Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Bankanidhi, Sahoo"'
Autor:
Mithun Maddheshiya, Bankanidhi Sahoo, Sreelakshmi Cherakara, Timir Baran Sil, Kanchan Garai, S. Deepa, Neeraja Chilukoti
Publikováno v:
Biophys J
Molecular chaperone Hsp70 plays important roles in the pathology of amyloid diseases by inhibiting aberrant aggregation of proteins. However, the biophysical mechanism of the interaction of Hsp70 with the intrinsically disordered proteins (IDPs) is u
Autor:
Bankanidhi Sahoo, Irene Arduini, Kenneth W Drombosky, Ravindra Kodali, Laurie H Sanders, J Timothy Greenamyre, Ronald Wetzel
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0155747 (2016)
Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington's disease (HD). Although there is general agreement that HTT toxicity resides primarily in N-terminal fragm
Externí odkaz:
https://doaj.org/article/0d7d5852f7b5410c952937e6b1b377c6
Autor:
Rajiv K. Kar, Sujan Kalita, Anirban Bhunia, Jeffrey R. Brender, Bhisma N Ratha, Bankanidhi Sahoo, Ranit Pariary
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 88:1648-1659
Insulin has long been served as a model for protein aggregation, both due to the importance of aggregation in the manufacture of insulin and because the structural biology of insulin has been extensively characterized. Despite intensive study, detail
Autor:
Bankanidhi Sahoo, Pavankumar Janardhan Bhandari, Mullapudi Mohan Reddy, Britto S. Sandanaraj, Akshay Bhagwan Lohote
Publikováno v:
ChemBioChem. 21:408-416
The custom design of protein-dendron amphiphilic macromolecules is at the forefront of macromolecular engineering. Macromolecules with this architecture are very interesting because of their ability to self-assemble into various biomimetic nanoscopic
Autor:
null Bhisma N Ratha, null Rajiv K Kar, null Jeffrey R Brender, null Ranit Pariary, null Bankanidhi Sahoo, null Sujan Kalita, null Anirban Bhunia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7f51ba11a792c08a6c2bdbec39bf745
https://doi.org/10.1002/prot.25983/v3/response1
https://doi.org/10.1002/prot.25983/v3/response1
Autor:
Mithun Maddheshiya, Neeraja Chilukoti, Sreelakshmi Cherakara, Kanchan Garai, S. Deepa, Bankanidhi Sahoo
Molecular chaperone Hsp70 plays important roles in the pathology of amyloid diseases by inhibiting aberrant aggregation of proteins. However, mechanism of the interactions of Hsp70 with the amyloidogenic intrinsically disordered proteins (IDPs) is no
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58f8fe83e44af883e41ac1783159b66b
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860:1917-1926
Injection of exogenous insulin in the subcutaneous mass has been a proven therapy for type II diabetes. However, chronic administration of insulin often develops local amyloidosis at the injection site, pathologically known as "Insulin Ball". This re
Autor:
Debanjan Bhowmik, Venus Singh Mithu, Sudipta Maiti, Perunthiruthy K. Madhu, Anand Kant Das, Bappaditya Chandra, Bankanidhi Sahoo
Publikováno v:
Biophysical Journal. 112:1597-1608
There are three specific regions in the Amyloid beta (Aβ) peptide sequence where variations cause enhanced toxicity in Alzheimer’s disease: the N-terminus, the central salt bridge, and the C-terminus. Here, we investigate if there is a close confo
Autor:
Anirban Bhunia, Sujan Kalita, Bankanidhi Sahoo, Rajiv K. Kar, Jeffrey R. Brender, Bhisma N Ratha
Insulin has long served as a model for protein aggregation, both because of the importance of aggregation in insulin manufacture and because the structural biology of insulin has been extensively characterized. Despite intensive study, details about
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::346b5e88d32523f7c03350ad74de4049