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Ottilie, S., Chernoff, J., Hannig, G., Hoffman, C. S., Erikson, R. L. (1991) A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases. Proceedings of the National Academy of Sciences, 88 (8) 3455-3459 doi:10.1073/pnas.88.8.3455

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Reference TypeJournal (article/letter/editorial)
TitleA fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases.
JournalProceedings of the National Academy of Sciences
AuthorsOttilie, S.Author
Chernoff, J.Author
Hannig, G.Author
Hoffman, C. S.Author
Erikson, R. L.Author
Year1991 (April 15)Volume88
Issue8
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.88.8.3455Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1507637Long-form Identifiermindat:1:5:1507637:5
GUID0
Full ReferenceOttilie, S., Chernoff, J., Hannig, G., Hoffman, C. S., Erikson, R. L. (1991) A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases. Proceedings of the National Academy of Sciences, 88 (8) 3455-3459 doi:10.1073/pnas.88.8.3455
Plain TextOttilie, S., Chernoff, J., Hannig, G., Hoffman, C. S., Erikson, R. L. (1991) A fission-yeast gene encoding a protein with features of protein-tyrosine-phosphatases. Proceedings of the National Academy of Sciences, 88 (8) 3455-3459 doi:10.1073/pnas.88.8.3455
In(1991, April) Proceedings of the National Academy of Sciences Vol. 88 (8) Proceedings of the National Academy of Sciences

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Hannig, G., Ottilie, S., Erikson, R. L. (1994) Negative regulation of mitosis in fission yeast by catalytically inactive pyp1 and pyp2 mutants. Proceedings of the National Academy of Sciences, 91 (21) 10084-10088 doi:10.1073/pnas.91.21.10084
Chernoff, J., Schievella, A. R., Jost, C. A., Erikson, R. L., Neel, B. G. (1990) Cloning of a cDNA for a major human protein-tyrosine-phosphatase. Proceedings of the National Academy of Sciences, 87 (7) 2735-2739 doi:10.1073/pnas.87.7.2735
Crews, C. M., Erikson, R. L. (1992) Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product. Proceedings of the National Academy of Sciences, 89 (17) 8205-8209 doi:10.1073/pnas.89.17.8205
Crews, C. M., Alessandrini, A. A., Erikson, R. L. (1991) Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine. Proceedings of the National Academy of Sciences, 88 (19) 8845-8849 doi:10.1073/pnas.88.19.8845
Malik, A., Egan, J. E., Houghten, R. A., Sadoff, J. C., Hoffman, S. L. (1991) Human cytotoxic T lymphocytes against the Plasmodium falciparum circumsporozoite protein. Proceedings of the National Academy of Sciences, 88 (8) 3300-3304 doi:10.1073/pnas.88.8.3300
Ballou, L., Hitzeman, R. A., Lewis, M. S., Ballou, C. E. (1991) Vanadate-resistant yeast mutants are defective in protein glycosylation. Proceedings of the National Academy of Sciences, 88 (8) 3209-3212 doi:10.1073/pnas.88.8.3209
(1991) Relationship of genes encoding Ca2+/calmodulin-dependent protein kinase Gr and calspermin: A gene within a gene. Proceedings of the National Academy of Sciences, 88 (20) 9375 doi:10.1073/pnas.88.20.9375-c
Weinstein, S. L., Gold, M. R., DeFranco, A. L. (1991) Bacterial lipopolysaccharide stimulates protein tyrosine phosphorylation in macrophages. Proceedings of the National Academy of Sciences, 88 (10) 4148-4152 doi:10.1073/pnas.88.10.4148
Alessandrini, A., Crews, C. M., Erikson, R. L. (1992) Phorbol ester stimulates a protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product. Proceedings of the National Academy of Sciences, 89 (17) 8200-8204 doi:10.1073/pnas.89.17.8200
Cassill, J. A., Whitney, M., Joazeiro, C. A., Becker, A., Zuker, C. S. (1991) Isolation of Drosophila genes encoding G protein-coupled receptor kinases. Proceedings of the National Academy of Sciences, 88 (24) 11067-11070 doi:10.1073/pnas.88.24.11067
Becker, D. M., Fikes, J. D., Guarente, L. (1991) A cDNA encoding a human CCAAT-binding protein cloned by functional complementation in yeast. Proceedings of the National Academy of Sciences, 88 (5) 1968-1972 doi:10.1073/pnas.88.5.1968
 
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