Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ganesh M. Mohite"'
Autor:
Rakesh Kumar, Namrata Singh, Per Nilsson, Samir K. Maji, Ambuja Navalkar, Pardeep Kumar, Ganesh M. Mohite, Ashutosh Kumar, Maheswaran Shanmugam, Makoto Shimozawa, Rajlaxmi Panigrahi, Shalini Tripathi, Shaffi Manchanda, Jan Johansson, Laxmikant G. Gadhe, Narayanaperumal Pravin
Publikováno v:
Journal of Neurochemistry. 156:1003-1019
Protein aggregation into amyloid fibrils is a key feature of a multitude of neurodegenerative diseases such as Alzheimer's, Parkinson's, and Prion disease. To detect amyloid fibrils, fluorophores with high sensitivity and better efficiency coupled wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8387100a929fd69d90fe3b7917d7523
https://doi.org/10.1111/jnc.15138
https://doi.org/10.1111/jnc.15138
Autor:
Pradeep K Singh, Dhiman Ghosh, Debanjan Tewari, Ganesh M Mohite, Edmund Carvalho, Narendra Nath Jha, Reeba S Jacob, Shruti Sahay, Rinti Banerjee, Amal K Bera, Samir K Maji
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0120346 (2015)
Conversion of amyloid fibrils by many peptides/proteins involves cytotoxic helix-rich oligomers. However, their toxicity and biophysical studies remain largely unknown due to their highly dynamic nature. To address this, we chose two helical peptides
Externí odkaz:
https://doaj.org/article/23f758e6065b4ad68684dd502e60c701
Autor:
Surabhi Mehra, Aishwarya Ramakrishnan, Rakesh Kumar, Ganesh M. Mohite, Vikas Chandrawanshi, Dhiman Ghosh, Samir K. Maji, Ambuja Navalkar, Laxmikant G. Gadhe, Basil Alias, Subhadeep Das, Sarika Mehra
Publikováno v:
Biochemistry. 57:5014-5028
Amyloid formation of α-synuclein (α-Syn) and its familial mutations are directly linked with Parkinson's disease (PD) pathogenesis. Recently, a new familial α-Syn mutation (A53E) was discovered, associated with an early onset aggressive form of PD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::639e848cd70c033440195b280fbce962
https://doi.org/10.1021/acs.biochem.8b00321
https://doi.org/10.1021/acs.biochem.8b00321
Autor:
Bhisma N Ratha, Samir K. Maji, Ambuja Navalkar, Dipita Bhattacharyya, Kanchan Garai, Atin K. Mandal, Rakesh Kumar, Nilanjan Gayen, Anirban Ghosh, Surabhi Mehra, Janarthanan Krishnamoorthy, Samuel A. Kotler, Ganesh M. Mohite, Anirban Bhunia
Publikováno v:
ACS chemical neuroscience. 10(5)
Altered intestinal permeability has been correlated with Parkinson's pathophysiology in the enteric nervous system, before manifestations in the central nervous system (CNS). The inflammatory endotoxin or lipopolysaccharide (LPS) released by gut bact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3a22d6b5dbcbe3857036f17b8aaaaa5
https://pubmed.ncbi.nlm.nih.gov/30855940
https://pubmed.ncbi.nlm.nih.gov/30855940
Autor:
Rakesh Kumar, Narendra Nath Jha, Subhadeep Das, Saumya Dwivedi, Samir K. Maji, Ganesh M. Mohite, Surabhi Mehra, Sravya Paluri, Neha Ruhela, Arunima S
Publikováno v:
ACS chemical neuroscience. 9(11)
α-Synuclein (α-Syn) aggregation and amyloid formation are associated with loss of dopaminergic neurons in Parkinson's disease (PD). In addition, familial mutations in α-Syn are shown to be one of the definite causes of PD. Here we have extensively
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cad40956a590a3804473e494387910ce
https://pubmed.ncbi.nlm.nih.gov/29906099
https://pubmed.ncbi.nlm.nih.gov/29906099
Autor:
Subhadeep Das, Debdeep Chatterjee, Samir K. Maji, Namrata Singh, Ambuja Navalkar, Rajlaxmi Panigrahi, Nitu Singh, Rakesh Kumar, Soumik Ray, Debalina Datta, Surabhi Mehra, Ashutosh Kumar, Laxmikant G. Gadhe, Ganesh M. Mohite
Publikováno v:
Biochemistry. 57(35)
The involvement of α-synuclein (α-Syn) amyloid formation in Parkinson's disease (PD) pathogenesis is supported by the discovery of α-Syn gene (SNCA) mutations linked with familial PD, which are known to modulate the oligomerization and aggregation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::410f6b60456e51561790e75d7162cbdd
https://pubmed.ncbi.nlm.nih.gov/29771508
https://pubmed.ncbi.nlm.nih.gov/29771508
Autor:
Vipin Agarwal, Rakesh Kumar, Subhadeep Das, Samir K. Maji, Surabhi Mehra, Narendra Nath Jha, Ganesh M. Mohite, Saayak Halder, Soumik Ray, Saroj K. Rout
Publikováno v:
Angewandte Chemie (International ed. in English). 57(19)
α-Synuclein (α-Syn) aggregation is associated with Parkinson's disease (PD) pathogenesis. In PD, the role of oligomers versus fibrils in neuronal cell death is debatable, but recent studies suggest oligomers are a proximate neurotoxin. Herein, we s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49eff0f907c7115bce4acd5f26b86c7b
https://pubmed.ncbi.nlm.nih.gov/29524323
https://pubmed.ncbi.nlm.nih.gov/29524323
Autor:
Shruti Sahay, Shinjinee Sengupta, Surabhi Mehra, Dhiman Ghosh, Guruswamy Krishnamoorthy, Mamata Kombrabail, Saikat Ghosh, Santanu K. Ghosh, Narendra Nath Jha, Reeba S. Jacob, Pradip Chaudhari, Subhadeep Das, Ganesh M. Mohite, Samir K. Maji, Ambuja Navalkar, Shimul Salot, Rakesh Kumar
The transcriptional regulator p53 has an essential role in tumor suppression. Almost 50% of human cancers are associated with the loss of p53 functions, where p53 often accumulates in the nucleus as well as in cytoplasm. Although it has been previous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::475e4bb9adc4fc6e821d403444bca4d6
https://europepmc.org/articles/PMC5596421/
https://europepmc.org/articles/PMC5596421/
Autor:
A. Anoop, Saumya Dwivedi, Mamata Kombrabail, Samir K. Maji, Dhiman Ghosh, Guruswamy Krishnamoorthy, Shruti Sahay, Ganesh M. Mohite
Background: Aggregation of -Syn is associated with PD pathogenesis. Results: Despite being natively unfolded, a site-specific structure exists in -Syn that is significantly altered by familial PD-associated E46K, A53T, and A30P mutations. Conclusion:
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cafd7212d1af251d097fb78d1b0935c
https://europepmc.org/articles/PMC4367280/
https://europepmc.org/articles/PMC4367280/
Autor:
Narendra Nath Jha, Shruti Sahay, Dhiman Ghosh, Rangan Banerjee, Amal Kanti Bera, Pradeep K. Singh, Edmund Carvalho, Debanjan Tewari, Reeba S. Jacob, Samir K. Maji, Ganesh M. Mohite
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0120346 (2015)
PLoS ONE
PLoS ONE
Conversion of amyloid fibrils by many peptides/proteins involves cytotoxic helix-rich oligomers. However, their toxicity and biophysical studies remain largely unknown due to their highly dynamic nature. To address this, we chose two helical peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd590c8075f8060b3035b1eedf7f422b
http://europepmc.org/articles/PMC4372375?pdf=render
http://europepmc.org/articles/PMC4372375?pdf=render