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Journal of Biosciences 1999年第1期24卷 33-198页

作者： N. Manoj V. R. Srinivas A. Surolia M. Vijayan K. Suguna R. Ravishankar R. Schwarzenbacher K. Zeth Diederichs G. M. Kostner A. Gries P. Laggner R. Prassl Madhusudan Pearl Akamine Nguyen-huu Xuong Susan S. Taylor M. Bidva Sagar K. Saikrishnan S. Roy K. Purnapatre P. Handa U. Varshney B. K. Biswal N. Sukumar J. K. Mohana Rao A. Johnson Vasantha Pattabhi S. Sri Krishna Mira Sastri H. S. Savithri M. R. N. Murthy Bindu Pillai Kannan M. V. Hosur Mukesh Kumar Swati Patwardhan K. K. Kannan B. Padmanabhaa S. Sasaki-Sugio M. Nukaga T. Matsuzaki S. Karthikevan S. Sharma A. K. Sharma M. Paramasivam P. Kumar J. A. Khan S. Yadav A. Srinivasan T. P. Singh S. Gourinath Neelima Alam A. Srintvasan Vikas Chandra Punit Kaur Ch. Betzel S. Ghosh A. K. Bera S. Bhattacharya S. Chakraborty A. K. Pal B. P. Mukhopadhyay I. Dey U. Haldar Asok Baneriee Jozef Sevcik Adriana Solovicova K. Sekar M. Sundaralingam N. Genov Dong-cai Liang Tao Jiang Ji-ping Zhang Wen-rui Chang Wolfgang Jahnke Marcel Blommers S. C. Panchal R. V. Hosur Bindu Pillay Puniti Mathur S. Srivatsun Ratan Mani Joshi N. R. Jaganathan V. S. Chauhan H. S. Atreya S. C. Sahu K. V. R. Chary Girjesh Govil Elisabeth Adjadj Éric Quinjou Nadia Izadi-Pruneyre Yves Blouquit Joël Mispelter Bernadette Heyd Guilhem Lerat Philippe Milnard Michel Desmadreil Y. Lin B. D. Nageswara Rao Vidva Raghunathan Mei H. Chau Prashant Pesais Sudha Srivastava Evans Coutinho Anil Saran Leizl F. Sapico Jayson Gesme Herbert Lijima Raymond Paxton Thamarapu Srikrishnan C. R. Grace G. Nagenagowda A. M. Lynn Sudha M. Cowsik Sarata C. Sahu S. Chauhan A. Bhattacharya G. Govil Anil Kumar Maurizio Pellecchia Erik R. P. Zuiderweg Keiichi Kawano Tomoyasu Aizawa Naoki Fujitani Yoichi Hayakawa Atsushi Ohnishi Tadayasu Ohkubo Yasuhiro Kumaki Kunio Hikichi Katsutoshi Nitta V. Rani Parvathy R. M. Kini Takumi Koshiba Yoshihiro Kobashigawa Min Yao Makoto Demura Astushi Nakagawa Isao Tanaka Kunihiro Kuwajima Jens Linge Seán O. Donoghue Michael Nilges G. Chakshusmathi Girish S. Ratnaparkhi P. K. Madhu R. Varadarajan C. Tetreau Molecular Biophysics Unit Indian Institute of Science Bangalore India Austrian Academy of Sciences Institute of Biophysics and X-ray Structure Research Graz Austria Faculty of Biology University of Konstanz Germany Institute of Medical Biochemistry University of Graz Austria Howard Huges Medical Institute Department of Chemistry & Biochemistry University of California La Jolla USA Department of Chemistry & Biochemistry University of California San Diego La Jolla USA Molecular Biophysics Unit India Department of Microbiology &Cell Biology Indian Institute of Science Bangalore India Macromolecular Structure Laboratory NCI - Frederick Cancer Research and Development Center ABL - Basic Research Program Frederick USA Department of Crystallography and Biophysics University of Madras Chennai Biochemistry Department Indian Institute of Science Bangalore India Condensed Matter Physics Division B.A.R.C. Trombay Mumbai Condensed Matter Physics Division Bhabha Atomic Research Centre Trombay Mumbai IMCB The University of Tokyo Tokyo Japan Mitsubishi Chemical Corporation Yokohama Research Center Yokohama Japan Faculty of Pharmaceutical Sciences Chiba University Chiba Japan Department of Biophysics All India Institute of Medical Sciences New Delhi India Department of Biophysics All India Institute of Medical sciences New Delhi India Institüt Physiologische Chemie Hamburg Germany Biophysics Department Bose Institute Calcutta India Slovak Academy of Sciences Institute of Molecular Biology Bratislava Slovakia Indian Institute of Science Bioinformatics Centre Bangalore Departments of Chemistry and Biochemistry Biological Macromolecular Structure Center USA Bulgarian Academy of Sciences Institute of Organic Chemistry Sofia Bulgaria Chinese Academy of Sciences Institute of Biophysics Beijing China Novartis Pharma AG Preclinical Research Basel Switzerland Department of Chemical Sciences Tata Institute of Fundamental Research Mumbai India Solid State Physics Div

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Protein–nucleic acid interactions and DNA conformation in a complex of human immunodeficiency virus type 1 reverse transcriptase with a double‐stranded DNA template‐primer

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Biopolymers 1998年第2期44卷

作者： Jianping Ding Stephen H. Hughes Edward Arnold Center for Advanced Biotechnology and Medicine (CABM) and Rutgers University Chemistry Department 679 Hoes Lane Piscataway NJ 08854‐5638 ABL‐Basic Research Program NCI‐Frederick Cancer Research and Development Center P. O. Box B Frederick MD 21702‐1201

The conformation of the DNA and the interactions of the nucleic acid with the protein in a complex of human immunodeficiency virus type 1 (HIV‐1) reverse transcriptase (RT) and a 19‐mer/18‐mer double‐stranded DNA template‐primer (dsDNA) are described. The structure of this HIV‐1 RT complex with dsDNA serves as a useful paradigm for studying aspects of nucleotide polymerases such as catalysis, fidelity, drug inhibition, and drug resistance. The bound dsDNA has a bend of approximately 41° at the junction of an A‐form region (first five base pairs near the polymerase active site) and a B‐form region (the last nine base pairs toward the RNase H active site). The 41° bend occurs smoothly over the four base pairs between the A‐form portion and the B‐form portion in the vicinity of helices αH and αI of the p66 thumb subdomain. The interactions between the dsDNA and protein primarily involve the sugar—phosphate backbone of the nucleic acid and structural elements of the palm, thumb, and RNase H of p66, and are not sequence specific. Amino acid residues from the polymerase active site region, including amino acid residues of the conserved Tyr‐Met‐Asp‐Asp (YMDD) motif and the “primer grip,” interact with 3′‐terminal nucleotides of the primer strand and are involved in positioning the primer terminal nucleotide and its 3′‐OH group at the polymerase active site. Amino acid residues of the “template grip” have close contacts with the template strand and aid in positioning the template strand near the polymerase active site. Helix αH of the p66 thumb is partly inserted into the minor groove of the dsDNA and helix αI is directly adjacent to the backbone of the template strand. Amino acid residues of B1′, αA′, αB′, and the loop containing His539 of the RNase H domain interact with the primer strand of the dsDNA. © 1997 John Wiley & Sons, Inc. Biopoly 44: 125–138, 1997

关键词： AIDS DNA structure polymerase structure protein—DNA interaction x‐ray crystallography

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In-place inactivation of Pb in Pb contaminated soils

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ENVIRONMENTAL SCIENCE & TECHNOLOGY 1997年第5期31卷 1359-1364页

作者： Berti, WR Cunningham, SD Environmental Biotechnology Program DuPont Central Research & Development Glasgow Business Community 301 P.O. Box 6101 Newark Delaware 19714-6101

There has been increasing attention to the use of soil amendments and green plants to remediate surface soils contaminated with Pb. We call one form of this technique in-place inactivation. In-place inactivation reduces the hazards associated with contaminated soils through the use of chemicals that change the molecule species of the Pb to stabilize the soil Pb chemically and physically in situ. We have seen significant changes in soil Pb chemistry, Pb leached from soil, and Pb measured by a physiologically based extraction test (PBET) after incorporating inexpensive and readily available materials to three soils. The soils have total Pb concentrations that range from 1200 to 3500 mg kg(-1). The leachable soil Pb was significantly reduced in all cases from as high as 30 mg Pb L-1 to below the regulatory limit of 5 mg Pb L-1 after soil treatment. The PBET mimics the mammalian gastric-intestinal tract solutions. In the simulated intestinal phase of the PBET, Pb in solution was reduced by 72% in one of the soils treated with a high Fe-containing industrial byproduct. These results help to illustrate the utility of incorporating soil amendments to reduce hazards associated with Pb-contaminated soils.

关键词： Plants Soils Bioavailability Extraction Bioaccessibility

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Abstracts of papers presented at the 14th conference of the Weed Science Society of Israel Abstracts of papers presented at the international conference on controlled atmosphere and fumigation (CAF) in stored products Abstracts of papers presented at the joint international conference of FAOPMA — CEPA on pest control in the 21st century Abstracts of papers presented at the 2nd international Agro-Ecology Symposium on integrated pest management: from the drawing board to the market

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Phytoparasitica 1996年第3期24卷 199-265页

作者： E. Yogev M. Berson Y. Benyamini Y. Sheinboim T. Lev-Ran A. Bahat Y. Barkai Y. Gatti M. Zaidan O. Barazani Y. Boshvize S. Graph U. Luchinsky T. Blumenfeld Y. Kleifeld G. Herzlinger H. Bucsbaum S. Golan T. Chilf R. Aly Y. Ohali A. Ovadia Y. Chachlon H. Yovel Y. Tesler G. Colodney A. Nir S. Zarka A. Tal B. Rubin T. Yaacoby Y. Alon Y. Kedar Orit Ben-Zvi Assaraf O. Shainberg H. D. Rabinowitch E. Tel-Or Y. Goldwasser D. M. Joel D. Plakhine V. Portnoy G. Tzuri N. Katzir Dalia Losner-Goshen A. M. Mayer R. Jacobsohn Z. Tanaami H. Eisenberg Ziva Amsellem Z. Kernyi L. Hornok J. Gressel Adiva Shomer-Ilan Ela Nir Daphna Michaeli V. Kampel A. Warshawsky M. Yogev M. Negbi J. Hershenhorn Y. Lavan T. Hilf M. Horowitz M. Cohen I. Hirsch A. Veneziani S. T. Conyers C. H. Bell Ana C. Sá-Fischer C. S. Adler Ch. Reichmuth P. W. Flinn D. W. Hagstrum G. N. Mbata R. G. Winks Elisabeth A. Hyne M. Q. Chaudhry A. D. MacNicoll N. R. Price M. Schöller J. -F. Dugast R. Plarre S. Navarro E. J. Donahaye R. Diaz Miriam Rindner A. Azrieli P. Trematerra F. Fontana M. Mancini Ailsa D. Hocking Marta H. Taniwaki J. Lacey A. Hamer N. Magan N. Paster F. M. Caliboso D. G. Alvindia G. C. Sabio M. T. dela Cruz Okky Setyawati Dharmaputra A. S. R. Putri M. Sidik Eleni Papademetriou A. Varnava C. Mouskos M. A. Malek B. Parveen K. A. Dzisi W. O. Ellis Ana Maria Estevez Ljubica Galletti T. Fichet E. Oteiza L. A. Lizana M. X. Gonzalez B. Yakobson Y. Slavezky H. Ephrati El-H. Bartaly R. K. Kashyap M. Gupta W. L. Kashyap B. S. Dahiya A. K. Dash J. R. Rangaswamy R. D. Shroff D. S. Jayas W. E. Muir N. D. G. White L Gaye Weller J. E. van S. Graver Wu-Kang Peng M. Bengston E. Alip C. Reed J. G. Leesch G. F. Knapp G. F. Russell L. B. Llewellin Ch. Ulrichs H. J. Banks P. C. Annis R. Allanson R. Tauscher K. Westphal S. Mohan M. Gopalan P. C. Sumdarababu V. V. Sree Narayanan Sabine Prozell G. Ziegleder B. Schartmann R. Matissek J. Kraus D. Gerard S. Rogg W. Raemann R. F. Ryan Ya-Nan Wang R. T. Noyes P. Kenkel J. T. Criswell G. W. Cuperus C. J. Waterford C. P. Whittle L. Be Luxembourg Chemicals and Agriculture Ltd. Tel Aviv Israel Agrochemicals Dept. Milchan Bros. Ltd. Ramat Gan Israel Extension Service Ministry of Agriculture Zefat Mevo Hamma Ramat HaGolan Israel Dept. of Weed Science ARO Newe Ya’ar Research Center Haifa Israel Agrochemicals Department Milchan Bros. Ltd. Ramat Gan Israel Tarsis-Agrichem Tel Aviv Israel Weed Control Co. Ltd. Bet Dagan Israel Dept. of Field Crops Vegetables and Genetics The Hebrew University of Jerusalem Faculty of Agriculture Rehovot Israel Plant Protection and Inspection Services Ministry of Agriculture Bet Dagan 50250 Agan Chemical Manufacturers Ltd. Ashdod Israel Dept. of Field Crops Vegetables and Genetics Rehovot Dept. of Agricultural Botany The Hebrew University of Jerusalem Faculty of Agriculture Rehovot Israel Dept. of Weed Science ARO Newe Ya’ar Research Center Haifa Dept. of Botany The Hebrew University of Jerusalem Jerusalem Israel Dept. of Vegetable Crops ARO The Volcani Center Bet Dagan Israel Dept. of Plant Genetics Weizmann Institute of Science Rehovot Israel Inst. for Plant Science Agricultural Biotechnology Center Gödöllö Hungary Dept. of Botany Tel-Aviv University Tel Aviv Israel Dept. of Plant Genetics The Weizmann Institute of Science Rehovot Israel Dept. of Organic Chemistry The Weizmann Institute of Science Rehovot Israel Dept. of Ornamental Horticulture ARO The Volcani Center Bet Dagan Israel Weed Control Co. Ltd. Bet Dagan Chem-Nir Ltd. Kefar Shemaryahu Tiveon-Chem Co. Haifa Israel Central Science Laboratory Ministry of Agriculture Fisheries and Food Slough Berks UK Federal Biological Research Centre for Agriculture and Forestry Inst. for Stored Product Protection Berlin Germany USDA-ARS Grain Marketing and Production Research Center Manhattan USA School of Biological Sciences Abia State University Uturu Nigeria CSIRO Division of Entomology SCMC Nambour CSIRO Division of Entomology Canberra Australia DowElanco Europe Letcombe Laboratory L

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ABSTRACTS OF PAPERS PRESENTED AT THE INTERNATIONAL WORKSHOP ON BEMISIA SPP AN ASSESSMENT OF THE BIOLOGY AND MANAGEMENT STRATEGIES OF BEMISIA SPP FROM AN INTERNATIONAL PERSPECTIVE - OCTOBER 3-7, 1994 SHORESH HOTEL AND CONFERENCE CENTER, SHORESH, ISRAEL

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PHYTOPARASITICA 1994年第4期22卷 309-359页

作者： [Anonymous] Dept. of Entomology University of California Riverside USA Biosciences Research Laboratory USDA-ARS State University Station Fargo USA Dept. of Biology University of St. Thomas Houston Dept. of Biology University of St. Thomas Houston USA Dept. of Plant Sciences University of Arizona Tucson USA Dept. of Plant Sciences University of Arizona Tucson Dept. of Plant Science University of Arizona Tucson USA Dept. of Entomology Agricultural University Wageningen the Netherlands Dept. of Virus Research John Innes Institute Norwich Norfolk UK John Innes Centre Norwich Norfolk UK Dept. of Virus Research John Innes Institute Norwich UK Dept. of Zoology The George S. Wise Faculty of Life Sciences Tel Aviv University Ramat Aviv Israel Dept. of Zoology The George S. Wise Faculty of Life Sciences Tel-Aviv University Ramat Aviv Israel FONAIAP Centro de Investigaciónes Agropecuarias del Estado Lara (CIALA) Barquisimeto Venezuela FONAIAP Centro de Investigaciónes Agropecuarias del Estado Lara (CIALA) Barquisimeto Instituto National de Investigations Agrarias (INIA) Sección Proceso de Datos Area de Recursos Forestales Carretera de La Coruña Madrid Spain Centro de Investigaabn y Tecnologiá Agrarias (CITA) Laguna Tenerife Canary Islands Dept. of Entomology University of Arizona Tucson USA Dept. of Entomology and Nematology University of Florida Gainesville USA Texas A&M University Texas Agricultural Experiment Station Weslaco Dept. of Entomology University of Florida Gainesville USA Dept. of Entomology and Nematology University of Florida Gainesville California State University Fresno Kearney Agricultural Center University of California — Davis Parlier Western Cotton Research Laboratory USDA-ARS Phoenix Dept. of Entomology University of Arizona Maricopa Agricultural Center Maricopa Centro de Investigación y Tecnología Agrarias (CITA) Laguna Tenerife Canary Islands Instituto Nacional de Investigaciones Agrarias (INIA) Sección Proceso de Datos Area de Recur

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Review of HIV-1 reverse transcriptase three-dimensional structure: Implications for drug design

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Perspectives in Drug Discovery and Design 1993年第1期1卷 129-150页

作者： Nanni, Raymond G. Ding, Jianping Jacobo-Molina, Alfredo Hughes, Stephen H. Arnold, Edward Chemistry Department Center for Advanced Biotechnology and Medicine (CABM) and Rutgers University Piscataway 08854-5638 NJ 679 Hoes Lane United States ABL-Basic Research Program NCI-Frederick Cancer Research and Development Center Frederick 21702-1201 MD P.O. Box B United States

Two recent X-ray crystallographic studies have resulted in the three-dimensional structure determination of the reverse transcriptase (RT) enzyme from the human immunodeficiency virus type 1 (HIV-1) [Kohlstaedt et al., Science, 256 (1992) 1783;Jacobo-Molina et al., Proc. Natl. Acad. Sci. USA, 90 (1993) 6320]. This report reviews the structure of the reverse transcriptase heterodimer and provides a detailed description of the folding and topology of the individual subdomains. The interactions of the enzyme with bound template- primer are highlighted. Structure-function relationships have been established and are discussed for several conserved sequence motifs located within the enzyme. Each of these motifs is found to interact significantly with template-primer during the polymerization process. This review integrates the findings of both structure determinations, in particular, to relate these structures to strategies for drug design and development. The structures of both the nucleoside and nonnucleoside inhibitor binding sites are described, and the spatial relationship between the two sites is discussed in light of some novel possibilities for drug development. The first indication of an HIV-1 RT drug-resistant mutation manifested in the p51 subunit is presented. This mutation is located in a region of p51 that is proximal to the nonnucleoside binding pocket. The mechanisms of HIV-1 RT inhibition by both nucleoside and nonnucleoside classes of inhibitors are discussed in relation to the structure of the enzyme. In addition, the implications of the structure for understanding and avoiding the development of resistance of HIV-1 reverse transcriptase to antiviral inhibitors are discussed. © 1993 ESCOM Science Publishers B.V.

关键词： AIDS Antiviral agents Drug resistance Polymerase structure Protein-nucleic acid interactions Reverse transcriptase inhibitors

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STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE/dsDNA/Fab COMPLEX:PROTEIN-DNA INTERACTIONS AND STRUCTURE OF THE POLYMERASE ACTIVE SITE

STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE/dsDNA/Fab COMPLEX:P...

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Sixteenth Congress of the International Union of Crystallography

作者： J.Ding A.Jacobo-Molina R.G.Nanni X.Lu C.Tantillo A.D.Clark Jr. S.H.Hughes E.Arnold Center for Advanced Biotechnology and Medicine and Rutgers University Dept.of Chemistry 679 Hoes LanePiscatawayNJ 08854-5638 ABL-Basic Research Program NCI-Frederick Cancer Research and Development CenterFrederickMD 21702-1201

The crystal structure of a ternary complex of human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) heterodimer p66/p51,a 19 base/18 base dsDNA template-primer and a monoclonal antibody Fab fragment has been determined at 3.0 A resolution(7 A resolution structure reported in Nature 357:85-89,1992).The polymerase domains of both p66 and p51 contain four subdomains,which are named fingers,palm,thumb and connection(Kohlstaedt,L.A.,Wang,J.,Friedman,J.M., Rice,P.A.& Steitz,T.A.,Science 256:1783-1790,1992).

关键词： dsDNA HIV STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE/dsDNA/Fab COMPLEX:PROTEIN-DNA INTERACTIONS AND STRUCTURE OF THE POLYMERASE ACTIVE SITE Fab

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INTERCOMPARTMENTAL FLUID SHIFTS IN HEMODIALYSIS-PATIENTS

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biotechnology PROGRESS 1987年第2期3卷 69-73页

作者： HEINEKEN, FG EVANS, MC KEEN, ML GOTCH, FA COBE Laboratories Inc. Lakewood Colorado Fred G. Heineken is currently Program Director for Biotechnology within the Emerging Engineering Technologies Division of the Engineering Directorate of the National Science Foundation. He received his B.Sc. degree in Chemical Engineering from Northwestern University and his Ph.D. degree in the same discipline from the University of Minnesota. His work experience includes fermentation research at Monsanto teaching and research in respiration physiology at the University of Colorado and hemodialysis product design and evaluation at COBE Laboratories. Hemodialysis Treatment and Research Center Franklin Hospital Ralph K. Davis Medical Center San Francisco California Mary C. Evans has a BS degree in Chemistry from the University of Florida. She has held positions in the artificial kidney development group at Dow Chemical Company and the new product development group of Cordis-Dow Corporation. She is currently working in clinical research in the Hemodialysis Treatment & Research Center at Franklin Hospital in San Francisco. Marcia Keen is currently a doctoral student at the University of California San Francisco and serves as Clinical Research Supervisor at the Hemodialysis Treatment & Research Center at Franklin Hospital in San Francisco. She received her MS at the University of California San Francisco. Her thesis research developed a non-invasive Doppler technique to quantitate vascular access graft flow in hemodialysis patients. Her research interests include physiologic responses to dialysis therapy manipulations. Frank Gotch is an Associate Clinical Professor of Medicine at the University of California San Francisco. He received his BA and MD from the University of California and is currently Medical Director of the Hemodialysis Treatment & Research Center at Franklin Hospital in San Francisco. His research has addressed such issues as adequacy of dialysis and mathematical modeling of hemodialysis and associated therapies. He is a past president of the American

Hemodialysis is a therapeutic procedure for replacing some functions of the natural kidney. As such, it is capable of allowing people with little or no residual kidney function to survive and in some cases to lead productive lives. There are, unfortunately, a number of side effects associated with this procedure (shock, muscle cramps, fatigue, etc.). In order to minimize these side effects, we have undertaken to model shifts of fluid between the intracellular and extracellular fluid spaces in hemodialysis patients. Fluid shifts are primarily a function of osmolality differences between these fluid spaces. Changes in osmolality are caused mainly by changes in urea and salt concentrations. Least squares analysis of patient data has been used to estimate the appropriate ultrafiltration and urea mass transfer coefficients for each patient. The model has then been used to find a dialysate sodium concentration profile that will minimize fluid shifts into and out of the intracellular fluid space.

关键词： BIOMEDICAL EQUIPMENT

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Abstracts of short lectures

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Pharmaceutisch Weekblad 1987年第4期9卷 215-248页

作者： H. W. Rauwald J. Conner A. Gray T. Reynolds P. Waterman T. Hartmann R. -D. Adolph A. Ehmke H. Sander G. Toppel L. Witte Sz. Nyiredy O. Sticher C. A. J. Erdelmeier P. A. S. van Leeuwen A. D. Kinghorn K. Dallenbach-Tölke M. Wink Deirdre Hennessy Ingrid Hook Helen Sheridan R. Mersinger H. Dornauer E. Reinhard L. Heide M. Tabata K. Knobloch H. Jansen B. Müller T. Adzet R. Vila S. Cañigueral J. Budzianowski P. Bachmann F. -C. Czygan P. de Witte J. Lemli L. A. 't Hart P. H. van Enckevort R. P. Labadie R. van der Heijden H. H. M. de Keyzer E. R. Verhey J. Schripsema P. A. A. Harkes R. Verpoorte A. Baerheim Svendsen E. M. Croom W. Letchamo A. Vömel R. Bauer V. Wray H. Wagner A. Marston K. Hostettmann L. Andersson L. Bohlin M. Iorizzi R. Riccio L. Minale J. Moreno-Lopez T. A. van Beek H. van Bokhoven J. Kraus W. Blaschek G. Franz A. J. J. van den Berg M. H. Radema J. Corthout L. Pieters M. Claeys D. Vanden Berghe A. J. Vlietinck F. M. v. d. Dungen N. P. E. Vermeulen F. C. Fischer M. J. H. Gijbels P. W. J. Caspers M. J. M. Gijbels S. Y. Fung W. M. Herrebout W. M. J. van Gelder G. M. van der Graaf E. J. M. Pennings H. Huizer K. van Zuilen S. Kosasi T. van der Leer S. M. ten Hoope J. M. van der Nat W. G. van der Sluis R. v. d. Bosch J. A. Duine R. v. d. Heijden T. v. d. Leer L. A. Pieters J. Totté M. M. Saleh R. Z. Abbas J. H. Zwaving E. Sarer A. Looman J. J. C. Scheffer A. H. Meijer C. R. Langezaal J. M. Simons L. Van Hoof D. A. Vanden Berghe H. J. Woerdenbag H. Hendriks K. van der Berg R. van Stralen Th. M. Malingré A. W. T. Konings W. Lemstra S. Abdo M. De Bernardi G. Marinoni S. Samaniego G. Mellerio G. Vidari Y. Adjibadé B. Kuballa P. Cabalion R. Anton C. Ibáñez I. Monasterio S. M. Hussein Ayoub L. K. Yankov R. O. Ovtcharov C. Bartsch A. A. BaŞaran I. Calis S. Nishibe S. Berger P. Junior L. Kopanski N. Beuscher M. Billeter B. Meier M. Döll H. Braunewell L. Skrzypczak M. Wesolowska G. A. Gross T. Winkler M. L. Colombo F. Tome N. Crespi-Perellino A. Guicciardi A. Minghetti E. Speroni F. Vincieri P. Vita-Finzi B. Gabetta A Institute of Pharmaceutical Biology University of Frankfurt Frankfurt/M. F.R.G. Phytochemistry Research Laboratories Department of Pharmacy University of Strathclyde Glasgow Scotland Jodrell Laboratory Royal Botanic Gardens Richmond England Institut für Pharmazeutische Biologie der T.U. Braunschweig F.R.G. Pharmazeutisches Institut Zürich Switzerland Pharmaceutical Institute University of Tübingen F.R.G. Pharmazeutisches Institut Eidgenössische Technische Hochschule Zürich Zürich Switzerland Dipartimento Scienze Farmaceutichc Bologna Italy Program for Collaborative Research in the Pharmaceutical Sciences and Department of Medicinal Chemistry and Pharmacognosy College of Pharmacy University of Illinois at Chicago Chicago USA Clinical Pharmacokinetics Laboratory College of Pharmacy University of Illinois at Chicago Chicago USA Institut für Pharmazeutische Biologie Universität München München 2 F.R.G. Department of Pharmacognosy School of Pharmacy Trinity College Dublin Dublin 4 Ireland Institut für Pharmazie der Universität Mainz Mainz F.R.G. Pharmazeutisches Institut Universität Tübingen Tübingen F.R.G. Pharmaceutical Institute University of Tübingen Tübingen F.R.G. Institut für Pharmazeutische Biologie Universität Bonn Bonn 1 F.R.G. Department of Pharmacognosy Faculty of Pharmaceutical Sciences Kyoto University Kyoto Japan Institut für Botanik und Pharmazeutische Biologie der Universität Erlangen-Nürnberg Erlangen F.R.G. Institut für Botanik und Pharmazeutische Biologie der Universität Erlangen-Nürnberg Erlangen F.R.G. Laboratory of Pharmacology and Pharmacognosy Faculty of Pharmacy University of Barcelona Barcelona Spain Department of Pharmaceutical Botany K. Marcinkowski Medical Academy Poznań Poland Lehrstuhl für Pharmazeutische Biologie der Universität Würzburg Würzburg F.R.G. Lehrstuhl für Pharmazeutische Biologie der Universität Würzburg Würzburg F.R.G. Laboratorium voor Farmaceutische Biologie en Fytofarmacologie K.U. Leuvan Leuven Bel

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Basic methods in molecular biology /

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1986年

作者： Davis Leonard G.

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