Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Jagadish P. Hazra"'
Autor:
Nisha Arora, Jagadish P. Hazra, Sandip Roy, Gaurav K. Bhati, Sarika Gupta, K. P. Yogendran, Abhishek Chaudhuri, Amin Sagar, Sabyasachi Rakshit
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Tip-links in the inner ear convey force from sound and trigger mechanotransduction. Here, we present evidence that tip-links (collectively as heterotetrameric complexes of cadherins) function as force filters during mechanotransduction. Our
Externí odkaz:
https://doaj.org/article/a3da42b00cf14a198dcf8d0e1ccc25d7
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Arora, Hazra & Rakshit investigate the significance of complex conformations in force sensing. They found that protein complexes possess a distinct response to mechanical force compared to individual force sensors.
Externí odkaz:
https://doaj.org/article/67079fc274904dc1b4bb721a687c22b8
Autor:
Nisha Arora, Jagadish P. Hazra, Sandip Roy, Gaurav K. Bhati, Sarika Gupta, Abhishek Chaudhuri, Amin Sagar, Sabyasachi Rakshit
Tip-links as gating-spring in the mechanotransduction in hearing is still a debate. While the molecular elasticity of individual tip-link proteins warrants its candidature, the apparent rigidity from the heterotetrameric tip-links assembly refutes th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb60a09e066d327a2cb1c52d6120e0ae
https://doi.org/10.1101/2022.08.10.503460
https://doi.org/10.1101/2022.08.10.503460
Publikováno v:
Journal of Materials Chemistry B. 8:523-533
Fabricating protein compartments from protein units is challenging and limited by the use of external stimuli and crosslinkers. Here we explore the fabrication of all-protein compartments using self-assembled proteins of prokaryotic organelles. These
Publikováno v:
Chembiochem : a European journal of chemical biology. 23(9)
A classic example of an all-protein natural nano-bioreactor, the bacterial microcompartment is a prokaryotic organelle that confines enzymes in a small volume enveloped by an outer protein shell. These protein compartments metabolize specific organic
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Communications Biology
Communications Biology
Proteins as force-sensors respond to mechanical cues and regulate signaling in physiology. Proteins commonly connect the source and response points of mechanical cues in two conformations, independent proteins in end-to-end geometry and protein compl
Autor:
Sabyasachi Rakshit, Jagadish P. Hazra, Simerpreet Kaur, Nisha Arora, Amin Sagar, Debadutta Deb
Publikováno v:
Biochemical Journal
Tip-link as force-sensor in hearing conveys the mechanical force originating from sound to ion-channels while maintaining the integrity of the entire sensory assembly in the inner ear. This delicate balance between structure and function of tip-links
A classic example of an all-protein natural nano-bioreactor, the bacterial microcompartments are a special kind of prokaryotic organelles that confine enzymes within a small volume enveloped by an outer layer of shell proteins. This arrangement provi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd93ba0c6744a23c9f35cf89e534aa3f
Autor:
Jagadish P. Hazra, Aashish Bhatt, Sharmistha Sinha, Ankush Garg, Gaurav Kumar, Md. Ehesan Ali, Naimat K. Bari
Publikováno v:
ACS Catalysis. 8:7742-7748
Bacterial microcompartments (MCPs) are polyhedral organelles containing an enzyme cluster wrapped inside a protein shell and carry out specific enzyme reactions in bacteria. These organelles have been explored meticulously using genetic, structural,
Publikováno v:
Biophys J
Mutations in p53 protein, especially in the DNA binding domain is one of the major hallmarks of cancer. The R273 position is a DNA contact position and has several oncogenic variants. Surprisingly, cancer patients carrying different mutant-variants o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47e9ead20e97f28b15654ec707c4b537
https://doi.org/10.1101/684407
https://doi.org/10.1101/684407