Zobrazeno 1 - 10 of 11 pro vyhledávání: '"M V, Milburn"'
1
Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
Autor: M. V. Milburn, Sung-Hou Kim, A. De Vos, Liang Tong
Publikováno v: Journal of Molecular Biology. 217:503-516
The biological functions of ras proteins are controlled by the bound guanine nucleotide GDP or GTP. The GTP-bound conformation is biologically active, and is rapidly deactivated to the GDP-bound conformation through interaction with GAP (GTPase Activ
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdf6335e8b80e12c576e3b91a9d2a541
https://doi.org/10.1016/0022-2836(91)90753-s
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2
Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain
Autor: Axel T. Brunger, Eiko Ohtsuka, Jarmila Jancarik, Sung-Hou Kim, Susumu Nishimura, Abraham M. deVos, Liang Tong, Ziro Yamaizumi, M. V. Milburn
Publikováno v: Proceedings of the National Academy of Sciences. 87:4849-4853
Normal RAS proteins play a key role of molecular switch in the transduction of the growth signal from extracellular to intracellular space. The state of the switch is "on" when GTP is bound and "off" when GDP is bound to the protein. The crystal stru
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cf260790873e7f29c1ad4b8853ac0fd
https://doi.org/10.1073/pnas.87.12.4849
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3
The PPARs and PXRs: nuclear xenobiotic receptors that define novel hormone signaling pathways
Autor: S A, Kliewer, J M, Lehmann, M V, Milburn, T M, Willson
Publikováno v: Recent progress in hormone research. 54
Traditional pharmacologic approaches had identified several classes of xenobiotics that elicited characteristic biological effects in vivo but that lacked defined molecular mechanisms of action. Among these xenobiotics were the peroxisome proliferato
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7d331a1aed69f4fee1fa0b94744d6d55
https://pubmed.ncbi.nlm.nih.gov/10548883
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4
Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium
Autor: Daniel L. Milligan, Joanne Yeh, William G. Scott, M. V. Milburn, Sung-Hou Kim, Gilbert G. Privé, Daniel E. Koshland
Publikováno v: Journal of molecular biology, vol 232, iss 2
Scott, WG; Milligan, DL; Milburn, MV; Privé, GG; Yeh, J; Koshland, DE; et al.(1993). Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium. Journal of Molecular Biology, 232(2), 555-573. doi: 10.1006/jmbi.1993.1411. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/5c21f0mb
The aspartate receptor is a transmembrane-signalling protein that mediates chemotaxis behaviour in bacteria. Aspartate receptors in Salmonella typhimurium and Escherichia coli exist as dimers of two subunits in the presence as well as in the absence
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19c83c9c18968919d07731a4d82d72b6
https://pubmed.ncbi.nlm.nih.gov/8345523
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5
X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis
Autor: S Nishimura, Sung-Hou Kim, Liang Tong, A. De Vos, M. V. Milburn, Z Yamaizumi, Gilbert G. Privé
Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 89(8)
RAS genes isolated from human tumors often have mutations at positions corresponding to amino acid 12 or 61 of the encoded protein (p21), while retroviral ras-encoded p21 contains substitutions at both positions 12 and 59. These mutant proteins are d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14c2a763615d869051bf32f79c2b9d66
https://pubmed.ncbi.nlm.nih.gov/1565661
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6
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
Autor: M. V. Milburn, Sung-Hou Kim, Daniel E. Koshland, Daniel L. Milligan, William G. Scott, Gilbert G. Privé, Joanne Yeh, Jarmila Jancarik
Publikováno v: Science (New York, N.Y.), vol 254, iss 5036
Milburn, MV; Privé, GG; Milligan, DL; Scott, WG; Yeh, J; Jancarik, J; et al.(1991). Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science, 254(5036), 1342-1347. doi: 10.1126/science.1660187. UC Santa Cruz: Retrieved from: http://www.escholarship.org/uc/item/5h52w0jp
The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b9bf149e995fc12f5f683e670f19f5
https://escholarship.org/uc/item/5h52w0jp
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8
Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21
Autor: Shigeru Noguchi, Susumu Nishimura, Sung-Hou Kim, Kazunobu Miura, P. M. Matias, A. De Vos, Jaru Jancarik, Eiko Ohtsuka, Liang Tong, M. V. Milburn
Publikováno v: Science (New York, N.Y.). 239(4842)
The crystal structure at 2.7 A resolution of the normal human c-H-ras oncogene protein lacking a flexible carboxyl-terminal 18 residue reveals that the protein consists of a six-stranded beta sheet, four alpha helices, and nine connecting loops. Four
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6945b8a99a73fff5575d9c8a5383f67f
https://pubmed.ncbi.nlm.nih.gov/2448879
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9
Structural differences between a ras oncogene protein and the normal protein
Autor: M. V. Milburn, E Ohtsuka, Sung-Hou Kim, A. De Vos, Liang Tong, Jaru Jancarik, S Noguchi, K Miura, S Nishimura
Publikováno v: Nature. 337(6202)
One of the most commonly found transforming ras oncogenes in human tumours has a valine codon replacing the glycine codon at position 12 of the normal c-Ha-ras gene1–4. To understand the structural reasons behind cell transformation arising from th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76914f460997a496bfd378c51a4028be
https://pubmed.ncbi.nlm.nih.gov/2642607
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10
Three-Dimensional Structure of ras p21 Proteins
Autor: Sung-Hou Kim, Liang Tong, M. V. Milburn, A. De Vos, P. M. Matias
Publikováno v: The Guanine — Nucleotide Binding Proteins ISBN: 9781475720396
ras genes (review in Barbacid, 1987) have been found in a large number of eukaryotic organisms, from Saccharomyces and Drosophila to chicken, rat, and man. Moreover, ras gene products of various species show a very high degree of homology: even betwe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b9da61ced66153b812aef0aeab954431
https://doi.org/10.1007/978-1-4757-2037-2_3
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