Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Raghavan, Pavithra"'
Autor:
Raghavan, Pavithra, Tumati, Vasu, Yu, Lan, Chan, Norman, Tomimatsu, Nozomi, Burma, Sandeep, Bristow, Robert G., Saha, Debabrata
Publikováno v:
In International Journal of Radiation Oncology, Biology, Physics 15 November 2012 84(4):e507-e514
Autor:
Saha, Debabrata, Watkins, Linda, Yin, Yi, Thorpe, Philip, Story, Michael D., Song, Kwang, Raghavan, Pavithra, Timmerman, Robert, Chen, Benjamin, Minna, John D., Solberg, Timothy D.
Publikováno v:
Radiation Research, 2010 Jul 01. 174(1), 62-71.
Externí odkaz:
https://www.jstor.org/stable/40785261
Publikováno v:
PLoS Computational Biology, Vol 3, Iss 9, Pp 1701-1715 (2007)
Molecular chaperones participate in the maintenance of cellular protein homeostasis, cell growth and differentiation, signal transduction, and development. Although a vast body of information is available regarding individual chaperones, few studies
Externí odkaz:
https://doaj.org/article/b9601073113a458fb1c27d52e9f58acd
Autor:
Kong, Zhaolu, Raghavan, Pavithra, Xie, Daxing, Boike, Thomas, Burma, Sandeep, Chen, David, Chakraborty, Arup, Hsieh, Jer-Tsong, Saha, Debabrata
Publikováno v:
In International Journal of Radiation Oncology, Biology, Physics 2010 78(4):1210-1218
Autor:
Raj Kumar Singh, S. Venketesh, Rishi Kumar Nageshan, Raghunath Reddy, Nainita Roy, Rajender Kumar, Pinaki Talukdar, Suresh Chandra Yadav, Ashok Kumar Gupta, Utpal Tatu, Soundara Raghavan Pavithra, Rani Pallavi
Publikováno v:
Journal of Biological Chemistry. 285:37964-37975
Using a pharmacological inhibitor of Hsp90 in cultured malarial parasite, we have previously implicated Plasmodium falciparum Hsp90 (PfHsp90) as a drug target against malaria. In this study, we have biochemically characterized PfHsp90 in terms of its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e7cf06d968e2419b8334bc3e1830d7a
https://doi.org/10.1074/jbc.m110.155317
https://doi.org/10.1074/jbc.m110.155317
Publikováno v:
Journal of Biosciences. 32:531-536
We have recently implicated heat shock protein 90 from Plasmodium falciparum (PfHsp90) as a potential drug target against malaria. Using inhibitors specific to the nucleotide binding domain of Hsp90, we have shown potent growth inhibitory effects on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c1775893feb216ee5e517b4bd0f417d
https://doi.org/10.1007/s12038-007-0052-x
https://doi.org/10.1007/s12038-007-0052-x
Autor:
Rani, Pallavi, Nainita, Roy, Rishi Kumar, Nageshan, Pinaki, Talukdar, Soundara Raghavan, Pavithra, Raghunath, Reddy, S, Venketesh, Rajender, Kumar, Ashok Kumar, Gupta, Raj Kumar, Singh, Suresh Chandra, Yadav, Utpal, Tatu
Publikováno v:
The Journal of biological chemistry. 285(49)
Using a pharmacological inhibitor of Hsp90 in cultured malarial parasite, we have previously implicated Plasmodium falciparum Hsp90 (PfHsp90) as a drug target against malaria. In this study, we have biochemically characterized PfHsp90 in terms of its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::14f685dadba89fff3d0bf94236c2068a
https://pubmed.ncbi.nlm.nih.gov/20837488
https://pubmed.ncbi.nlm.nih.gov/20837488
Publikováno v:
IndraStra Global.
The human malarial parasite Plasmodium falciparum (Pf) is exposed to wide temperature fluctuations during its life cycle, ranging from 25 degrees C in the mosquito vector and 37 degrees C in humans to 41 degrees C during febrile episodes in the patie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b646bcca374b144f3e6d77aa6efffd07
https://igi.indrastra.com/items/show/192452
https://igi.indrastra.com/items/show/192452
Publikováno v:
IndraStra Global.
Malarial parasite Plasmodium falciparum is responsible for the most severe form of malaria in humans, causing about 2 million deaths every year. Lack of effective vaccines and emergence of drug-resistant strains necessitate the need of novel drug tar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::e9640840b4316dbc057cd172f4cb9667
http://eprints.iisc.ac.in/3187/1/a_novel_assay.pdf
http://eprints.iisc.ac.in/3187/1/a_novel_assay.pdf
Publikováno v:
The Journal of biological chemistry. 278(20)
Hsp90 is important for normal growth and development in eukaryotes. Together with Hsp70 and other accessory proteins, Hsp90 not only helps newly synthesized proteins to fold but also regulates activities of transcription factors and protein kinases.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0b60c928e37a155c52ed50b9a04d1d9
https://pubmed.ncbi.nlm.nih.gov/12584193
https://pubmed.ncbi.nlm.nih.gov/12584193