Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Dolly Banerjee"'
Autor:
Prasad, Swati, Wright, Kelly J., Roy, Dolly Banerjee, Bush, Leslie A., Cantwell, Angelene M., Di Cera, Enrico
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2003 Nov . 100(24), 13785-13790.
Externí odkaz:
https://www.jstor.org/stable/3148865
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
Publikováno v:
Molecular and Biochemical Parasitology. 83:189-200
In Plasmodium falciparum, a cysteine protease known as falcipain has been implicated in the essential metabolic process of hemoglobin degradation. Parallel lines of investigation, using native or recombinant enzyme, have led to differing conclusions
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
Publikováno v:
Proteins; May2001, Vol. 43 Issue 3, p315-318, 4p
Publikováno v:
Proteins: Structure, Function, and Bioinformatics; May 2001, Vol. 43 Issue: 3 p315-318, 4p