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Comparative biochemical properties of normal and activated human ras p21 protein
Human Ha- ras 1 cDNAs encoding normal and activated p21 polypeptides have been efficiently expressed in Escherichia coli and the biochemical activities associated with each polypeptide compared. In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is se...
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| Published in: | Nature (London) 1984-08, Vol.310 (5979), p.644-649 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c407t-918851315afe2d4411b346926e263d0ab85f172d7b0443ea19d92352e55070d73 |
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| cites | cdi_FETCH-LOGICAL-c407t-918851315afe2d4411b346926e263d0ab85f172d7b0443ea19d92352e55070d73 |
| container_end_page | 649 |
| container_issue | 5979 |
| container_start_page | 644 |
| container_title | Nature (London) |
| container_volume | 310 |
| creator | McGrath, John P. Capon, Daniel J. Goeddel, David V. Levinson, Arthur D. |
| description | Human Ha-
ras
1 cDNAs encoding normal and activated p21 polypeptides have been efficiently expressed in
Escherichia coli
and the biochemical activities associated with each polypeptide compared. In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is selectively impaired by a mutation which activates its oncogenic potential |
| doi_str_mv | 10.1038/310644a0 |
| format | article |
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Escherichia coli
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Action of oncogenes and antioncogenes</topic><topic>Cloning, Molecular</topic><topic>DNA - metabolism</topic><topic>DNA Restriction Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. 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ras
1 cDNAs encoding normal and activated p21 polypeptides have been efficiently expressed in
Escherichia coli
and the biochemical activities associated with each polypeptide compared. In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is selectively impaired by a mutation which activates its oncogenic potential</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>6147754</pmid><doi>10.1038/310644a0</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1984-08, Vol.310 (5979), p.644-649 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81223515 |
| source | Nature |
| subjects | Biological and medical sciences Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cloning, Molecular DNA - metabolism DNA Restriction Enzymes Escherichia coli - genetics Fundamental and applied biological sciences. Psychology GTP Phosphohydrolases - genetics Guanosine Triphosphate - metabolism Humanities and Social Sciences Humans Molecular and cellular biology multidisciplinary Mutation Neoplasm Proteins - genetics Oncogene Protein p21(ras) Oncogenes Phosphorylation Protein Binding Proto-Oncogene Proteins p21(ras) RNA, Messenger - genetics Science Science (multidisciplinary) Substrate Specificity |
| title | Comparative biochemical properties of normal and activated human ras p21 protein |
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