Zobrazeno 1 - 10
of 12
pro vyhledávání: '"S D, Emerson"'
Autor:
S. D. Emerson, J. E. Scheffler, Kwei-Lan Tsao, S. P. Liu, Robert Palermo, David S. Waugh, Vincent S. Madison, David C. Fry, S.E. Kiefer
Publikováno v:
Biochemistry. 34:6911-6918
The structure of the Ras-binding domain of human c-Raf-1 (residues 55-132) has been determined in solution by nuclear magnetic resonance (NMR) spectroscopy. Following complete assignment of the backbone and side-chain 1H, 15N, and 13C resonances, the
Autor:
Kathleen Prinzo, Joseph E. LoSardo, B. Wegrzynski, S.E. Kiefer, S. D. Emerson, J. E. Scheffler, Kwei-Lan Tsao, Anthony Neri, Eva Bekesi, David S. Waugh
Publikováno v:
Journal of Biological Chemistry. 269:22340-22346
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
Autor:
Weining Jiang, Wenqing Feng, Gaetano T. Montelione, Masayori Inouye, K. Newkirk, S. D. Emerson, Roberto Tejero
Publikováno v:
Proceedings of the National Academy of Sciences. 91:5114-5118
Sequence-specific 1H and 15N resonance assignments have been determined for the major cold shock protein (CspA) from Escherichia coli with recently developed three-dimensional triple-resonance NMR experiments. By use of these assignments, five antipa
Publikováno v:
The Journal of Biochemistry. 114:663-669
CS7.4 is the major cold-shock protein specifically expressed to a level as high as 13% of the total cellular protein within the first hour when Escherichia coli cell culture is shifted from 37 to 15 degrees C [Goldstein et al. (1990) Proc. Natl. Acad
Publikováno v:
Biopolymers. 32:327-334
A general approach is described for measuring homo- and heteronuclear spin coupling constants in polypeptides and small proteins. This method uses selective magnetization transfer to generate cross peaks similar to exclusive correlated spectroscopy (
Autor:
D C, Fry, S D, Emerson
Publikováno v:
Drug design and discovery. 17(1)
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
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
Publikováno v:
Biochemistry. 33(25)
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the cell growth signal transduction pathway. Recent genetic and biochemical experiments have demonstrated that (1) Ras interacts directly with the ami
Publikováno v:
Journal of biochemistry. 114(5)
CS7.4 is the major cold-shock protein specifically expressed to a level as high as 13% of the total cellular protein within the first hour when Escherichia coli cell culture is shifted from 37 to 15 degrees C [Goldstein et al. (1990) Proc. Natl. Acad