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Year | Number of Results |
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1988 | 1 |
1989 | 1 |
1990 | 2 |
1992 | 1 |
2024 | 0 |
PubMed for id: 156873
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Page 1
Structure of ras proteins.
Science. 1989 Jul 21;245(4915):244. doi: 10.1126/science.2665078.
Science. 1989.
PMID: 2665078
Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21.
de Vos AM, Tong L, Milburn MV, Matias PM, Jancarik J, Noguchi S, Nishimura S, Miura K, Ohtsuka E, Kim SH.
de Vos AM, et al.
Science. 1988 Feb 19;239(4842):888-93. doi: 10.1126/science.2448879.
Science. 1988.
PMID: 2448879
Item in Clipboard
Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins.
Milburn MV, Tong L, deVos AM, Brünger A, Yamaizumi Z, Nishimura S, Kim SH.
Milburn MV, et al.
Science. 1990 Feb 23;247(4945):939-45. doi: 10.1126/science.2406906.
Science. 1990.
PMID: 2406906
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Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.
Brünger AT, Milburn MV, Tong L, deVos AM, Jancarik J, Yamaizumi Z, Nishimura S, Ohtsuka E, Kim SH.
Brünger AT, et al.
Proc Natl Acad Sci U S A. 1990 Jun;87(12):4849-53. doi: 10.1073/pnas.87.12.4849.
Proc Natl Acad Sci U S A. 1990.
PMID: 2191303
Free PMC article.
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X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.
Privé GG, Milburn MV, Tong L, de Vos AM, Yamaizumi Z, Nishimura S, Kim SH.
Privé GG, et al.
Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3649-53. doi: 10.1073/pnas.89.8.3649.
Proc Natl Acad Sci U S A. 1992.
PMID: 1565661
Free PMC article.
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