Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Margaret T. Haldeman"'
Publikováno v:
Biochemistry. 36:10526-10537
Individual members of the conserved family of ubiquitin conjugating enzymes (E2s) mediate the ubiquitination and turnover of specific substrates of the ubiquitin-dependent degradation pathway. E2 proteins have a highly conserved core domain of approx
Autor:
Tina M. Henkin, Margaret T. Haldeman, Gillian M. Hornblow, Judith M. Ward, Frank J. Grundy, Alison F. Chalker
Publikováno v:
Journal of Bacteriology. 179:3767-3772
The Staphylococcus aureus ileS gene, encoding isoleucyl-tRNA synthetase (IleRS), contains a long mRNA leader region. This region exhibits many of the features of the gram-positive synthetase gene family, including the T box and leader region terminat
Publikováno v:
Journal of Biological Chemistry. 270:9507-9516
To gain insight into the role of ubiquitin-mediated proteolysis in erythroid differentiation, levels of ubiquitin conjugating enzymes (E2s) and ubiquitin conjugates were analyzed during in vitro differentiation of murine erythroleukemic (MEL) cells.
Publikováno v:
Journal of Biological Chemistry. 267:14418-14423
Covalent ligation of multiubiquitin chains targets eukaryotic proteins for degradation. Ubiquitin-conjugating enzyme E2(25K) utilizes isolated ubiquitin as the substrate for synthesis of such chains, in which successive ubiquitin units are linked by
Publikováno v:
Nucleic acids research. 30(7)
The T box transcription termination control system is used in Gram-positive bacteria to regulate expression of aminoacyl-tRNA synthetase and other amino acid-related genes. Readthrough of a transcriptional terminator located in the leader region of t
Autor:
Lucy D. Mastrandrea, Margaret T. Haldeman, Daniel Finley, Judith Tamburlin, Cecile M. Pickart, Inge Wefes, Stephen T. Koury
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 92(11)
A global cellular reorganization occurs during the reticulocyte stage of erythroid differentiation. This reorganization is accomplished partly through programmed protein degradation. The selection of proteins for degradation can be mediated by covale