Výsledky vyhledávání - "J E, Scheffler"

Ras-dependent maturation of Xenopus oocytes is blocked by modified peptides of GTPase activating protein (GAP)

Autor: Edgar P. Heimer, J. E. Scheffler, Anthony Neri, Joseph E. LoSardo, Eva Bekesi, Kathleen Prinzo

Publikováno v: International Journal of Peptide and Protein Research. 45:194-199

Guanosine triphosphatase activating protein (GAP) is an important modulator of p21ras (Ras)-dependent signal transduction in mammalian cells and in insulin-induced maturation of Xenopus oocytes. A synthetic octapeptide from the catalytic domain of GA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3274cddc195980a486afe01e9502d40
https://doi.org/10.1111/j.1399-3011.1995.tb01040.x

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Solution Structure of the Ras-Binding Domain of c-Raf-1 and Identification of Its Ras Interaction Surface

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c79085ce8c910b1f15ff4663b489aa17
https://doi.org/10.1021/bi00021a001

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Covalent modification of the interleukin-5 receptor by isothiazolones leads to inhibition of the binding of interleukin-5

Autor: José Van der Heyden, Geert Plaetinck, Jan Tavernier, Rene Devos, Louise H. Foley, J. E. Scheffler, Yves Guisez, Sigrid Cornelis

Publikováno v: European Journal of Biochemistry. 225:635-640

Using a fusion protein of the human interleukin-5-receptor alpha chain (hIL5R alpha) and the human IgG C gamma 3 chain (hIL5R alpha-h gamma 3), we have developed a solid-phase assay for high-flux screening of a collection of synthetic compounds. We r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::486d041839c114fdf0592fd9f27e010e
https://doi.org/10.1111/j.1432-1033.1994.00635.x

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Characterization of a 78-residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with Ras-GTP

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::87f1edc085e5dede0d57155fe12d76b1
https://doi.org/10.1016/s0021-9258(17)31795-7

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A role for the carboxyl terminus of human granulocyte-macrophage colony-stimulating factor in the binding of ligand to the alpha-subunit of the high affinity receptor

Autor: Gail F. Seelig, Winifred W. Prosise, J E Scheffler

Publikováno v: Journal of Biological Chemistry. 269:5548-5553

A synthetic segment (110-127) of the carboxyl terminus of recombinant human granulocyte-macrophage colony-stimulating factor (rh-GM-CSF) was used to generate a rabbit polyclonal antibody (345-6), which recognized both peptide and full-length Escheric

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d3ead0aad9ed6218bb2d57d392c7590b
https://doi.org/10.1016/s0021-9258(17)37496-3

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Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region that interacts with Ras

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

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Scintillation proximity assay to measure the binding of ras-GTP to the ras-binding domain of c-Raf-1

Autor: J. E. Scheffler, Eva Bekesi, Susan E. Kiefer, Kathleen Prinzo

Publisher Summary This chapter describes the scintillation proximity assay (SPA) to measure the binding of Ras-GTP to the Ras-binding domain of c-Raf-1. By capturing the protein-bound [ 3 H]GTP on SPA beads, it is possible to measure the binding of R

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4df209203cbedfa227732c26a525325c
https://doi.org/10.1016/s1080-8914(96)80014-7

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Characterization of a 78-residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with Ras-GTP

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)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::54c5f0203e34fd3a0f6a5d5eab19f8d6
https://pubmed.ncbi.nlm.nih.gov/8071362

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Mapping of the p56lck-mediated phosphorylation of GAP and analysis of its influence on p21ras-GTPase activity in vitro

Autor: Willi Bannwarth, Hans-Werner Lahm, J. E. Scheffler, Juliette Molnos, Paul Burn, Nicholas Flint, Kurt Amrein, Baerbel Panholzer

Publikováno v: Biochimica et biophysica acta. 1222(3)

The protein tyrosine kinase p56lck and other members of the src family can transduce signals from activated cell-surface receptors. As we showed earlier the GTPase-activating protein (GAP), a regulator of p21ras, is a substrate of p56lck. Here, trypt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82cfaf54ceeaf1fd12d583bf35695b3c
https://pubmed.ncbi.nlm.nih.gov/8038213

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Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy

Autor: David C. Fry, Kathleen Prinzo, S. D. Emerson, J. E. Scheffler, Kwei-Lan Tsao, David S. Waugh

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c147038b9ad27a4fb7a514ca1269ce8
https://pubmed.ncbi.nlm.nih.gov/8011639

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