Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Aseem Chaphalkar"'
Autor:
Kanika Verma, Kanika Saxena, Rajashekar Donaka, Aseem Chaphalkar, Manish Kumar Rai, Anurag Shukla, Zainab Zaidi, Rohan Dandage, Dhanasekaran Shanmugam, Kausik Chakraborty
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Changes in osmotic homeostasis alter metabolites and therefore chemical milieu of the cells. Here, the authors show that altering metabolites in E. coli also change the cellular capacity for buffering mutations that impair protein folding and influen
Externí odkaz:
https://doaj.org/article/798249b34fd54ac1bcfc784baef16d78
Autor:
Anwar Sadat, Satyam Tiwari, S. Sunidhi, Aseem Chaphalkar, Manisha Kochar, Mudassar Ali, Zainab Zaidi, Akanksha Sharma, Kanika Verma, Kannan Boosi Narayana Rao, Manjul Tripathi, Asmita Ghosh, Deepika Gautam, null Atul, Arjun Ray, Koyeli Mapa, Kausik Chakraborty
Publikováno v:
Proceedings of the National Academy of Sciences. 119
The GroEL/ES chaperonin cavity surface charge properties, especially the negative charges, play an important role in its capacity to assist intracavity protein folding. Remarkably, the larger fraction of GroEL/ES negative charges are not conserved am
Autor:
Monika Verma, Niraj Rajesh Bhatt, Aseem Chaphalkar, Kriti Verma, Shreyansh Umale, Shweta Verma, Chetana Sachidanandan, Kausik Chakraborty
Redox homeostasis is an integral part of many cellular processes, and its perturbation is associated with conditions such as diabetes, aging, and neurodegenerative disorders. Redox homeostasis or redox potential in organelles is maintained within a p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::71e75f9dab162a22c6c3b5702d391045
https://doi.org/10.1101/2022.02.12.480199
https://doi.org/10.1101/2022.02.12.480199
Autor:
Arjun Ray, Anwar Sadat, Mudassar Ali, Kanika Verma, Asmita Ghosh, Rahul Chakraborty, Anupam Singh, Vaibhav Upadhyay, Aseem Chaphalkar, Satyam Tiwari, Koyeli Mapa, Kausik Chakraborty
The folding landscape of proteins can change during evolution with the accumulation of mutations that may introduce entropic or enthalpic barriers in the protein folding pathway, making it a possible substrate of molecular chaperones in vivo. Can the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aecb6b30409cdb3e9018d6f500b2fde8
https://doi.org/10.1101/2020.05.12.090233
https://doi.org/10.1101/2020.05.12.090233