Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Pradeep Kadu"'
Autor:
Manisha Poudyal, Komal Patel, Laxmikant Gadhe, Ajay Singh Sawner, Pradeep Kadu, Debalina Datta, Semanti Mukherjee, Soumik Ray, Ambuja Navalkar, Siddhartha Maiti, Debdeep Chatterjee, Jyoti Devi, Riya Bera, Nitisha Gahlot, Jennifer Joseph, Ranjith Padinhateeri, Samir K. Maji
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-21 (2023)
Abstract Liquid-liquid phase separation (LLPS) has emerged as a crucial biological phenomenon underlying the sequestration of macromolecules (such as proteins and nucleic acids) into membraneless organelles in cells. Unstructured and intrinsically di
Externí odkaz:
https://doaj.org/article/b30a93f83546417b873e83f6d8ce220c
Autor:
Debdeep Chatterjee, Reeba S Jacob, Soumik Ray, Ambuja Navalkar, Namrata Singh, Shinjinee Sengupta, Laxmikant Gadhe, Pradeep Kadu, Debalina Datta, Ajoy Paul, Sakunthala Arunima, Surabhi Mehra, Chinmai Pindi, Santosh Kumar, Praful Singru, Sanjib Senapati, Samir K Maji
Publikováno v:
eLife, Vol 11 (2022)
Synergistic-aggregation and cross-seeding by two different proteins/peptides in the amyloid aggregation are well evident in various neurological disorders including Alzheimer’s disease. Here, we show co-storage of human Prolactin (PRL), which is as
Externí odkaz:
https://doaj.org/article/54d99c7977ee49a782c1221d6dd5f8b3
Autor:
Samir K. Maji, Korak Kumar Ray, Jaladhar Mahato, Arindam Chowdhury, Subhadeep Das, Pradeep Kadu
Publikováno v:
The Journal of Physical Chemistry B. 125:13406-13414
Amyloid fibrils are structurally heterogeneous protein aggregates that are implicated in a wide range of neurodegenerative and other proteopathic diseases. These fibrils exist in a variety of different tertiary and higher-level structures, and this e
Autor:
Pradeep Kadu, Laxmikant Gadhe, Ambuja Navalkar, Komal Patel, Rakesh Kumar, Murali Sastry, Samir K. Maji
Publikováno v:
Nanoscale. 14(40)
Biomolecules are known to interact with metals and produce nanostructured hybrid materials with diverse morphologies and functions. In spite of the great advancement in the principles of biomimetics for designing complex nano-bio structures, the inte
Autor:
Arunima Sakunthala, Debalina Datta, Ambuja Navalkar, Laxmikant Gadhe, Pradeep Kadu, Komal Patel, Surabhi Mehra, Rakesh Kumar, Debdeep Chatterjee, Jyoti Devi, Kundan Sengupta, Ranjith Padinhateeri, Samir K. Maji
Publikováno v:
The journal of physical chemistry letters. 13(28)
The size of amyloid seeds is known to modulate their autocatalytic amplification and cellular toxicity. However, the seed size-dependent secondary nucleation mechanism, toxicity, and disease-associated biological processes mediated by α-synuclein (
Autor:
Namrata Singh, Komal Patel, Ambuja Navalkar, Pradeep Kadu, Debalina Datta, Debdeep Chatterjee, Semanti Mukherjee, Ranjit Shaw, Nitisha Gahlot, Abhishek Shaw, Sachin Jadhav, Samir K. Maji
Publikováno v:
Biomaterials. 295:122032
Autor:
Semanti Mukherjee, Arunima Sakunthala, Laxmikant Gadhe, Manisha Poudyal, Ajay Singh Sawner, Pradeep Kadu, Samir K. Maji
Publikováno v:
Journal of Molecular Biology. 435:167713
Aberrant aggregation of the misfolded presynaptic protein, α-Synuclein (α-Syn) into Lewy body (LB) and Lewy neuritis (LN) is a major pathological hallmark of Parkinson's disease (PD) and other synucleinopathies. Numerous studies have suggested that
Autor:
Rakesh Kumar, Murali Sastry, Pradeep Kadu, Samir K. Maji, Suditi Neekhra, Satyaprakash Pandey, Laxmikant G. Gadhe, Rohit Srivastava
Publikováno v:
The Journal of Physical Chemistry Letters. 11:10489-10496
Photothermal effects of metal nanoparticles (NPs) are used for various biotechnological applications. Although NPs have been used in a polymerase chain reaction (PCR), the effects of shape on the photothermal properties and its efficiency on PCR are
Autor:
Surabhi Mehra, Sahil Ahlawat, Harish Kumar, Debalina Datta, Ambuja Navalkar, Nitu Singh, Komal Patel, Laxmikant Gadhe, Pradeep Kadu, Rakesh Kumar, Narendra N. Jha, Arunima Sakunthala, Ajay S. Sawner, Ranjith Padinhateeri, Jayant B. Udgaonkar, Vipin Agarwal, Samir K. Maji
Publikováno v:
Journal of molecular biology. 434(19)
α-Synuclein (α-Syn) amyloids in synucleinopathies are suggested to be structurally and functionally diverse, reminiscent of prion-like strains. The mechanism of how the aggregation of the same precursor protein results in the formation of fibril po
Autor:
Debdeep Chatterjee, Reeba S Jacob, Soumik Ray, Ambuja Navalkar, Namrata Singh, Shinjinee Sengupta, Laxmikant Gadhe, Pradeep Kadu, Debalina Datta, Ajoy Paul, Sakunthala Arunima, Surabhi Mehra, Chinmai Pindi, Santosh Kumar, Praful Singru, Sanjib Senapati, Samir K Maji
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90d3a188c349f95902a3541605aee5f8
https://doi.org/10.7554/elife.73835.sa2
https://doi.org/10.7554/elife.73835.sa2