P
P Goodfellow
Researcher at University of Oxford
Publications - 12
Citations - 850
P Goodfellow is an academic researcher from University of Oxford. The author has contributed to research in topics: Antigen & Gene. The author has an hindex of 10, co-authored 12 publications receiving 848 citations.
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Journal ArticleDOI
Chromosomal localization of human cellular homologues of two viral oncogenes.
Nora Heisterkamp,John Groffen,John R. Stephenson,Nigel K. Spurr,P Goodfellow,Ellen Solomon,B. Carritt,Walter F. Bodmer +7 more
TL;DR: It is shown that the human equivalents of c-fes and c-abl are localized on human chromosomes 15 and 9, respectively, and this findings exclude the possibility that these transformation-related genes are clustered at a single locus within the human genome.
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Human gene mapping using an X/autosome translocation.
E. Solomon,Martin Bobrow,P Goodfellow,Walter F. Bodmer,Dallas M. Swallow,Susan Povey,B. Noël +6 more
TL;DR: Human fibroblasts containing a translocation between the X chromosome and chromosome 15 were fused with the 6-thioguanine-resistant mouse cell line, IR, and hybrids, selected in HAT medium, retained the X/15 chromosome.
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Serological identification of HL-A-linked human "Ia-type" antigens.
TL;DR: The Ir genetic region of the mouse has been shown to contain genes controlling a new set of serological specificities called Ia for immune associated, which has a tissue distribution that often does not include T lymphocytes.
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Subcellular separation and molecular nature of human histocompatibility antigens (HL-A).
TL;DR: This interpretation is based on the following arguments: that the antigens solubilised from guinea pig and human tissues by sonication and 3 M KCl extraction have been reported to be non-glycosylated, which would be explicable if the latter procedures had caused degradation and the consequent separation of the carbohydrate from the molecule bearing the antigenic determinant.
Journal ArticleDOI
Cellular Distribution, Purification, and Molecular Nature of Human la Antigens
TL;DR: Human Ia antigens were extensively purified (1390‐fold increase in specific activity) in 32% yield from BRI8 cells, a lymphoblastoid B‐cell line, and were determined by the polypeptide structure.