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Akademický článek

Cross dimerization of amyloid-β and αsynuclein proteins in aqueous environment: a molecular dynamics simulations study.

Autor: Jaya C Jose, Prathit Chatterjee, Neelanjana Sengupta

Publikováno v: PLoS ONE, Vol 9, Iss 9, p e106883 (2014)

Self-assembly of the intrinsically unstructured proteins, amyloid beta (Aβ) and alpha synclein (αSyn), are associated with Alzheimer's Disease, and Parkinson's and Lewy Body Diseases, respectively. Importantly, pathological overlaps between these n

Externí odkaz: https://doaj.org/article/73c69df818db48af8a201d3f0c85fbc2

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Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent

Autor: Sanjoy Bandyopadhyay, Neelanjana Sengupta, Prabir Khatua, Jaya C. Jose

Publikováno v: Physical Chemistry Chemical Physics. 18:30144-30159

Accumulation of the amyloid beta (Aβ) peptide in the brain is responsible for debilitating neurodegenerative diseases, such as Alzheimer's disease (AD). We have carried out atomistic molecular dynamics simulations of the full-length Aβ42 peptide mo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::db4aadccd6e895ab4ebde95939d0bcac
https://doi.org/10.1039/c6cp04925g

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Clinicopathological Factors of Cervical Nodal Metastasis and the Concept of Selective Lateral Neck Dissection in the Surgical Management of Carcinoma Larynx and Hypopharynx and Its Outcome

Autor: Elizabeth Mathew Iype, Bipin T. Varghese, Sreekanth S Kumar, Jaya C. Jose, Santhosh Kumar N

To study the clinicopathological and molecular factors which correlate with nodal metastasis in laryngeal and hypopharyngeal carcinoma, a retrospective analysis of 170 patients who underwent surgery for laryngeal and hypopharyngeal carcinoma at RCC,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c49447a379ba7888f53fcf40733b3bb5
https://europepmc.org/articles/PMC5856687/

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The basic structural motif and major biophysical properties of Amyloid-β are encoded in the fragment 18–35

Autor: Sushma Gurav, Jaya C. Jose, Suman Nag, Neelanjana Sengupta, Sucheta Dandekar, Raja Banerjee, Bidyut Sarkar, Muralidharan Chandrakesan, Riddhi Shah, Bankanidhi Sahoo, Sudipta Maiti, Rajiv Abhyankar, Perunthiruthy K. Madhu, Venus Singh Mithu, Debanjan Bhowmik

Publikováno v: Chemical Physics. 422:80-87

Aggregation and misfolding of the amyloid beta (Aβ) peptide is thought to initiate Alzheimer’s disease (AD). Here we study the role played by its central segment (Aβ 18–35 ) in determining these properties. Aβ 18–35 has a solubility of 18 μ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1f02d8e674c9cd8d3a33ec529a46b754
https://doi.org/10.1016/j.chemphys.2013.01.010

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Molecular dynamics simulation studies of the structural response of an isolated Aβ1–42 monomer localized in the vicinity of the hydrophilic TiO2 surface

Autor: Jaya C. Jose, Neelanjana Sengupta

Publikováno v: European Biophysics Journal. 42:487-494

We have probed the effect of a model hydrophilic surface, rutile TiO(2), on the full-length amyloid beta (Aβ(1-42)) monomer using molecular dynamics simulations. The rutile surface brings about sharp changes in the peptide's intrinsic behavior in a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb48d7deebf0cb37a1878e65657c589a
https://doi.org/10.1007/s00249-013-0900-6

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Conformational features of the Aβ

Autor: Prabir, Khatua, Jaya C, Jose, Neelanjana, Sengupta, Sanjoy, Bandyopadhyay

Publikováno v: Physical chemistry chemical physics : PCCP. 18(43)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::55453049c55fc30a460a3743519880ff
https://pubmed.ncbi.nlm.nih.gov/27777990

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Microscopic hydration properties of the aβ1-42 Peptide monomer and the globular protein ubiquitin: a comparative molecular dynamics study

Autor: Neelanjana Sengupta, Jaya C. Jose, Prabir Khatua, Sanjoy Bandyopadhyay, Nupur Bansal

Publikováno v: The journal of physical chemistry. B. 118(40)

Atomistic molecular dynamics simulations of eight selected conformations of a disordered protein, amyloid beta (1-42) (Aβ), and a globular protein, ubiquitin (UBQ), have been carried out in aqueous media at 310 K. Detailed analyses were carried out

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f60563bb42642754425621939a3414d
https://pubmed.ncbi.nlm.nih.gov/25198420

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Cross Dimerization of Amyloid-β and αSynuclein Proteins in Aqueous Environment: A Molecular Dynamics Simulations Study

Autor: Prathit Chatterjee, Jaya C. Jose, Neelanjana Sengupta

Publikováno v: PLoS ONE
PLoS ONE, Vol 9, Iss 9, p e106883 (2014)

Self-assembly of the intrinsically unstructured proteins, amyloid beta (Aβ) and alpha synclein (αSyn), are associated with Alzheimer’s Disease, and Parkinson’s and Lewy Body Diseases, respectively. Importantly, pathological overlaps between the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::363a3adf7882c0554270780b2172c26a
http://europepmc.org/articles/PMC4161357

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Critical roles of key domains in complete adsorption of Aβ peptide on single-walled carbon nanotubes: insights with point mutations and MD simulations

Autor: Asis K. Jana, Neelanjana Sengupta, Jaya C. Jose

Publikováno v: Physical chemistry chemical physics : PCCP. 15(3)

Owing to the influence of nanomaterials on biomacromolecular behavior, their potential applications are rapidly gaining attention. Based on atomistic molecular dynamics simulation studies we have recently reported that the full-length Aβ peptide, wh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc851d676d3a753e08d517934b0339ee
https://pubmed.ncbi.nlm.nih.gov/23203213

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