Hot Papers

P. Gregor, I. Mano, I. Maoz, M. McKeown, V.I. Teichberg, "Molecular structure of the chick cerebellar kainate-binding subunit of a putative glutamate receptor," Nature, 342:689-92, 1989. Vivian Teichberg (Weizmann Institute of Science, Israel): "In the last decade, there has been an explosive interest in brain glutamate receptors. This comes from the recognition that this set of membranous proteins plays crucial roles in brain physiology and pathology. "In contrast to the great strides being m

Jul 8, 1991
The Scientist Staff

P. Gregor, I. Mano, I. Maoz, M. McKeown, V.I. Teichberg, "Molecular structure of the chick cerebellar kainate-binding subunit of a putative glutamate receptor," Nature, 342:689-92, 1989.

Vivian Teichberg (Weizmann Institute of Science, Israel): "In the last decade, there has been an explosive interest in brain glutamate receptors. This comes from the recognition that this set of membranous proteins plays crucial roles in brain physiology and pathology.

"In contrast to the great strides being made in the field of glutamate receptor research by anatomists, electrophysiologists, and pharmacologists, the efforts of the biochemists to isolate the glutamate receptors were frustrated for a long time.

"It is therefore not too surprising that our paper, published together with those from the groups of Stephen Heinemann at the Salk Institute [M. Hollmann, A. O'Shea-Greenfield, S.W. Rogers, S. Heinemann, Nature, 342:643-48, 1989; `Hot Papers,' The Scientist, January 21, 1991, page 14] and of Robert Wenthold at the National Institutes of Health [K. Wada, C.J. Dechesne, S. Shimasaki, et al., Nature, 342:684-89, 1989], attracted wide attention.

"These papers described the molecular structure of a rat kainate receptor and that of putative subunits of frog and chick kainate receptors. They showed, to the surprise of many, that the kainate/glutamate receptors belong to a protein family distinct from the family of ligandgated receptor/channels, although the members of both families share similar topological features, such as the presence of four putative trans-membrane domains in their polypeptide chain. These papers also provided, for the first time, unique nucleotide sequence data of potential importance for reaching the present Holy Grail--the structure of the much heralded NMDA-type of glutamate receptor."