Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ranit Pariary"'
Autor:
Sandip Dolui, Anupam Roy, Uttam Pal, Shubham Kundu, Esha Pandit, Bhisma N Ratha, Ranit Pariary, Achintya Saha, Anirban Bhunia, Nakul C. Maiti
Publikováno v:
ACS Physical Chemistry Au, Vol 4, Iss 3, Pp 268-280 (2024)
Externí odkaz:
https://doaj.org/article/ca8419e1e561450d83c9372f12f62c6b
Publikováno v:
International Journal of Biological Macromolecules. 218:981-991
The aggregation of proteins into ordered fibrillar structures called amyloids, and their disintegration represent major unsolved problems that limit the therapeutic applications of several proteins. For example, insulin, commonly used for the treatme
Autor:
Kanti Kusum Yadav, Monalisha Ojha, Ranit Pariary, Manoranjan Arakha, Suman Jha, Anirban Bhunia
Publikováno v:
Biochimie. 193:64-77
Zinc oxide nanoparticle with negative surface potential (ZnONP) enhances bovine insulin fibrillation. Here, we are exploring ZnONP with positive surface potential (ZnONPUnc) and surface functionalized with tyrosine and tryptophan amino acids to obser
Autor:
Ranit Pariary, Sandip Dolui, Gourav Shome, Sk Abdul Mohid, Achintya Saha, Bhisma N Ratha, Amaravadhi Harikishore, Kuladip Jana, Atin K Mandal, Nakul Chandra Maiti, Anirban Bhunia
Publikováno v:
Chemical Communications.
Our studies show Coomassie Brilliant Blue G-250 as a promising chemical chaperone that stabilises the α-helical native human insulin conformers, disrupting its aggregation. Furthermore, it also increases the insulin secretion....
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:
Ranit Pariary, Anirban Bhunia, Snehasikta Swarnakar, Bhisma N Ratha, Susmita Saha, Amaravadhi Harikishore, Sandip Dolui, Nakul C. Maiti, Achintya Saha
Human insulin (HI) is an essential protein hormone and its biological activity mostly depends on folded and active conformation in the monomeric state. The present investigation established that Coomassie Brilliant Blue G-250 (CBBG), a small multicyc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c726a08256e24a585aad9b398de4264
https://doi.org/10.1101/2020.08.26.267799
https://doi.org/10.1101/2020.08.26.267799
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:
Ranit Pariary, Dipita Bhattacharyya, Zuzana Bednarikova, Sreyan Raha, Atin K. Mandal, Zuzana Gazova, Kyriakos G. Varnava, Baijayanti Ghosh, Vijayalekshmi Sarojini, Bhisma N Ratha, Anirban Bhunia
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1868(5)
Amyloidogenic disorders are currently rising as a global health issue, prompting more and more studies dedicated to the development of effective targeted therapeutics. The innate affinity of these amyloidogenic proteins towards the biomembranes adds
Publikováno v:
Gene Reports. 16:100423
The mitochondrial association of α-synuclein has been known to play a crucial homeostatic role in the neuronal cells. The slightest of a tweak in this association cause for activating the neurodegenerative mechanism, ultimately leading to neuronal l