl protease complex with presenilin as the catalytic component, cleaves within the transmembrane domain (TMD) of its many substrates, which include the amyloid precursor protein (APP) of Alzheimer9s disease (AD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ef8c5e4bebed4de3ab60a34d8e6e63c
https://doi.org/10.1101/2021.08.05.455313
https://doi.org/10.1101/2021.08.05.455313
Autor:
Michael S. Wolfe, Hung Nguyen Do, Apurba Bhattarai, Yinglong Miao, Sujan Devkota, Sanjay Bhattarai, Jinan Wang
The membrane-embedded γ-secretase complex processively cleaves within the transmembrane domain of amyloid precursor protein (APP) to produce 37-to-43-residue amyloid β-peptides (Aβ) of Alzheimer’s disease (AD). Despite its importance in pathogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05d1c45a4c1cf4f6ef35da39c52a26b1
https://doi.org/10.1101/2021.08.05.455243
https://doi.org/10.1101/2021.08.05.455243