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pro vyhledávání: '"Dolly Banerjee Roy"'
Autor:
Thierry Rose, Dolly Banerjee-Roy, Angelene M. Cantwell, Ellen K. LeMosy, Enrico Di Cera, James B. Skeath
Publikováno v:
Journal of Biological Chemistry. 278:11320-11330
Three-dimensional models of the catalytic domains of Nudel (Ndl), Gastrulation Defective (Gd), Snake (Snk), and Easter (Ea), and their complexes with substrate suggest a possible organization of the enzyme cascade controlling the dorsoventral fate of
Autor:
Angelene M. Cantwell, Leslie A. Bush, Enrico Di Cera, Kelly J. Wright, Swati Prasad, Dolly Banerjee Roy
Monovalent-cation-activated enzymes are abundantly represented in plants and in the animal world. Most of these enzymes are specifically activated by K + , whereas a few of them show preferential activation by Na + . The monovalent cation specificity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d967523ac5770cb021c857221779705
https://europepmc.org/articles/PMC283499/
https://europepmc.org/articles/PMC283499/
Autor:
Thierry, Rose, Ellen K, LeMosy, Angelene M, Cantwell, Dolly, Banerjee-Roy, James B, Skeath, Enrico, Di Cera
Publikováno v:
The Journal of biological chemistry. 278(13)
Three-dimensional models of the catalytic domains of Nudel (Ndl), Gastrulation Defective (Gd), Snake (Snk), and Easter (Ea), and their complexes with substrate suggest a possible organization of the enzyme cascade controlling the dorsoventral fate of
Publikováno v:
Proteins. 43(3)
Na+ binding to thrombin enhances the catalytic activity toward numerous synthetic and natural substrates. The bound Na+ is located in a solvent channel 16 A away from the catalytic triad, and connects with D189 in the S1 site through an intervening w