Zobrazeno 1 - 9 of 9 pro vyhledávání: '"Roopa Jones Ganji"'
1
Puromycin, a selective inhibitor of PSA acts as a substrate for other M1 family aminopeptidases: Biochemical and structural basis
Autor: Naga Veera Yerra, Anthony Addlagatta, Sandeep Chowdary Bala, Neshatul Haque, Anil Kumar Marapaka, Ravikumar Reddi, Roopa Jones Ganji
Publikováno v: International Journal of Biological Macromolecules. 165:1373-1381
Puromycin sensitive aminopeptidase (PSA or NPEPPS) is a M1 class aminopeptidase is selectively inhibited by the natural product puromycin, an aminonucleoside antibiotic produced by the bacterium Streptomyces alboniger. The molecular basis for this se
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef27de839b722bee0d687375f32736ec
https://doi.org/10.1016/j.ijbiomac.2020.10.035
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2
Highly functionalized tetrahydropyridines are cytotoxic and selective inhibitors of human puromycin sensitive aminopeptidase
Autor: Roopa Jones Ganji, Raghunath Aeluri, Anthony Addlagatta, Anil Kumar Marapaka, Manjula Alla, Vijaykumar Pillalamarri
Publikováno v: European Journal of Medicinal Chemistry. 106:26-33
Efficient one-pot five-component synthetic protocols for highly functionalized tetrahydropyridines (THPs) and their biological evaluation have been illustrated. Synthesis of novel functionalized tetrahydropyridines containing differential substitutio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0975c16d2954d16d57eb1b59910a365f
https://doi.org/10.1016/j.ejmech.2015.10.026
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3
Structural basis for the inhibition of M 1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E . coli aminopeptidase N
Autor: Rajesh Gumpena, Roopa Jones Ganji, Ravikumar Reddi, Tarun Arya, Anil Kumar Marapaka, Anthony Addlagatta, Supriya Bhukya, Priyanka Sankoju
Publikováno v: Protein Science. 24:823-831
Actinonin is a pseudotripeptide that displays a high affinity towards metalloproteases including peptide deformylases (PDFs) and M1 family aminopeptidases. PDF and M1 family aminopeptidases belong to thermolysin-metzincin superfamily. One of the majo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e43b79230efd00cec366a8120ea0cfe5
https://doi.org/10.1002/pro.2653
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4
Discovery of Tröger's base analogues as selective inhibitors against human breast cancer cell line: Design, synthesis and cytotoxic evaluation
Autor: Manjula Alla, Bhaskar Reddy Manda, Roopa Jones Ganji, Anthony Addlagatta
Publikováno v: European Journal of Medicinal Chemistry. 86:39-47
A library of structurally diverse Troger's base analogues has been constructed via unusual amination of methylene bridge employing Vilsmeier–Haack conditions as well as by the incorporation of five and six membered heterocycles on the aromatic core
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c62b62a3c12ccf9a2afa052890a30130
https://doi.org/10.1016/j.ejmech.2014.08.044
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5
Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N
Autor: Roopa Jones Ganji, Anthony Addlagatta, Chandan Kishor, Rajesh Gumpena, Nishant Jain
Publikováno v: Protein Science. 21:727-736
Escherichia coli aminopeptidase N (ePepN) belongs to the gluzincin family of M1 class metalloproteases that share a common primary structure with consensus zinc binding motif (HEXXH-(X18)-E) and an exopeptidase motif (GXMEN) in the active site. There
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eccb36025277ee2532176eb7d6719791
https://doi.org/10.1002/pro.2060
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6
Discovery of α,β- and α,γ-Diamino Acid Scaffolds for the Inhibition of M1 Family Aminopeptidases
Autor: Anthony Addlagatta, Rajesh Gumpena, Chandan Kishor, Roopa Jones Ganji
Publikováno v: ChemMedChem. 6:1971-1976
The a-amino group is an important moiety in the binding of peptides to their target peptidases. Herein we report that a gamino group displaces the a-amino by adopting an unexpected binding mode, resulting in the inhibition of the peptidase. a,b- and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7992a922fb3e70aa2a58f1c8ababcc50
https://doi.org/10.1002/cmdc.201100298
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8
Iodine-catalyzed condensation of isatin with indoles: a facile synthesis of di(indolyl)indolin-2-ones and evaluation of their cytotoxicity
Autor: Y. Prashanthi, N. Rajeswari, B. V. Subba Reddy, Roopa Jones Ganji, Anthony Addlagatta, M. Sarangapani
Publikováno v: Bioorganicmedicinal chemistry letters. 22(7)
Isatin reacts smoothly with indoles in the presence of a catalytic amount of molecular iodine under mild conditions to afford a novel class of di(indolyl)indolin-2-one derivatives in good yields. These molecules are found to possess a promising cytot
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42c5280f960446056f51391e4f8ade1c
https://pubmed.ncbi.nlm.nih.gov/22386528
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9
Synthesis, cytotoxicity and hDHFR inhibition studies of 2H-pyrido[1,2-a]pyrimidin-2-ones
Autor: Manjula Alla, Vittal Rao Bommena, Roopa Jones Ganji, Chandan Kishor, Anthony Addlagatta, Venkateshwarlu Saddanapu, Sreevani Rapolu
Publikováno v: MedChemComm. 4:817
Synthesis of the titled scaffolds was achieved by the condensation of Baylis–Hillman acetates with 2-aminopyridines under solvent-free conditions. Resulting compounds were evaluated for anticancer activity against five different cancer cell lines.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cef6eea89dcaa425cd0d9776a2e9f786
https://doi.org/10.1039/c3md00013c
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