The research career of Richard B. Stein (1940-)

This report reviews the research and mentoring career of Richard B. Stein (1940-). In 1962, he completed a B.S. degree in physics at the Massachusetts Institute of Technology, USA, and thereafter an M.A. (1964), Ph.D. (1966), and postdoctoral training (1966-68) at the University of Oxford, UK. He subsequently assumed a faculty position at the University of Alberta (Canada), where he is currently an active researcher and mentor. To this point in 2004, Stein has trained and collaborated closely with over 160 scientists, largely neuroscientists and biomedical engineers, from 27 countries. He and his former trainees and collaborators have made important contributions on topics that span the cellular-to-behavioral spectrum of movement and rehabilitation-prosthetics neuroscience. His mentors, trainees, and collaborators include scientists whose countries of origin are: Australia, 2; Austria, 1; Belgium, 1; Bulgaria, 1; Canada, 64; China, 6; Denmark, 1; Germany, 1; Great Britain, 16; Hong Kong, 4; India, 5; Iraq, 2; Italy, 2; Japan, 10; Kenya, 1; New Zealand, 4; Pakistan, 1; Palestine, 1; Poland, 1; Romania, 1; South Africa, 1; Sri Lanka, 1; The Netherlands, 1; Turkey, 1; Uruguay, 1; USA, 21; and Yugoslavia, 6. In all instances, Stein's research collaborations and mentoring have advanced the careers of his trainees and junior collaborators, a well-deserved and important compliment to a stellar movement neuroscientist.     

Uronychia transfuga (O. F. Müller, 1786) Stein, 1859 (Ciliophora, Hypotrichia, Uronychiidae): Cortical Structure and Morphogenesis during Division

Morphogenesis of cell division was investigated in Uronychia transfuga utilizing both light microscopy of living and stained specimens and SEM of preserved specimens. The cortical morphogenetic pattern of Uronychia is similar in several respects to that of the members of the family Euplotidae. These features include: the de novo development of the opisthe oral primordium in a subcortical pouch; the development of frontoventral and transverse cirri for both the proter and opisthe from 5 cirral primordia that form de novo within a single latitudinal developmental zone; and the absence of right marginal cirri. The members of the genus Uronychia also show a number of unique characteristics: development of a proter oral primordium that causes partial replacement of the parental adoral zone of oral polykinetids during development of the proter; a large oral membrane that is divided into a right and left component; large caudal cirri that bend to the left; and dorsal kineties comprised of closely set paired-kinetosome kinetids. When compared to the other euplotid-like ciliates, these unique features support the placement of the genus Uronychia in a separate family, Uronychiidae.     

Wright KL,Birnbaum MJ,van Wijnen AJ,Stein GS,Stein JL (1995): Bipartite structure of the proximal promoter of a human H4 histone gene. J Cell Biochem 58:372–379.

The proximal promoter of the human H4 histone gene FO108 contains two regions of in vivo protein-DNA interaction, Sites I and II. electrophoretic, mobility shift assays using a radiolabeled DNA probe revealed that several proteins present in HeLa cell nuclear extracts bound specifically to Site 1 (nt-125 to nt-86). The most prominent complex, designated HiNF-C, and a complex of greater mobility, HiNF-C′, using were specifically competed by an Sp1 consensus oligonucleotide. Fractionation of HiNF-C using wheat germ agglutinin affinity chromatography suggested that, like Sp1, HiNF-C contains N-acetylglucosamine moieties. Two minor complexes of even greater mobility, designated HiNF-E and F, were competed by ATF consensus oligonucleotides. A DNA probe carrying a site-specific mutation in the distal portion of Site I failed to bind HiNF-E, indicating that this protein associated specifically to this region. UV cross-linking analysis showed that several proteins of different molecular wieghts interact specifically with Site I. These data indicate that Site I possesses as bipartite structure and that multiple proteins present in HeLa cell nuclear extracts interact specifically with Site I sequences. © 1995 Wiley-Liss, Inc.