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Preview FEBS Letters 1996: Vol 378-399 Index

— - FEBS|N 4a843%- AN INTERNATIONAL JOURNAL FOR THE RAPID PUBLICATION OF SHORT REPORTS IN BIOCHEMISTRY, BIOPHYSICS AND MOLECULAR CELL BIOLOGY , supplement | FEBLAL 399 (Suppl.) 1-100 ISSNO 014 5793 @mazky LETTERS An international journal established for the most rapid possible publication of essentialflinya l short papers in the field of Biochemistry, Biophysics and Molecular Cell Biology Published by Elsevier Science B.V. on behalf of the FEDERATION OF EUROPEAN BIOCHEMICAL SOCIETIES FEBS Letters is intended to be a journal for the fast dissemination of significant and novel work in an essentially complete form. It is NOT the vehicle for preliminary or fragmentary observations, or for ‘leftovers’ from larger papers, or for material which, although sound, does not have to appear quickly, or is addressed to a small audience only. As a rule, for example, we do not publish incomplete sequences, or sequences which are known in other species; or incomplete NMR or other spectroscopic assignments; or the conventionally achieved crystallisation of a protein; or the conven- tionally achieved expression of a gene in bacteria or yeast; or just negative observations. Also, methodological papers are not usually published by us, unless they are truly novel and significant. The overriding criterion is that a paper must be of sufficient immediate importance to justify urgent publication. As space is finite, we are forced to refuse papers which, although sound, do not have top priority. We apologise, therefore, for ‘approving but not publishing’ such manuscripts. Attention of the authors is drawn to the fact that our rejection procedure may take as long as in other journals, as explained elsewhere (see FEBS Letters, 217 (1987) 143-144. 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AVILA, Centro de Biologia Molecular, ‘Severo Ochoa’, CSIC — Universidad Autonoma, E-28049 Madrid, Spain (34-1-397-47-99; E-mail: [email protected]) M. BAGGIOLINI, Th. Kocher-Institut, Universitat Bern, Freiestrasse 1, CH-3012 Berne, Switzerland (41-31-631-3799; E-mail: [email protected]) H. EKLUND, Department of Molecular Biology, BMC, PO Box 590, S-75124 Uppsala, Sweden (46-18-53-6971 ; E-mail: [email protected]) H. FELDMANN, Institut fiir Physiologische Chemie, Physikalische Biochemie und Zellbiologie, Munich University, Schillerstrasse 44, D-80336 Miinchen, Germany (49-89-59 96 316; E-mail: feldmann@dec]!.bio.med.uni-muenchen.de) U.-I. FLUGGE, Lehrstuhl Botanik II, Gyrhofstr. 15, 50931 Kéln, Germany (49-221-470-5039; E-mail: [email protected]) T. GOJOBORI, Center for Information Biology, National Institute of Genetics, Mishima, Shizuoka-ken, 411, Japan (81-559-81-6848; E-mail: [email protected]) B. HALLIWELL, Pharmacology Group, King’s College, Chelsea Campus, Manresa Road, London SW3 6LX, England (44-171-333-4949) J. HANOUNE, Unite de Recherches, INSERM U-99, Hopital Henri Mondor, 94010 Créteil, France (33-1-48-98-09-08 ; E-mail: [email protected]) H. HOLZER, Biochemisches Institut der Universitat, Hermann-Herder-Str. 7, D-79104 Freiburg i.Br., Germany (49-761-203-5253; E-mail: [email protected]) Th.L. JAMES, UCSF Magnetic Resonance Laboratory, Department of Pharmaceutical Chemistry, 926 Medical Science, San Francisco, CA 94143-0446, USA (1-415- 502-4690; E-mail: [email protected]) P. JOLLES, Laboratoire de Chimie des Substances Naturelles, URA CNRS 401, Proteins/Glycoconjugates/Enzymes, Muséum National d'Histoire Naturelle, 63, rue Buffon, F 75005 Paris, France (33-1-4079-3122) L. KISSELEV, Engelhardt Institute of Molecular Biology, 32, Vavilov str., Moscow 117984, Russia (7-095-135-1405; E-mail: [email protected]) C. KLEE, Laboratory of Biochemistry, NCI, Bldg. 37, Room 4E 28, 37 Convent DR. MSC 4255, Bethesda, MD 20892-4255, USA (1-301-402-3095; E-mail: [email protected]) N. MANTEI, Neurobiologie, ETH-Hénggerberg, CH-8093 Ziirich, Switzerland (41-1-633-1046; E-mail: [email protected]) T. MASAKI, Department of Pharmacology, Kyoto University, Faculty of Medicine, Kyoto 606, Japan (81-75-753-4402; E-mail: [email protected]) P. MATHIS, Dept. de Biologie Moléculaire et Cellulaire, Section de Bioénergétique, Bat. 532, C.E. Saclay, F 91191 Gif-sur-Yvette, France (33-1-69-08-87-17:; E-mail: [email protected]) M. MONTAL, Department of Biology, Science Building, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA (1-619-534 0931; E-mail: [email protected]) M.J. OWEN, Imperial Cancer Research Fund, PO Box 123, 44 Lincoln’s Inn Fields, London WC2A 3PX, England (44-171-269-3479; E-mail: [email protected]) P.J. RANDLE, Nuffield Department of Clinical Biochemistry, Radcliffe Infirmary, Woodstock Rd., Oxford OX2 6HE, England (44-1865-224 000) S. SHALTIEL, The Kleeman Professor of Biochemistry, Head, Department of Biological Regulation, The Weizmann Institute of Science, Rehovot 76100, Israel (972-8-9342 804; E-mail: [email protected]) V.P. SKULACHEV, Department of Bioenergetics, A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia* (7-095-939-0338; E-mail: [email protected]) A.V. SOMLYO, Department of Molecular Physiology and Biological Physics, Box 449, University of Virginia, 1300 Jefferson Park Avenue, Charlottesville, VA 22908, USA (1-804-982-1616; E-mail: [email protected]) G. TETTAMANTI, Universita degli Studi di Milano, Facolta di Medicina e Chirurgia, Dipartimento di Chimica e Biochimica Medica, Via Saldini, 50, | 20133 Milano, Italy (39-2-236-3584; E-mail: [email protected]) M. VAN MONTAGU, Laboratorium voor Genetika, Universiteit Gent, Ledeganckstraat 35, B-9000 Gent, Belgium (32-9-264-5349; E-mail: [email protected]) G. VON HEIJNE, Department of Biochemistry, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden (46-8-15-36-79; E-mail: [email protected]) F. WIELAND, Institut fiir Biochemie I, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany (49-6221-544-366; E-mail: [email protected]) Sh. YAMAMOTO, Department of Biochemistry, Tokushima University School of Medicine, Kuramoto-cho, Tokushima 770, Japan (81-886-33-6409) Published weekly. Printed in The Netherlands. (@) The paper used in this publication meets the requirements of ANSI/NISO Z39.48-1992 (Permanence of Paper) Elsevier Science B.V., PO Box 211, 1000 AE Amsterdam, The Netherlands MASTER INDEX VOLUMES 378-399 FEBLAL Volume 399 (Suppl.) 1-100 | (maleKyLETTER An international journal for the rapid publication of short reports in biochemistry, biophysics and molecular cell biology EDITORS J. Avila, Madrid T. Masaki, Kyoto M. Baggiolini, Berne P. Mathis, Saclay J.E. Celis, Aarhus M. Montal, La Jolla S.P. Datta, London, Honorary Chairman M.J. Owen, London H. Eklund, Uppsala P.J. Randle, Oxford H. Feldmann, Minchen M. Saraste, Heidelberg, Reviews Editor U.-l. Flugge, KdIn G. Semenza, Zurich, Managing Editor T. Gojobori, Shizuoka-ken S. Shaltiel, Rehovot B. Halliwell, London V.P. Skulachev, Moscow J. Hanoune, Créteil A.V. Somlyo, Charlottesville H. Holzer, Freiburg i.Br. G. Tettamanti, Milan Th.L. James, San Francisco M. Van Montagu, Gent P. Jolles, Paris G. von Heijne, Stockholm L. 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USA POSTMASTERS: Send address changes to FEBS Letters, Publications Expediting, Inc., 200 Meacham Avenue, Elmont, NY 11003. Airfreight and mailing in the USA by Publications Expediting. FEBS Letters Volumes 378—399 Master Author Index Volumes 378—399 (1996) A Akhoundova, A. see A.E. Busch (395) 153 Akimov, S.S. see Y.E. Yegorov (389) 115 Akira, S. see M. Matsumoto (395) 143 Akira, S. see T. Sugiyama (381) 191 Akisue, T. see K. Shimooku (387) 141 Akiyama, M. see A. Tomomura (386) 26 Aarden, L.A. see J.P.J. Brakenhoff (395) 235 Akiyama, T. see O. Higuchi (396) 81 Aarsman, A.J. see M.J.B.M. Vervoordeldonk (397) 108 Akiyama, T. see M. Seishima (398) 120 Abal, M. see J. Gualix (391) 195 Akiyama, Y., A. Kihara and K. Ito, Subunit a of proton ATPase Fy Abastado, J.-P. see A. Quesnel (387) 42 sector is a substrate of the FtsH protease in Escherichia coli (399) 26 Abbott, F.S. see G.S. Baldwin (384) 58 Akparov, V.Kh. see T.A. Gudasheva (391) 149 Abdallah, M.A. see A. Ocaktan (396) 243 Aktories, K. see J. van Damme (380) 291 Abdulaev, N.G. see V.S. Pashkov (381) 119 Akutsu, H. see K. Tozawa (397) 122 Abdulkarim, F., M. Ehrenberg and D. Hughes, Mutants of EF-Tu Alakhov, V. see I. Astafieva (389) 278 defective in binding aminoacyl-tRNA (382) 297 Alape-Giron, A., B. Stiles, J. Schmidt, M. Giron-Cortes, M. Abe, H. see S. Sakuma (398) 165 Thelestam, H. Jérnvall and T. Bergman, Characterization of Abe, K. see T. Misaka (381) 208 multiple nicotinic acetylcholine receptor-binding proteins and Abee, C.R. see L. Morelli (379) 132 phospholipases Ay from the venom of the coral snake Micrurus Abel, P. see A.P. Stubbs (383) 237 nigrocinctus nigrocinctus (380) 29 Abella, A. see C. Claise (398) 223 Alban, C. see S. Aubert (383) 175 Abelskov, A.K. see L. Ostergaard (398) 243 Albanese, V. see S. Sipione (384) 19 Aberg, A. see D.E.A. Birse (384) 215 Albanesi, J.P. see S. Earnest (396) 62 Aberg, A. see S. Doublié (384) 219 Alberghina, M. see S. Sipione (384) 19 Abid, Md.R. see K. Sasaki (384) 151 Albertini, R., S. Rindi, A. Passi, G. Pallavicini and G. De Luca, Abraham, E.P. see P.A. Whiteman (394) 31 Heparin protection against Fe?*-and Cu**-mediated oxidation of Acharya, K.R. see V. Calderone (394) 91 liposomes. (383) 155 Acharya, K.R. see M. Kontou (389) 195 Aledo, J.C. see H.S. Hundal (384) 204 Adachi, A. see Y. Fujii (393) 93 Aledo, J.C., E. Hajduch, F. Darakhshan and H.S. Hundal, Analyses Adachi, A. see Y. Fujii (393) 105 of the co-localization of cellubrevin and the GLUT4 glucose Adachi, A. see Y. Fujii (395) 257 transporter in rat and human insulin-responsive tissues (395) 211 Adachi, O. see H. Izu (394) 14 Aleshin, A.E., C. Zeng, H.J. Fromm and R.B. Honzatko, Adachi, T. see Y. Tada (391) 341 Crystallization and preliminary X-ray analysis of human brain Adam, C. and J.G. Bieth, Inhibition of neutrophil elastase by the hexokinase (391) 9 ( -proteinase inhibitor-immunoglobulin A complex (385) 201 Alessi, D.R., F.B. Caudwell, M. Andjelkovic, B.A. Hemmings and P. Adami, R. see P. Cuneo (397) 136 Cohen, Molecular basis for the substrate specificity of protein Adams, B., R. Fowler, M. Hudson and R.H. Pain, The role of the kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase C-terminal lysine in the hinge bending mechanism of yeast (399) 333 phosphoglycerate kinase (385) 101 Alexandratos, J. see G. Bujacz (398) 175 Adcock, I. see E.-B. Haddad (379) 265 Alexandre, D. see Y. Anouar (394) 295 Addlesee, H.A., L.C.D. Gibson, P.E. Jensen and C.N. Hunter, Alfano, M. see V. Grazioli (388) 134 Cloning, sequencing and functional assignment of the chlorophyll Alho, H. see R. Aejmelaeus (384) 128 biosynthesis gene, ch/P, of Synechocystis sp. PCC 6803 (389) 126 Alizadeh, P. and D. J. Klionsky, Purification and biochemical Adelman, J.P. see S.J. Tucker (390) 253 characterization of the ATH/ gene product, vacuolar acid Adermann, K. see J.J. Calvete (379) 207 trehalase, from Saccharomyces cerevisiae (391) 273 Adinolfi, S., R. Piccoli, F. Sica and L. Mazzarella, BS-R Nase Allan, B.B. see D. Schmoll (383) 63 tetramers: an example of domain-swapped oligomers (398) 326 Allemann, R.K. see A.G.E. Kiinne (391) 79 Adler, K., G. Gerisch, U. von Hugo, A. Lupas and A. Schweiger, Allen, J.F., Reply to Commentary by Helmut Beinert and Patricia Classification of tyrosine kinases from Dictyostelium discoideum Kiley (382) 220 with two distinct, complete or incomplete catalytic domains (395) Allen, S., J. Davies, A.C. Dawkes, M.C. Davies, J.C. Edwards, M.C. 286 Parker, C.J. Roberts, J. Sefton, $.J.B. Tendler and P.M. Williams, Adman, E.T. see M. Kukimoto (394) 87 In situ observation of streptavidin-biotin binding on an Aducci, P. see M. Marra (382) 293 immunoassay well surface using an atomic force microscope (390) Adzhubei, A.A., I.A. Adzhubei, I.A. Krasheninnikov and S. Neidle, 161 Non-random usage of ‘degenerate’ codons is related to protein Allen, T.M. see P.S. Uster (386) 243 three-dimensional structure (399) 78 Almeida, R.P. see V. Witko-Sarsat (382) 130 Adzhubei, I.A. see A.A. Adzhubei (399) 78 Alok, D. see D. Pillai (387) 23 Aebersold, R. see J.D. Watts (398) 217 Alonso, A. see F.M. Goni (390) 1 Aejmelaeus, R., T. Metsdé-Ketela, P. Laippala and H. Alho, Is there Aloria, K. see M. Llosa (397) 283 an unidentified defence mechanism against infection in human Altamura, N., N. Capitanio, N. Bonnefoy, S. Papa and G. Dujardin, plasma? (384) 128 The Saccharomyces cerevisiae OXA1] gene is required for the correct Aeschlimann, D. see H. Chen (387) 36 assembly of cytochrome c oxidase and oligomycin-sensitive ATP Agapov, I.I. see A.G. Tonevitsky (392) 166 synthase (382) 111 Ahmad, M.B. see K.U. Devi (396) 123 Altendorf, K. see A. Iwane (396) 172 Ahnert-Hilger, G. see B. Niirnberg (389) 61 Altendorf, K. see A. Ménard (386) 161 Aicardi, G. see D. Platano (391) 189 Altshuller, Y., N.G. Copeland, D.J. Gilbert, N.A. Jenkins and M.A. Ailhaud, G. see J. Aubert (397) 117 Frohman, Gem], a mammalian homolog of Drosophila Glial Cells Aimoto, S. see S. Miki (399) 241 Missing (393) 201 Aistrup, G.L., M. Szentirmay, K.N. Kumar, K.K. Babcock, R.L. Altura, B.M. see M.A. Delpiano (394) 335 Schowen and E.K. Michaelis, lon channel properties of a protein Alvarez, A.M. see I. Fabregat (384) 14 complex with characteristics of a glutamate/N-methyl-p-aspartate Alves, J. see G. Grabowski (381) 106 receptor (394) 141 Amada, F. see N. Kunishima (378) 291 Aitken, A. see G.M. Smith (396) 90 Amano, O. see Y. Sai (392) 25 Akamatsu, Y. see K. Saito (395) 262 Amano, T. see K. Tozawa (397) 122 Akao, T., T. Fukumoto, H. Ihara and A. Ito, Conformational change Amchenkova, A. see A. Vartanian (381) 32 in DNA induced by cationic bilayer membranes (391) 215 Amemiya, K. see K. Fujita (395) 293 Akhmanova, A., K. Miedema and W. Hennig, Identification and Ames, R.S., P. Nuthulaganti and C. Kumar, In Xenopus oocytes the characterization of the Drosophila histone H4 replacement gene human C3a and CSa receptors elicit a promiscuous response to the (388) 219 anaphylatoxins (395) 157 Volumes 378—399 (1996) Amler, E. see M. Opekarova (386) 181 Anwaruzzaman, Y. Nakano and A. Yokota, Different location in Amontov, S. see H. Sugiyama (392) 215 dark-adapted leaves of Phaseolus vulgaris of ribulose-1,5- Amontoyv, S., S. Nishikawa and K. Taira, Dependence on Mg** ions bisphosphate carboxylase/oxygenase and 2-carboxyarabinitol of the activities of dimeric hammerhead minizymes (386) 99 1-phosphate (388) 223 Amorim, A. see L. Morelli (379) 132 Aoki, T., Y. Takahashi, K.S. Koch, H.L. Leffert and H. Watabe, Amoroso, D. see M.G. Cattaneo (397) 164 Construction of a fusion protein between protein A and green Ampe, C. see M. Van Troys (397) 191 fluorescent protein and its application to Western blotting (384) Amsterdam, A. see F. Pitzer (394) 47 193 An, B., J.-R. Jin, P. Lin and Q.P. Dou, Failure to activate interleukin Aoto, M. see S. Sahara (384) 138 1B-converting enzyme-like proteases and to cleave retinoblastoma Aplin, R.T. see J.A.E. Kraunsoe (396) 108 protein in drug-resistant cells (399) 158 Appella, E. see M. Miller (399) 166 An, S. and K.A. Knox, Ligation of CD40 rescues Ramos-Burkitt Aradi, J. see S. Tokeés (396) 43 lymphoma B cells from calcium ionophore- and antigen receptor- Aragon, I. see M.D. Ardell (389) 213 triggered apoptosis by inhibiting activation of the cysteine protease Arai, S. see T. Misaka (381) 208 CPP32/Yama and cleavage of its substrate PARP (386) 115 Arakawa, T. see N. Nishioka (396) 333 An, W. see M.J. McLaren (387) 63 Arav, R. and I. Friedberg, Combined effects of ATP and its analogs Anadon, R. see P. Carpintero (394) 103 on the membrane permeability in transformed mouse fibroblasts Ananthapadmanaban, D., Commentary on: “Thermostability of (387) 149 B-xylosidase from Aspergillus sydowii MG49’ by M. Gosh and G. Araya, Z., M. Norlin and H. Postlind, A possible role for CYP27 as a Nanda, FEBS Letters 330, 275-278 (1993) (385) 244 major renal mitochondrial 25-hydroxyvitamin Ds; la-hydroxylase Andersen, G., A. Poterszman, J.M. Egly, D. Moras and J.-C. Thierry, (390) 10 The crystal structure of human Cyclin H (397) 65 Arbatsky, N.P. see A.A. Kramerov (378) 213 Andersen, N.H., Z. Liu and K.S. Prickett, Efforts toward deriving the Arciero, D.M. see J.A. Zahn (397) 35 CD spectrum of a 3,9 helix in aqueous medium (399) 47 Ardell, M.D., I. Aragon, L. Oliveira, G.E. Porche, E. Burke and S.J. Anderson, J.M. see M.S. Balda (399) 326 Pittler, The § subunit of human rod photoreceptor cGMP-gated Anderson, V.E. see M. Gdtte (390) 226 cation channel is generated from a complex transcription unit (389) Andersson, H., I. Nilsson and G. von Heijne, Calnexin can interact 213 with N-linked glycans located close to the endoplasmic reticulum Arden, J. see Z. Wang (387) 53 . membrane (397) 321 Arends, S., J. Kraus and H. Beier, The tRNA‘ multigene family of Andjelkovic, M. see D.R. Alessi (399) 333 Triticum aestivum: genome organization, sequence analyses and Andra, J., O. Berninghausen, J. Wiilfken and M. Leippe, Shortened maturation of intron-containing pre-tR NAs in wheat germ extract amoebapore analogs with enhanced antibacterial and cytolytic (384) 222 activity (385) 96 Arendt, T. see C. Janke (379) 222 Andra, S., G. Frey, M. Nitsch, W. Baumeister and K.O. Stetter, Arenz, A. see C. Drewke (390) 179 Purification and structural characterization of the thermosome Arese, P. see E. Schwarzer (388) 119 from the hyperthermophilic archaeum Methanopyrus kandleri (379) Argibay, J. see A. Mijares (399) 188 127 Ariel, N. see B. Velan (395) 22 Andrade-Gordon, P. see K.H. Mayo (378) 79 Arita, H. see T. Nakano (387) 75 André, B., A.A. Noegel and M. Schleicher, Dictyostelium discoideum Arita, H. see T. Nakano (387) 78 contains a family of calmodulin-related EF-hand proteins that are Arlaud, G.J. see J.-M. Lancelin (391) 203 developmentally regulated (382) 198 Arlaud, G.J. see S. Pelloux (386) 15 André, F. see E. Pinet (395) 217 Armand, S. see B. Iseli (382) 186 Andreani-Mangeney, M., Y. Vandenbrouck, B. Janvier, D. Girlich Armato, U. see M. Menegazzi (379) 279 and G. Bereziat, Transcriptional regulation of apolipoprotein E Armbrecht, H.J., V.J. Wongsurawat, T.L. Hodam and N. expression by cyclic AMP (397) 155 Wongsurawat, Insulin markedly potentiates the capacity of Andréasson, L.-E. see J. Kurreck (381) 53 parathyroid hormone to increase expression of 25-hydroxyvitamin Andreeva, N. see E. Gustchina (379) 60 D;-24-hydroxylase in rat osteoblastic cells in the presence of 1,25- Andreeva, S.G. see E.A. Feshchenko (381) 149 dihydroxyvitamin Ds (393) 77 Andréoni, C. see A. Robert (390) 327 Armitage, I.M. see C.W. Peterson (379) 85 Andrews, S.C. see N.E. Le Brun (397) 159 Armstrong, P.B. see K. Dolmer (393) 37 Andrieu, J.-P. see P. Guy (395) 53 Arnold, L. see S. Limmer (385) 15 Andriolo, M. see B. Chini (397) 201 Arnold, R.S. and A.C. Newton, Diacylglycerol directly stimulates the Anel, A. see 8. Gamen (390) 233 insulin receptor tyrosine kinase (380) 58 Anemiiller, S. see C.L. Schmidt (388) 43 Arnon, R. see D. Avichezer (395) 103 Anfuso, C.D. see S. Sipione (384) 19 Aro, H.T. see J. Rantakokko (393) 307 Angelotti, T. and F. Hofmann, Tissue-specific expression of splice Arrondo, J.L.R., F.J. Blanco, L. Serrano and F.M. Goni, Infrared variants of the mouse voltage-gated calcium channel «2/8 subunit evidence of a B-hairpin peptide structure in solution (384) 35 (397) 331 Arseniev, A.S. see E.V. Bocharov (379) 291 Aniento, F., A.G. Papavassiliou, E. Knecht and E. Roche, Selective Arseniev, A.S. see V.S. Pashkov (381) 119 uptake and degradation of c-Fos and v-Fos by rat liver lysosomes Arthington-Skaggs, B.A., D.N. Crowell, H. Yang, S.L. Sturley and (390) 47 M. Bard, Positive and negative regulation of a sterol biosynthetic Ankarcrona, M., J.M. Dypbukt, S. Orrenius and P. Nicotera, gene (ERG3) in the post-squalene portion of the yeast ergosterol Calcineurin and mitochondrial function in glutamate-induced pathway (392) 161 neuronal cell death (394) 321 Arthur, J.R. see G. Bermano (387) 157 Anouar, Y., S. Jegou, D. Alexandre, I. Lihrmann, J.M. Conlon and Artur, Y. see T. Masmoudi (379) 181 H. Vaudry, Molecular cloning of frog secretogranin II reveals the Arumugam, S. see W. Huang (384) 155 occurrence of several highly conserved potential regulatory Asahara, H. see N. Nameki (396) 201 peptides (394) 295 Asahi, S. see T. Nakaya (378) 145 Anraku, Y. see I. Tanida (379) 38 Asano, A. see N. Mimura (397) 253 Ansorge, S. see S. Wrenger (383) 145 Ashcroft, F.M. see S.J. Tucker (390) 253 Antonsson, P. see A. Oldberg (386) 29 Ashley, R.H. see S. Howell (390) 207 Antropova, O. see I. Kuznetsova (383) 105 Askari, A. see G. Liu (390) 323 Antsypovich, S.I., T.S. Oretskaya, E.A. Romanova, E.M. Volkov, Asselberghs, S. see P.P. Van Veldhoven (388) 80 V.N. Tashlitsky, M. Vasser and Z.A. Shabarova, Synthesis and Asselin, J. see N.J. Willmott (386) 39 properties of cross-linked DNA duplexes (378) 224 Assert, R., H. Schatz and A. Pfeiffer, Upregulation of PKC 6- and Antz, C. see H. WeiBhoff (387) 201 downregulation of PKC a-mRNA and protein by a phorbol ester in human T84 cells (388) 195 Assfalg-Machleidt, I. see C. Randak (398) 97 Volumes 378—399 (1996) Assfalg-Machleidt, I. see N. Schaschke (391) 297 Bachelot, C. see H. Falet (383) 165 Assunta Costa, M. see G. Duro (399) 295 Bachi, T. see A. Robert (390) 327 Astafieva, I., I. Maksimova, E. Lukanidin, V. Alakhov and A. Bachmann, M., J.L. Huber, G.S. Athwal, K. Wu, R.J. Ferl and S.C. Kabanov, Enhancement of the polycation-mediated DNA uptake Huber, 14-3-3 proteins associate with the regulatory and cell transfection with Pluronic P85 block copolymer (389) 278 phosphorylation site of spinach leaf nitrate reductase in an isoform- Atabekov, J.G. see N.O. Kalinina (397) 75 specific manner and reduce dephosphorylation of Ser-543 by Athwal, G.S. see M. Bachmann (398) 26 endogenous protein phosphatases (398) 26 Atkin, A. see R. Heller (389) 225 Bachmann, M., J.L. Huber, P.-C. Liao, D.A. Gage and S.C. Huber, Atlante, A., T.M. Seccia, E. Marra, G.M. Minervini, V. Vulpis, A. The inhibitor protein of phosphorylated nitrate reductase from Pirrelli and S. Passarella, Carrier-mediated transport controls spinach (Spinacia oleracea) leaves is a 14-3-3 protein (387) 127 hydroxyproline catabolism in heart mitochondria from Backstrém, G. see J. Kreysing (385) 181 spontaneously hypertensive rat (396) 279 Badasso, M.O. see J.B. Cooper (387) 105 Atlas, D. see O. Wiser (379) 15 Bade, E.G. see K. Sultan (394) 51 Attaix, D. see L. Combaret (393) 292 Badman, M.K., K.I.J. Shennan, J.L. Jermany, K. Docherty and A. Attal, J.. M.-C. Theron, F. Taboit, M. Cajero-Juarez, G. Kann, P. Clark, Processing of pro-islet amyloid polypeptide (prolAPP) by Bolifraud and L.M. Houdebine, The RU5 (‘R’) region from human the prohormone convertase PC2 (378) 227 leukaemia viruses (HTLV-1) contains an internal ribosome entry Baeg, G.-H. see O. Higuchi (396) 81 site (IRES)-like sequence (392) 220 Baehr, W. see L. Feng (395) 77 Aubert, J.,G. Ailhaud and R. Negrel, Evidence for a novel regulatory Baehr, W. see S.L. Semple-Rowland (385) 47 pathway activated by (carba)prostacyclin in preadipose and Baerends, R.J.S. see M. Veenhuis (383) 114 adipose cells (397) 117 Baeuerle, P.A. see H.L. Pahl (392) 129 Aubert, S. see M. Padua (398) 248 Bag, J. see J.S. Grewal (383) 267 Aubert, S., C. Alban, R. Bligny and R. Douce, Induction of B- Bagavathi, S. and R. Malathi, Introns and protein revolution — An methylcrotonyl-coenzyme A carboxylase in higher plant cells analysis of the exon/intron organisation of actin genes (392) 63 during carbohydrate starvation: evidence for a role of MCCase in Bagdasarian, M. see Y. Taguchi (388) 169 leucine catabolism (383) 175 Baggiolini, M. see K. Rajarathnam (399) 43 Aubry, F., M.-G. Mattei, J.-P. Barque and F. Galibert, Bagshaw, C.R. see P.B. Conibear (380) 13 Chromosomal localization and expression pattern of the RNase L Baier-Bitterlich, G. see W. Schobersberger (397) 263 inhibitor gene (381) 135 Bailey, V.C., S.M. Fortt, R.J. Summerhill, A. Galione and B.V.L. Auer, M. see R. Csonga (380) 209 Potter, Cyclic aristeromycin diphosphate ribose: a potent and Auerswald, E.A. see C. Randak (398) 97 poorly hydrolysable Ca**-mobilising mimic of cyclic adenosine Auger, G., J. van Heijenoort, J.C. Vederas and D. Blanot, Effect of diphosphate ribose (379) 227 analogues of diaminopimelic acid on the meso-diaminopimelate- Bailly, C., A.M innock and M.J. Waring, A simple ligation assay to adding enzyme from Escherichia coli (391) 171 detect effects of drugs on the curvature/flexibility of DNA (396) 253 Aumelas, A. see M.E. Mangoni (383) 93 Bailly, C., S. Routier, J.-L. Bernier and M.J. Waring, DNA Aunis, D. see R. Kannan (385) 159 recognition by two mitoxantrone analogues: influence of the Aunis, D. see J. Strub (379) 273 hydroxyl groups (379) 269 Aussel, L. see I. Fobis-Loisy (397) 149 Bailly, P. see B. Olives (386) 156 Authier, F., B.I. Posner and J.J.M. Bergeron, Endosomal proteolysis Bajor, T. see A. Hrabak (390) 203 of internalized proteins (389) 55 Baker, E.N. see M.C. Bewley (386) 215 Auzou, G. see S. Jalaguier (384) 112 Baker, E.N., T.L. Bluntell, M. Vijayan, E. Dodson, G. Dodson, G.L. Avaeva, S., P. Ignatov, S. Kurilova, T. Nazarova, E. Rodina, N. Gilliland and J.L. Sussman, Publication of macromolecular crystal Vorobyeva, V. Oganessyan and E. Harutyunyan, Escherichia coli structures (380) 302 inorganic pyrophosphatase: site-directed mutagenesis of the metal Baker, J. see A. Slominski (399) 175 binding sites (399) 99 Bakhanashvili, M., O. Avidan and A. Hizi, Mutational studies of Avaeva, S.M., E.V. Rodina, S.A. Kurilova, T.I. Nazarova and N.N. human immunodeficiency virus type | reverse transcriptase: the Vorobyeva, Effect of D42N substitution in Escherichia coli involvement of residues 183 and 184 in the fidelity of DNA inorganic pyrophosphatase on catalytic activity and Mg** binding synthesis (391) 257 (392) 91 Balashova, T.A. see V.S. Pashkov (381) 119 Averna, M. see M. Michetti (392) 11 Bald, R. see M. Griine (385) 114 Avichezer, D. and R. Arnon, Differential reactivities of the Arachis Balda, M.S., J.M. Anderson and K. Matter, The SH3 domain of the hypogaea (peanut) and Vicia villosa B4 lectins with human ovarian tight junction protein ZO-1 binds to a serine protein kinase that carcinoma cells, grown either in vitro or in vivo xenograft model phosphorylates a region C-terminal to this domain (399) 326 (395) 103 Baldwin, G.S., F.S. Abbott and H. Nau, Binding ofa valproate Avidan, O. see M. Bakhanashvili (391) 257 metabolite to the trifunctional protein of fatty acid oxidation (384) Avila, J. see M. Llosa (397) 283 58 Awaji, T. see A. Hirasawa (386) 141 Baldwin, J.E. see M.-H. Lee (393) 269 Axelrod, J. see C.C. Felder (393) 231 Baldwin, S.A. see S. Boyer (396) 218 Axmann, S.E. see R. Zahn (380) 152 Balestre, M.-N. see B. Chini (397) 201 Azibi, K. see D. Jung (381) 15 Balint, R.F. see J.W. Larrick (398) 74 Azzi, A. see O. Cantoni (389) 285 Ballesta, J.J. see F. Vicente-Agullo (399) 83 Azzi, A. see L. Palomba (390) 91 Ballicora, M.A. see S. Mora-Garcia (380) 123 Ballio, A., F. Bossa, L. Camoni, D. Di Giorgio, M.-C. Flamand, H. Maraite, G. Nitti, P. Pucci and A. Scaloni, Structure of fuscopeptins, phytotoxic metabolites of Pseudomonas fuscovaginae B (381) 213 Ballmer-Hofer, K. see R. Meili (394) 34 Bally, I. see J.-M. Lancelin (391) 203 Banba, N. see K. Kasai (394) 137 Bandyopadhyay, G. see M.L. Standaert (388) 26 Banfalvi, Z., A. Molnar, G. Molnar, L. Lakatos and L. Szabo, Starch Baader, S.L., E. Bill, A.X. Trautwein, G. Bruchelt and B.F. synthesis-, and tuber storage protein genes are differently expressed Matzanke, Mobilization of iron from cellular ferritin by ascorbic in Solanum tuberosum and in Solanum brevidens (383) 159 acid in neuroblastoma SK-N-SH cells: an EPR study (381) 131 Bang, N.U. see U. Reuning (392) 125 Baba, M. see J.P. Merin (394) 9 Bangert, K. see U. Christensen (387) 58 Babcock, K.K. see G.L. Aistrup (394) 141 Bangio, H. see A. Liberzon (388) 5 Babkina, I.N. see S.V. Seregin (382) 79 Bangio, H. see E. Yona (382) 97 Bachellerie, J.-P. see M.-H. Renalier (379) 212 Banhegyi, G. see L. Braun (388) 173 Volumes 378—399 (1996) Banhegyi, G. see L. Braun (390) 183 Beavers, M.P. see K.H. Mayo (378) 79 Banhegyi, G., M. Csala, L. Braun, T. Garzo and J. Mandl, Ascorbate Bec-Ferte, M.-P., H.B. Krishnan, A. Savagnac, S.G. Pueppke and J.- synthesis-dependent glutathione consumption in mouse liver (381) C. Promé, Rhizobium fredii synthesizes an array of 39 lipooligosaccharides, including a novel compound with glucose Banki, K. and A. Perl, Inhibition of the catalytic activity of human inserted into the backbone of the molecule (393) 273 transaldolase by antibodies and site-directed mutagenesis (378) 161 Beck, K.-F. and R.B. Sterzel, Cloning and sequencing of the proximal Bafiuelos, S. and A. Muga, Interaction of native and partially folded promoter of the rat iNOS gene: activation of NF«B is not sufficient conformations of a-lactalbumin with lipid bilayers: for transcription of the iNOS gene in rat mesangial cells (394) 263 characterization of two membrane-bound states (386) 21 Becker, G.W. see C.C. Felder (393) 231 Barak, D. see B. Velan (395) 22 Beck-Sickinger, A.G. see B. Rist (394) 169 Baralle, F.E. see R. Pariyarath (397) 79 Bedford, M. see C.S. Fishburn (381) 257 Baranov, A.V. see A.V. Feofanov (396) 289 Bedmar, E.J. see M. Fernandez-Lopez (392) | Baratova, L. see M. Kovina (392) 293 Beekman, B., J.W. Drijfhout, W. Bloemhoff, H.K. Ronday, P.P. Tak Barberis, C. see B. Chini (397) 201 and J.M. te Koppele, Convenient fluorometric assay for matrix Barbieri, L. see F. Olivieri (396) 132 metalloproteinase activity and its application in biological media Barbieri, L. see F. Stirpe (382) 309 (390) 221 Barbouche, R., N. Marrakchi, P. Mansuelle, M. Krifi, E. Fenouillet, Beerhues, L., Benzophenone synthase from cultured cells of H. Rochat and M. El Ayeb, Novel anti-platelet aggregation Centaurium erythraea (383) 264 polypeptides from Vipera lebetina venom: isolation and Beermann, F. see V. del Marmol (381) 165 characterization (392) 6 Behrendt, N. and K. Dang, Effect of purified, soluble urokinase Barbrook, A.C., J.C.L. Packer and C.J. Howe, Inhibition by penem receptor on the plasminogen—pro-urokinase activation system (393) of processing peptidases from cyanobacteria and chloroplast 3] thylakoids (398) 198 Beiche, F., S. Scheuerer, K. Brune, G. Geisslinger and M. Goppelt- Barcellona, M.L. see M. Renis (390) 153 Struebe, Up-regulation of cyclooxygenase-2 mRNA in the rat Barchi Jr., J.J. see X. Huang (393) 280 spinal cord following peripheral inflammation (390) 165 Barciszewski, J., G.E. Siboska, B.O. Pedersen, B.F.C. Clark and Beier, H. see S. Arends (384) 222 S.I.S. Rattan, Evidence for the presence of kinetin in DNA and cell Beinert, H. and P. Kiley, Redox control of gene expression involving extracts (393) 197 iron-sulfur proteins. Change of oxidation-state or assembly/ Bard, M. see B.A. Arthington-Skaggs (392) 161 disassembly of Fe-S clusters? (382) 218 Bard, M. see T. Husselstein (381) 87 Beintema, J.J. see K.I. Panov (398) 57 Bardouille, C., D. Vullhorst and H. Jockusch, Expression of chloride Beitz, E. see H. Vélkel (378) 245 channel | mRNA in cultured myogenic cells: a marker of myotube Bektas, M. see C.C. Geilen (378) 88 maturation (396) 177 Beldman, G. see S.M. Pitson (398) 7 Barenholz, Y. see D. Glick (394) 237 Belikov, S.V. see D.A. Papatsenko (381) 103 Barford, D. see C. MacKintosh (397) 235 Bell, J. see S.W. Reid (383) 119 Barhanin, J. see M. Fink (378) 64 Bell, J.D. see A.V.W. Nunn (392) 295 Barklis, E. see C.B. Clish (378) 43 Bellmann, K., M. Jaattela, D. Wissing, V. Burkart and H. Kolb, Heat Barlow, S.W. see R. Rafaeloff (378) 219 shock protein hsp70 overexpression confers resistance against nitric Barnard, M.L. see A.V.W. Nunn (392) 295 oxide (391) 185 Barnard, R.J.O. see A.W. Sudlow (393) 185 Bellvé, A.R. see A. Liévano (388) 150 Barnes, P.J. see E.-B. Haddad (379) 265 Beltramini, M. see T. Zlateva (384) 251 Barque, J.-P. see F. Aubry (381) 135 Belyavsky, A.V. see A.E. Popsueva (391) 5 Barr, F.A. and W.B. Huttner, A role for ADP-ribosylation factor 1, Ben-Aroya, N. see L. Nur Levi (379) 186 but not COP I, in secretory vesicle biogenesis from the trans-Golgi Bendinelli, P., R. Piccoletti, P. Maroni and A. Bernelli-Zazzera, The network (384) 65 MAP kinase cascades are activated during post-ischemic liver Barre, A. see E.J.M. Van Damme (397) 352 reperfusion (398) 193 Barron-Casella, E. see V.T. Nachmias (378) 258 Benen, J. see P. Biely (382) 249 Barsova, E. see A. Fradkov (390) 145 Benfenati, F. see E. Chieregatti (398) 211 Bartelsen, O. see S. Lansmann (399) 227 Benito, A. see X. Carbonell (397) 169 Barton, G.J. see A. Fiser (397) 225 Benito, M. see I. Fabregat (384) 14 Bartorelli, A. see F. Ceciliani (393) 147 Benjannet, S. see N.G. Seidah (379) 247 Barwise, J.L. and J.H. Walker, Subcellular localization of annexin V Benjannet, S. see M. Zhong (396) 31 in human foreskin fibroblasts: nuclear localization depends on Ben-Meir, D. see A. Spungin-Bialik (380) 79 growth state (394) 213 Benne, R. see D. Speijer (381) 123 Barylko, B. see S. Earnest (396) 62 Benner, S.A. see N. Trabesinger-Ruef (382) 319 Baskova, I. see A. Fradkov (390) 145 Bennett, A.J., J.S. Bruce, A.M. Salter, D.A. White and M.A. Billett, Bassi, R. see L. Riboni (391) 336 Hepatic microsomal triglyceride transfer protein messenger RNA Bassi, R. see M.G. Testi (399) 245 concentrations are increased by dietary cholesterol in hamsters Batkin, M. see A. Chestukhin (382) 265 (394) 247 Batra, J.K. see D. Rathore (392) 259 Bentura, M.L. see M. Cueto (398) 159 Batra, R.S., R. Brown, G.K. Brown and I.W. Craig, Molecular Benveniste, P. see T. Husselstein (381) 87 cloning and tissue-specific expression of mouse kidney 6- Berchtold, M.W. see U. Débbeling (391) 131 phosphofructo-2-kinase/fructose-2,6-bisphosphatase (393) 167 Berden, J.A. see H. Boumans (390) 137 Battistuta, R. see J. Ottl (398) 31 Berden, J.A. see G. Lobo-Hajdu (395) 199 Baudry, N., P.-J. Lejeune, P. Niccoli, L. Vinet, P. Carayon and B. Berezhnoy, S. see A. Fradkov (390) 145 Mallet, Dityrosine bridge formation and thyroid hormone Bereziat, G. see M. Andreani-Mangeney (397) 155 synthesis are tightly linked and are both dependent on N-glycans Berezov, T.T. see N.V. Koudinova (395) 204 (396) 223 Berg, A. see C. Dennison (394) 340 Baum, M. and A. Schén, Localization and expression of the closely Berg, B. see M. Graessmann (394) 233 linked cyanelle genes for RNase P RNA and two transfer RNAs Bergeron, J.J.M. see F. Authier (389) 55 (382) 60 Berglund, T., G. Kalbin, A. Strid, J. Rydstr6m and A.B. Ohlsson, Baumeister, W. see S. Andra (379) 127 UV-B- and oxidative stress-induced increase in nicotinamide and Baumeister, W. see F. Pitzer (394) 47 trigonelline and inhibition of defensive metabolism induction by Baumeister, W. see T. Tamura (398) 101 poly(ADP-ribose)polymerase inhibitor in plant tissue (380) 188 Baxter, N.J. see A.J. Charlton (382) 289 Bergman, A.-C. and T. Bergman, Micropreparation of peptides by Bayer, P. see D. Hirschl (383) 31 capillary electrophoresis for matrix assisted laser desorption mass Beadle, D.J. see L.A. Obosi (381) 233 spectrometry (397) 45 Beatriz see M.A. Noventa-Jordaéd (378) 32 Bergman, T. see A. Alape-Giron (380) 29

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