Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Ganapathy Ayappa"'
Autor:
Luc Bondaz, Anshaj Ronghe, Shaoxian Li, Kristia̅ns Čerņevičs, Jian Hao, Oleg V. Yazyev, K. Ganapathy Ayappa, Kumar Varoon Agrawal
Publikováno v:
JACS Au, Vol 3, Iss 10, Pp 2844-2854 (2023)
Externí odkaz:
https://doaj.org/article/e504b94d54c248a19968bf000250decb
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Pore forming proteins are a broad class of pathogenic proteins secreted by organisms as virulence factors due to their ability to form pores on the target cell membrane. Bacterial pore forming toxins (PFTs) belong to a subclass of pore forming protei
Externí odkaz:
https://doaj.org/article/de65fb91e4574f64aa5350fb9d0f94bf
Autor:
Wan-Chi Lee, Anshaj Ronghe, Luis Francisco Villalobos, Shiqi Huang, Mostapha Dakhchoune, Mounir Mensi, Kuang-Jung Hsu, K. Ganapathy Ayappa, Kumar Varoon Agrawal
Publikováno v:
ACS Nano. 16:15382-15396
Enhancing the kinetics of liquid-vapor transition from nanoscale confinements is an attractive strategy for developing evaporation and separation applications. The ultimate limit of confinement for evaporation is an atom thick interface hosting angst
Autor:
Pradyumn Sharma, K. Ganapathy Ayappa
Publikováno v:
The Journal of Membrane Biology. 255:665-675
With rising bacterial resistance, antimicrobial peptides (AMPs) have been widely investigated as potential antibacterial molecules to replace conventional antibiotics. Our understanding of the molecular mechanisms for membrane disruption are largely
Plasma membrane induced protein folding and conformational transitions play a central role in cellular homeostasis. Several transmembrane proteins are folded in the complex lipid milieu to acquire a specific structure and function. Bacterial pore for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c004950affd67480ff2006051c68d72
https://doi.org/10.1101/2023.05.07.539733
https://doi.org/10.1101/2023.05.07.539733
CXCR4 is a G-protein coupled receptor which mediates signalling for diverse functions such as cell proliferation and migration, hematopoiesis and plays a role in embryogenesis and development. Signal transduction occurs primarily through transmembran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d385e186114f8bbf14d1e66ed400f2eb
https://doi.org/10.1101/2023.02.28.530397
https://doi.org/10.1101/2023.02.28.530397
Publikováno v:
Soft Matter. 18:4483-4492
Mitochondrial populations in cells are maintained by cycles of fission and fusion events. Perturbation of this balance has been observed in several diseases such as cancer and neurodegeneration. In fission yeast cells, the association of mitochondria
Autor:
Avijeet Kulshrestha, Satyaghosh Maurya, Twinkle Gupta, Rahul Roy, Sudeep N Punnathanam, K. Ganapathy Ayappa
Publikováno v:
The journal of physical chemistry. B.
Several bacterial infections are mediated by pore-forming toxins (PFTs), a subclass of proteins that oligomerize on mammalian cell membranes forming lytic nanopores. Cytolysin A (ClyA), an α-PFT, undergoes a dramatic conformational change restructur
Autor:
Pradyumn Sharma, Rakesh Vaiwala, Srividhya Parthasarathi, Nivedita Patil, Anant Verma, Morris Waskar, Janhavi S. Raut, Jaydeep Kumar Basu, K. Ganapathy Ayappa
Publikováno v:
Langmuir : the ACS journal of surfaces and colloids.
Surfactants with their intrinsic ability to solubilize lipid membranes are widely used as antibacterial agents, and their interactions with the bacterial cell envelope are complicated by their differential aggregation tendencies. We present a combine
Publikováno v:
Soft matter. 18(39)
The transition of an α-helix to a β-sheet in proteins is among the most complex conformational changes seen in biomolecular systems. Due to long time scales involved in the transition, it is challenging to study such protein conformational changes