Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jaya C. Jose"'
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
Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent
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
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/
https://europepmc.org/articles/PMC5856687/
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
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
Publikováno v:
Physical chemistry chemical physics : PCCP. 18(43)
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 Aβ
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
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 9, p e106883 (2014)
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
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