Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ramesh Kumar Sistla"'
Autor:
Joel C. Barrish, John Hynes, Ajay Saxena, Natesan Murugesan, Dianlin Xie, Anjaneya Chimalakonda, Stefan Ruepp, Mitalee Das, Richard Rampulla, Durgarao Kantheti, Chunhong Yan, Julie Carman, Jignesh Nagar, Siva Subramani, Qian Ruan, William J. Pitts, Rajeev S. Bhide, Paul A. Elzinga, Venkatram Reddy Paidi, John S. Sack, Mark Fereshteh, Thangavel Soodamani, Amrita Jha Mukherjee, T. Thanga Mariappan, Ramesh Kumar Sistla, Kaushik Ghosh, Debarati Mazumder, Kamalavenkatesh Palanisamy, Deborah A. Holloway, Susan E. Kiefer, John A. Newitt, Satheesh Kesavan Nair, Polimera Subba Rao, Shailesh Dudhgoankar, Percy H. Carter, Xin Li, Srinivas Maddi, S. Pon Saravanakumar, Sreekantha Ratna Kumar, Sucharita Bose
Publikováno v:
ACS Med Chem Lett
[Image: see text] IRAK4 is an attractive therapeutic target for the treatment of inflammatory conditions. Structure guided optimization of a nicotinamide series of inhibitors has been expanded to explore the IRAK4 front pocket. This has resulted in t
Autor:
Siva Prasad Putlur, Kumaravel Selvakumar, Deepak Ahire, Ramesh Kumar Sistla, Santosh Wagh, Sarmistha Sinha, Benjamin M. Johnson, Janet Caceres Cortes, Sandhya Mandlekar, Dibakar Mullick
Publikováno v:
Chemical Research in Toxicology. 27:2052-2061
Certain aromatic nitriles are well-known inhibitors of cysteine proteases. The mode of action of these compounds involves the formation of a reversible or irreversible covalent bond between the nitrile and a thiol group in the active site of the enzy
Structural studies on xLi2S–(1−x)P2S5 glasses by X-ray diffraction and molecular dynamics simulation
Autor:
Ramesh Kumar Sistla, M. Seshasayee
Publikováno v:
Journal of Non-Crystalline Solids. 349:54-59
Short range order in x Li 2 S–(1 − x )P 2 S 5 glasses with x = 0.50 and 0.60 was studied by X-ray diffraction and molecular dynamics simulation. The glasses were prepared in evacuated quartz ampoules by the melt quenching method. Results from an
Autor:
Ramesh Kumar Sistla, M. Seshasayee
Publikováno v:
Journal of Non-Crystalline Solids. 349:22-29
The structures of x Li 2 O–(1 − x )P 2 O 5 glasses with x = 0.10, 0.20 and 0.30 have been examined using X-ray radial distribution functions. The composition range x = 0.10–0.75 also has been studied by molecular dynamics simulations. MD config
Autor:
Krishnaprasad Subbarao, Jwala Nagaraj, Rajendra K. Palakurthy, Ramesh Kumar Sistla, Hosahalli Subramanya, Murali Ramachandra, Chakshusmathi Ghadiyaram, Gerd Wohlfahrt, Narasimha Rao Krishnamurthy, Sreevalsam Gopinath, Anu Moilanen, Subhendu Mukherjee, Pekka Kallio, Tarja Ikonen, Rajeev Goswami, Leena Khare Satyam
Publikováno v:
Bioorganicmedicinal chemistry. 22(12)
Matriptase is a serine protease implicated in cancer invasion and metastasis. Expression of matriptase is frequently dysregulated in human cancers and matriptase has been reported to activate latent growth factors such as hepatocyte growth factor/sca
Autor:
M. Seshasayee, Ramesh Kumar Sistla
Publikováno v:
Solid State Communications. 113:35-39
Short-range order in the ionically conducting 40Li 2 O–60P 2 O 5 glass has been studied by the reverse Monte Carlo (RMC) method, using X-ray diffraction data. The initial configuration for RMC was obtained by constant volume molecular dynamics simu
Autor:
Jwala Nagaraj, Chakshusmathi Ghadiyaram, Anu Moilanen, Ramesh Kumar Sistla, Murali Ramachandra, Hosahalli Subramanya, Subhendu Mukherjee, Leena Khare Satyam, DS Samiulla, Rajeev Goswami, Beeram Ravi Chandra, Gerd Wohlfahrt
Matriptase belongs to trypsin-like serine proteases involved in matrix remodeling/degradation, growth regulation, survival, motility, and cell morphogenesis. Herein, we report a structure-based approach, which led to the discovery of sulfonamide and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::307579e787f4faa4490227606014b2fa
https://europepmc.org/articles/PMC4027570/
https://europepmc.org/articles/PMC4027570/
We present a novel method for the identification of structural domains and domain interface residues in proteins by graph spectral method. This method converts the three-dimensional structure of the protein into a graph by using atomic coordinates fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2f5e0395cf47c4d4c031595b9383024
http://eprints.iisc.ernet.in/3249/
http://eprints.iisc.ernet.in/3249/