Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Sudhakar Voruganti"'
Autor:
Sambit R. Kar, Tapan K. Das, Xue Li, Sudhakar Voruganti, Jiahui Xu, Surinder M. Singh, Gurusamy Balakrishnan
Publikováno v:
Journal of pharmaceutical sciences. 110(2)
N-linked glycosylation is an important post translational modification that occurs on Asparagine 297 residue or a homologous position on the Fc portion of monoclonal antibodies (mAbs). mAb Fc glycans play important roles in antibody structure, stabil
Autor:
Sudhakar, Voruganti, Jake T, Kline, Maurie J, Balch, Janet, Rogers, Robert L, Matts, Steven D, Hartson
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1709
Mass spectrometry assays demonstrate that Hsp90 inhibitors alter the expression of approximately one-quarter of the assayable proteome in mammalian cells. These changes are extraordinarily robust and reproducible, making "proteomics profiling" the go
Autor:
Maurie Balch, Sudhakar Voruganti, Robert L. Matts, Jake T. Kline, Janet Rogers, Steven D. Hartson
Publikováno v:
Methods in Molecular Biology ISBN: 9781493974764
Mass spectrometry assays demonstrate that Hsp90 inhibitors alter the expression of approximately one-quarter of the assayable proteome in mammalian cells. These changes are extraordinarily robust and reproducible, making "proteomics profiling" the go
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef5f8d4eb7ea19e9b0bac7fa16fdc59a
https://doi.org/10.1007/978-1-4939-7477-1_11
https://doi.org/10.1007/978-1-4939-7477-1_11
Autor:
Janet Rogers, Chelsea N. Rogers, Steven D. Hartson, Robert L. Matts, Jeff C. LaCroix, Sudhakar Voruganti
Publikováno v:
Journal of Proteome Research. 12:3697-3706
AUY922 is a potent synthetic Hsp90 antagonist that is moving steadily through clinical trials against a small range of cancers. To identify protein markers that might measure the drug’s effects, and to gain understanding of mechanisms by which AUY9
Autor:
Robert L. Matts, Gennady M. Verkhivker, Steve Hartson, Sudhakar Voruganti, Laura B. Peterson, Palgunan Kalyanaraman, Anshuman Dixit, Brian S. J. Blagg, Liang Sun
Publikováno v:
ACS Chemical Biology. 6:800-807
The Hsp90 chaperone machine is required for the folding, activation, and/or stabilization of more than 50 proteins directly related to malignant progression. Hsp90 contains small molecule binding sites at both its N- and C-terminal domains; however,