P.W.H. Bolland, B.L.M. Hogan, "Expression of homeo box genes during mouse development," Genes & Development, 2(7), 773-82, July 1988.
Brigid L.M. Hogan (Department of Cell Biology, Vanderbilt University Medical School, Nashville, Tenn.): "The subdivision of Drosophiia into distinct body segments is regulated by development genes, many of which have a highly conserved DNA sequence known as a homeobox In 1984, Bill . McGinnis and his colleagues published the unexpected observation that homeobox sequences are also present in many different organisms, including mouse and man, raising the exciting possibility that a common set of genetic rules underlies the establishment of their basic body plans (W. McGinnis, R.L. Garber, J. Wirz, A. Kuroiwa, W.J. Gehring, Cell, 31, 403-8, 1984). Our paper reviewed data from many labs on the temporal and spatial patterns of expression of homeobox genes in mouse embryos. The data support the hypothesis that homeobox genes play a central role in, vertebrate development, a finding that has wide implications for animal evolution and teratology, as well as developmental biology."
N.W. Kleckner, R. Dingledine, "Requirement for glycine in activation of NMDA-receptors expressed in Xenapus oocytes," Science, 835-7, 12 August 1988.
Raymond Dingledine and Nancy W. Kleckner (Department of Pharmacology, University of North Carolina at Chapel Hill): "This paper built on the discovery that the small amino acid glycine greatly potentiates the activation of N-methyl-D-aspartate (NMDA) receptors by the 'conventional' agonist NMDA in mammalian central nervous system neurons (J.W. Johnson, P. Ascher, Nature, 325,529-31. 1987). We found that NMDA receptors expressed in Xenopus oocytes could not be activated at all in. the absence of glycine, and we used the term 'coagonist' to refer to the role of glycine in NMDA receptor activation. This paper provided the first demonstration of a neurotransmitter receptor which appears to require two different agonists for activation, and raised the, possibility of using glycine site antagonists to treat is chemic neuron injury caused by overactivation of NMDA receptors."
P. Wbyte, K.J. Buchkovich, J.M. Horowitz, S.H. Friend, M. Raybuck, R.A. Weinberg, E. Harlow, "Association between an oncogene and an anti-oncogene: the adenovirus, E1A proteins bind to the retinoblastoma gene product," Nature, 334 (6178), 124-9, 14 July 1988.
Karen J. Buvhkovich (Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.): "I think this research is exciting because it unifies two separate avenues of cancer research-work on DNA tumor viruses and oncogenes on the one hand, and anti- or negative oncogenes, on the other. We found that the protein of a virus oncogene, adenovirus E1A, interacts with an anti-oncogene that inhibits the function of the retinoblastoma protein."
