Zobrazeno 1 - 10
of 148
pro vyhledávání: '"Siddhartha Banerjee"'
Publikováno v:
Small Science, Vol 4, Iss 9, Pp n/a-n/a (2024)
Aggregation of the amyloid β (Aβ) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the
Externí odkaz:
https://doaj.org/article/61d4412c1b96452a8533fabeadc49861
Autor:
Shailendra Dhakal, Malay Mondal, Azin Mirzazadeh, Siddhartha Banerjee, Ayanjeet Ghosh, Vijayaraghavan Rangachari
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-16 (2023)
Abstract Many neurodegenerative diseases including frontotemporal lobar degeneration (FTLD), Lewy body disease (LBD), multiple system atrophy (MSA), etc., show colocalized deposits of TDP-43 and α-synuclein (αS) aggregates. To understand whether th
Externí odkaz:
https://doaj.org/article/b54d2c6e33c74fd2b5960b342efeba33
Publikováno v:
Journal of Applied Science and Engineering, Vol 26, Iss 10, Pp 1501-1511 (2023)
Unwanted text messages are called Spam SMSs. It has been proven that Machine Learning Models can categorize spam messages efficiently and with great accuracy. However, the lack of proper spam filtering software or misclassification of genuine SMS as
Externí odkaz:
https://doaj.org/article/c836b9475c0c48d5a91735f46a56ea7c
Autor:
Shailendra Dhakal, Malay Mondal, Azin Mirzazadeh, Siddhartha Banerjee, Ayanjeet Ghosh, Vijayaraghavan Rangachari
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-2 (2024)
Externí odkaz:
https://doaj.org/article/ac1246ef73364b59bd895923ec6a702b
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 6, p 5175 (2023)
The aggregation of amyloid beta (Aβ) into fibrillar aggregates is a key feature of Alzheimer’s disease (AD) pathology. β-carotene and related compounds have been shown to associate with amyloid aggregates and have direct impact on the formation o
Externí odkaz:
https://doaj.org/article/8ef3ffabf2f642cfb136dfca81c50be1
Autor:
Natalie Landeck, Katherine E. Strathearn, Daniel Ysselstein, Kerstin Buck, Sayan Dutta, Siddhartha Banerjee, Zhengjian Lv, John D. Hulleman, Jagadish Hindupur, Li-Kai Lin, Sonal Padalkar, Lia A. Stanciu, Yuri L. Lyubchenko, Deniz Kirik, Jean-Christophe Rochet
Publikováno v:
Molecular Neurodegeneration, Vol 15, Iss 1, Pp 1-23 (2020)
Abstract Background α-Synuclein (aSyn) aggregation is thought to play a central role in neurodegenerative disorders termed synucleinopathies, including Parkinson’s disease (PD). Mouse aSyn contains a threonine residue at position 53 that mimics th
Externí odkaz:
https://doaj.org/article/577ae13724214a3bac084228b03fe4b4
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 5, p 2803 (2022)
The effects of membranes on the early-stage aggregation of amyloid β (Aβ) have come to light as potential mechanisms by which neurotoxic species are formed in Alzheimer’s disease. We have shown that direct Aβ-membrane interactions dramatically e
Externí odkaz:
https://doaj.org/article/c189bac471c449abbaba402130830fd4
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 3, p 1129 (2020)
The self-assembly of amyloid β (Aβ) proteins into oligomers is the major pathogenic event leading to Alzheimer’s disease (AD). Typical in vitro experiments require high protein concentrations, whereas the physiological concentration of Aβ is in
Externí odkaz:
https://doaj.org/article/70e793bbefd5490c9f84c19c5acb2265
Autor:
Siddhartha Banerjee
Publikováno v:
Iraqi Journal of Science. :4601-4608
A quantitative description of microstructure governs the characteristics of the material. Various heat and excellent treatments reveal micro-structures when the material is prepared. Depending on the microstructure, mechanical properties like hardnes
Autor:
Siddhartha Banerjee, Brooke Holcombe, Sydney Ringold, Abigail Foes, Tanmayee Naik, Divya Baghel, Ayanjeet Ghosh
Publikováno v:
J Phys Chem B
Amyloid plaques are one of the central manifestations of Alzheimer’s disease pathology. Aggregation of the amyloid beta (Aβ) protein from amorphous oligomeric species to mature fibrils has been extensively studied. However, structural heterogeneit