Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Prasunkumar J. Mishra"'
Autor:
Güray Saydam, M Aracil, Jose Jimeno, Joseph R. Bertino, L D Lewis, Prasunkumar J. Mishra, Debabrata Banerjee, Lata G. Menon, Rita Humeniuk, Y Elisseyeff, G S A Longo-Sorbello
Publikováno v:
Leukemia. 21:2399-2405
Aplidin (plitidepsin) is a novel marine-derived antitumor agent presently undergoing phase II clinical trials in hematological malignancies and solid tumors. Lack of bone marrow toxicity has encouraged further development of this drug for treatment o
Autor:
Chandran Ragunath, Prasunkumar J. Mishra, Leonard M. Thomas, Lili Kandra, Narayanan Ramasubbu, Gyöngyi Gyémánt
Publikováno v:
European Journal of Biochemistry. 271:2517-2529
The nonreducing end of the substrate-binding site of human salivary alpha-amylase contains two residues Trp58 and Trp59, which belong to beta2-alpha2 loop of the catalytic (beta/alpha)(8) barrel. While Trp59 stacks onto the substrate, the exact role
Probing the Role of a Mobile Loop in Substrate Binding and Enzyme Activity of Human Salivary Amylase
Publikováno v:
Journal of Molecular Biology. 325:1061-1076
Mammalian amylases harbor a flexible, glycine-rich loop 304 GHGAGGA 310 , which becomes ordered upon oligosaccharide binding and moves in toward the substrate. In order to probe the role of this loop in catalysis, a deletion mutant lacking residues 3
Autor:
H. Gao, Jose Jimeno, Giuseppe S. A. Longo-Sorbello, B. Kamen, Joseph R. Bertino, M.F. Paz De Paz, Prasunkumar J. Mishra, D. Banerjee, Miguel Aracil, A. Soto
Publikováno v:
Journal of chemotherapy (Florence, Italy). 21(5)
Plitidepsin (Aplidin) is a novel antitumor agent, derived from the mediterranean tunicate Aplidium albicans, and is currently in phase ii clinical trials with evidence of activity in heavily pretreated multiple myeloma, renal cell carcinoma, melanoma
Autor:
Debabrata Banerjee, Lata G. Menon, Nancy E. Skacel, Joseph R. Bertino, Emine Ercikan Abali, Prasunkumar J. Mishra, Rowayda Peters
Publikováno v:
The Journal of biological chemistry. 280(24)
Human dihydrofolate reductase (DHFR) protein levels rapidly increase upon exposure to methotrexate, a potent inhibitor of this enzyme. A model to explain this increase proposes that DHFR inhibits its own translation by binding to its cognate mRNA and
Publikováno v:
Biochemical and biophysical research communications. 292(2)
Hydrolysis of starch or oligosaccharides by mammalian amylases, in general, results in maltose as the leaving group. The active site of these amylases harbors three aromatic residues Trp59, Tyr62, and Tyr151, which provide stacking interactions to th
Autor:
Giuseppe S.A. Longo, Debabrata Banerjee, Joseph R. Bertino, Lata G. Menon, Emine Ercikan Abali, Prasunkumar J. Mishra
Publikováno v:
Blood. 104:2084-2084
Dihydrofolate reductase (DHFR) catalyzes the reduction of dihydrofolate to tetrahydrofolate (THF) required for the synthesis of thymidylate and purines. Methotrexate (MTX) acts as a tight-binding inhibitor of DHFR and remains an important chemotherap