Zobrazeno 1 - 8
of 8
pro vyhledávání: '"D S, Waugh"'
Autor:
A. S. Zdanov, J. Phan, A. G. Evdokimov, J. E. Tropea, H. K. Peters III, R. B. Kapust, M. Li, A. Wlodawer, D. S. Waugh
Publikováno v:
Russian Journal of Bioorganic Chemistry. 29:415-418
Tobacco Etch Virus Protease (TEV protease) is widely used as a tool for separation of recombinant target proteins from their fusion partners. The crystal structures of two mutants of TEV protease, the active autolysis-resistant mutant TEV-S219D in co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d041081551db97f8ed6f916248a74493
https://doi.org/10.1023/a:1026041223534
https://doi.org/10.1023/a:1026041223534
Autor:
Robert T. Sauer, D S Waugh
Publikováno v:
Journal of Biological Chemistry. 269:12298-12303
A genetic screen was used to identify amino acid substitutions that enable the FokI restriction endonuclease to cleave DNA in cells that express the cognate methyltransferase activity. Missense mutations that give rise to this phenotype were isolated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::038cec8aa0c38b66ec8183644e795332
https://doi.org/10.1016/s0021-9258(17)32715-1
https://doi.org/10.1016/s0021-9258(17)32715-1
Publikováno v:
Journal of molecular biology. 312(4)
Many Gram-negative bacterial pathogens employ a contact-dependent (type III) secretion system to deliver effector proteins into the cytosol of animal or plant cells. Collectively, these effectors enable the bacteria to evade the immune response of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3d9ac2c736f15820e68030d1f6d631cf
https://pubmed.ncbi.nlm.nih.gov/11575934
https://pubmed.ncbi.nlm.nih.gov/11575934
Publikováno v:
The Journal of biological chemistry. 273(27)
The multifunctional signal transducer and activator of transcription (STAT) proteins relay signals from the cell membrane to the nucleus in response to cytokines and growth factors. STAT4 becomes activated when cells are treated with interleukin-12,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5989f4d966133ca532df196b6cb72735
https://pubmed.ncbi.nlm.nih.gov/9642277
https://pubmed.ncbi.nlm.nih.gov/9642277
Autor:
S D, Emerson, V S, Madison, R E, Palermo, D S, Waugh, J E, Scheffler, K L, Tsao, S E, Kiefer, S P, Liu, D C, Fry
Publikováno v:
Drug design and discovery. 13(3-4)
The structure of the Ras-binding domain of human c-Raf-1 (residues 55 to 132) as determined in solution by NMR spectroscopy is presented. It consists of a five-stranded beta-sheet, a twelve residue alpha-helix, and an additional one-turn helix. The f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::524791e2b8b6410fac9993dcf9e400b1
https://pubmed.ncbi.nlm.nih.gov/8874046
https://pubmed.ncbi.nlm.nih.gov/8874046
Autor:
J E, Scheffler, D S, Waugh, E, Bekesi, S E, Kiefer, J E, LoSardo, A, Neri, K M, Prinzo, K L, Tsao, B, Wegrzynski, S D, Emerson
Publikováno v:
The Journal of biological chemistry. 269(35)
Four overlapping peptide fragments of human c-Raf-1 (residues 55-132, 55-117, 77-132, and 77-117) were expressed in Escherichia coli as carboxyl-terminal extensions of maltose binding protein (MBP). The MBP-Raf fusions were purified by affinity chrom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::54c5f0203e34fd3a0f6a5d5eab19f8d6
https://pubmed.ncbi.nlm.nih.gov/8071362
https://pubmed.ncbi.nlm.nih.gov/8071362
Autor:
D S, Waugh, R T, Sauer
Publikováno v:
The Journal of biological chemistry. 269(16)
A genetic screen was used to identify amino acid substitutions that enable the FokI restriction endonuclease to cleave DNA in cells that express the cognate methyltransferase activity. Missense mutations that give rise to this phenotype were isolated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2a850e9bb2c844e7804b823578d77ec8
https://pubmed.ncbi.nlm.nih.gov/8163534
https://pubmed.ncbi.nlm.nih.gov/8163534
Autor:
N R, Pace, D S, Waugh
Publikováno v:
Methods in enzymology. 203
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::69f981566a393a900b886e6804db4b85
https://pubmed.ncbi.nlm.nih.gov/1722276
https://pubmed.ncbi.nlm.nih.gov/1722276