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Preview FEBS Letters 1991: Vol 278-295 Index

FEBS=| a8i4.% : AN INTERNATIONAL JOURNAL FOR THE RAPID PUBLICATION OF SHORT REPORTS IN BIOCHEMISTRY, BIOPHYSICS AND MOLECULAR CELL BIOLOGY Published by Elsevier on behalf of the Federation of European Biochemical Societies Volume 295, Supplement FEBLAL 295 (Suppl.) 1-70 ISSN 00145793 f@alzkyJ LETTERS An international journal established for the most rapid possible publication of essentially final short papers in the field of Biochemistry, Biophysics and Molecular Cell Biology Published by Elsevier Science Publishers B.V. on behaolf fth e FEDERATION OF EUROPEAN BIOCHEMICAL SOCIETIES A Federation of Biochemical Societies in Austria, Belgium, Bulgaria, Czechoslovakia, Denmark, Estonia, Finland, France, Germany, Great Britain, Greece, Hungary, Iceland, Ireland, Israel, Italy, Latvia, Lithuania, The Netherlands, Norway, Poland, Portugal, Rumania, Spain, Sweden, Switzerland, Turkey, USSR, Yugoslavia. 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 As a rule, for example, we do not publish incomplete sequences, or sequences which are known in other species; or incomplete NMR or other spectroscopic assignments; or the conventionally achieved 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 impor- tance to justify urgent publication. 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. For details on the preparation of the manuscripts, see our ‘Notes’ (e.g. FEBS Letters, Volume 290, No. 1,2, pp. 256—257 and thereafter at the end of each tenth volume, i.e. at the end of Vol. 300, 310, 320 etc.). The authors should submit their papers to the Editor who is the closest to their field of interest (rather than geographically): this accelerates the reviewing process. The authors are urged to submit one of the copies of their paper, if at all possible, as a floppy disk (see under Notes to Authors). This also accelerates the handling process and reduces the danger of misprints eventually appearing. Note: telefax numbers are included below (in parentheses). *When corresponding with these editors it is preferable to use a courier service. Editors: G. SEMENZA (Managing Editor), Eidgenéssische Technische Hochschule Ziirich, Laboratorium fiir Biochemie, ETH-Zentrum, Universitatstrasse 16, CH-8092 Ziirich, Switzerland (41-1-252-8744) S.P. DATTA (Honorary Chairman), London, England M. SARASTE (Reviews Editor) EMBL, Meyerhofstrasse |, Postfach 10.2209, D-W-6900 Heidelberg, Germany (49-6221-387306) H.R.V. ARNSTEIN (Editor of the Index of Biochemical Reviews and book reviews), London, England E. BOCK, The Protein Laboratory, University of Copenhagen, Panum Institute, 3C Blegdamsvej, bld. 6.2, DK-2200 Copenhagen N, Denmark (45-35-360-116) J.E. CELIS, Department of Medical Biochemistry, Ole Worms Allé, Building 170, University Park, Aarhus University, DK-8000 Aarhus, Denmark (45-86-131-160) J.M. GANCEDO, Instituto de Investigaciones, Biomédicas, CSIC, Calle Arturo Duperier 4, 28029 Madrid, Spain (34-1-585-4015) B. HALLIWELL, Division of Pulmonary-Critical Care Medicine, UC Davis Medical Center, 4301 X St., Sacramento, CA 95817, USA (1-916-734-7924) J. HANOUNE, Unité de Recherches, INSERM U-99, Hopital Henri Mondor, 94010 Créteil, France (33-1-48-98-09-08) P.M. HARRISON, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Firth Court, Western Bank, Sheffield, S10 2UH, England (44-742-728-697) M. HATANAKA, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606, Japan (81-75-761-5626) G. HAUSKA, Universitat Regensburg, Lehrstuhl fiir Zellbiologie und Pflanzenphysiologie, Universitatstrasse 31, Postfach 397, D-W-8400 Regensburg 31, Germany (49-941 -943-2305) H. HOLZER, Biochemisches Institut der Universitat, Hermann-Herder-Str. 7, D-W-7800 Freiburg i1.Br., Germany (49-761-203-3331) P. JOLLES, Laboratory of Proteins/Enzymes/Glycoconjugates, CNRS/Université de Paris V, 45, rue des Saint-Péres, F 75270 Paris Cedex 06, France (33-1-4015-9296) C. KLEE, NIH, National Cancer Institute, Laboratory of Biochemistry, Bldg. 37, Room 4E-28, Bethesda, MD 20892, USA (1-301-402-3095) A. KOTYK, Institute of Physiology, Czechoslovak Academy of Sciences, KRC, Videiiska 1083, 142 20 Praha 4, Czechoslovakia (42-24712253) N. MANTEI, Laboratorium fiir Biochemie, ETH Zentrum, Universitatstrasse 16, CH 8092 Ziirich, Switzerland (41-1-252-8744) 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) A.D. MIRZABEKOYV, Institute of Molecular Biology, Academy of Sciences of the USSR, Vavilov str. 32, 117984 Moscow B-334, USSR* (7-095-135-1405) Sh. MIZUSHIMA, Institute of Applied Microbiology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo 113, Japan (81-3-3818-9435) M.J. OWEN, Imperial Cancer Research Fund, PO Box 123, Lincoln’s Inn Fields, London WC2A 3PX, England (44-71-269-3479) P.J. RANDLE, Nuffield Department of Clinical Biochemistry, John Radcliffe Hospital, Oxford OX3 9DU, England (44-865-220348) T.A. RAPOPORT, Zentralinstitut fiir Molekularbiologie, Robert Réssle-Strasse 10, 1115 D-O-Berlin-Buch, Germany (37-2-349-4161) M. SARASTE, EMBL, Meyerhofstrasse |, Postfach 10.2209, D-W-6900 Heidelberg, Germany (49-6221-387306) R. SATO, Osaka University, Institute for Protein Research, 3-2 Yamadaoka, Suita, Osaka 565, Japan (81-6-876-2533) S. SHALTIEL, The Weizmann Institute of Science, Rehovot 76100, Israel (972-8-465-488) V.P. SKULACHEYV, A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, 119899 Moscow, USSR* (7-095-939-0338) A.V. SOMLYO, Department of Physiology, Box 449, University of Virginia, 1300 Jefferson Park Avenue, Charlottesville, VA 22908, USA (1-804-982-1616) G. TETTAMANTI, Universita degli Studi di Milano, Facolta di Medicina e Chirurgia, Dipartimento di Chimica e Biochimica Medica, Via Saldini, 50, I 20133 Milano, Italy (39-2-236-3584) G. WAGNER, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA (1-617-432-4383) J.H. WEIL, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire des Plantes (IBMP), 12, rue du General Zimmer, F 67084 Strasbourg, France (33-88-6 1-4442) Published weekly. This journal is printed on acid-free paper Printed in The Netherlands. Elsevier Science Publishers B.V., PO Box 211, 1000 AE Amsterdam, The Netherlands alk LETTERS MASTER INDEX VOLUMES 278-295 FEBLAL 295 (Suppl.) 1-70 lg@falzky LETTER An international journal for the rapid publication of short reports in biochemistry, biophysics and molecular cell biology EDITORS H.R.V. Arnstein, London, Book Reviews Editor P. Mathis, Saclay E. Bock, Copenhagen A.D. Mirzabekov, Moscow J.E. Celis, Aarhus Sh. Mizushima, Tokyo S.P. Datta, London, Honorary Chairman M.J. Owen, London J.M. Gancedo, Madrid P.J. Randle, Oxford B. Halliwell, Sacramento T.A. Rapoport, Berlin-Buch P.M. Harrison, Sheffield M. Saraste, Heidelberg, Reviews Editor J. Hanoune, Créteil R. Sato, Osaka M. Hatanaka, Kyoto G. Semenza, Zurich, Managing Editor G. Hauska, Regensburg S. Shaltiel, Rehovot H. Holzer, Freiburg i.Br. V.P. Skulachev, Moscow P. Jollés, Paris V.P. Somlyo, Charlottesville C. Klee, Bethesda G. Tettamanti, Milan A. Kotyk, Prague G. Wagner, Boston N. Mantei, Zurich J.H. 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Box 1110, Greens Farms, CT 06436-1110, U.S.A., Tel.: 203-261.2500; Fax: 203-261.0101 FEBS Letters Volumes 278-295 Master Author Index Volumes 278-295 (1991) A Alafia, A., M.J. Llama and J.L. Serra, Purification and some properties of the pectin lyase from Penicillium italicum (280) 335 Albracht, S.P.J. see S. Rospert (291) 371 Alfandari, D. see J. -F. Riou (279) 346 Ali, S.T. see D.E. Brookfield (295) 13 Alimov, A.A. see A.V. Zelenin (280) 94 Aatsinki, J. see A. Pulkka (291) 289 Alimov, A.A. see A.V. Zelenin (287) 118 Ab, G. see M.J. de Hoop (291) 299 Allen, A.G. and R.N. Perham, Two lipoyl domains in the Abad, C. see E. Pérez-Paya (278) 51 dihydrolipoamide acetyltransferase chain of the pyruvate Abarca, D., M. Fernandez-Lobato, L. del Pozo and A. Jiménez, dehydrogenase multienzyme complex of Streptococcus faecalis (287) Isolation of a new gene (SWA2) encoding an a-amylase from 206 Schwanniomyces occidentalis and its expression in Saccharomyces Allen, J.F. see M.A. Harrison (282) 295 cerevisiae (279) 41 Allende, J. see V. Pulgar (292) 85 Abbondanza, A. see M. Chiricolo (291) 173 Allocatelli, C.T. see F. Cutruzzola (282) 281 Abdulaev, N.G. see M.A. Kutuzov (293) 21 Almendros, G., R. Friind, F.J. Gonzalez-Vila, K.M. Haider, H. Abdulaev, N.G. see M.A. Kutuzov (289) 179 Knicker and H.-D. Liidemann, Analysis of '*C and '"N CPMAS Abe, S. see K. Umezawa (279) 132 NMR- spectra of soil organic matter and composts (282) 119 Abe, E. see T. Sato (285) 21 Alsina, M.M. see T. Yoneda (278) 171 Abe, K. see H. Kondo (278) 87 Altendorf, K. see B. Schneppe (292) 145 Aberg, F. see P. Forsmark (285) 39 Alvarez, L., M. Asuncion, F. Corrales, M.A. Pajares and J.M. Mato, Abergel, C. see C. Devaux (286) 64 Analysis of the 5’ non-coding region of rat liver S- Abramov, V.M. see V.P. Zav’yalov (278) 187 adenosylmethionine synthetase mRNA and comparison of the Abramov, V.M. see E.E. Galyov (286) 79 M, deduced from the cDNA sequence and the purified enzyme (290) Ackerman, M.S. see B.P. England (279) 87 142 Ackerman, S.H., D.L. Gatti, P. Gellefors, M.G. Douglas and A. Alzar, P.M. see C. Devaux (286) 64 Tzagoloff, ATP/3, a nuclear gene of Saccharomyces cerevisiae Amaya, Y. and A. Nakano, SRH/ protein, the yeast homologue of essential for the expression of subunit 9 of the mitochondrial the 54 kDa subunit of signal recognition particle, is involved in ER ATPase (278) 234 translocation of secretory proteins (283) 325 Adamiker, D. see A. Buchstaller (287) 27 Amberger, A., H. Bauer, U. Tontsch, G. Gabbiani, O. Kocher and Adams, P.D. and P.J. Parker, TPA-induced activation of MAP kinase H.C. Bauer, Reversible expression of sm q@-actin protein and sm (290) 77 a-actin mRNA in cloned cerebral endothelial cells (287) 223 Adler, L. see L. André (286) 13 Ambrosini, A., E.A. Barnard and G. Prestipino, AMPA and kainate- Aebersold, R. see E. Schwartz (280) 229 operated channels reconstituted in artificial bilayers (281) 27 Affranchino, J.L., G.D. Pollevick and A.C.C. Frasch, The expression Ambudkar, I.S. see V.J. Horn (282) 289 of the major shed Trypanosoma cruzi antigen results from the Amemiya, Y. see M. Nakasako (292) 73 developmentally-regulated transcription of a small gene family Amerik, A.Yu., V.K. Antonov, A.E. Gorbalenya, S.A. Kotova, T.V. (280) 316 Rotanova and E.V. Shimbarevich, Site-directed mutagenesis of La Afonina, E.I., N.V. Chichkova and A.A. Bogdanov, NA-RNA and protease: A catalytically active serine residue (287) 211 RNA-protein interactions in 30 S ribosomal subunits: Association Amess, B. see H.A. Manjarrez-Hernandez (292) 121 of 16 S rRNA fragments in the presence of ribosomal proteins (283) Amesz, J. see M. Kobayashi (284) 129 251 Amlaiky, N. see J.P. Montmayeur (278) 239 Agerberth, B., C.-G. Ostenson, S. Efendic and H. Jérnvall, Pancreatic Amouric, M. see B. Miszczuk-Jamska (294) 175 secretory trypsin inhibitor (PSTI) isolated from pig intestine: Anborgh, P.H., G.W.M. Swart and A. Parmeggiani, Kirromycin- Influence on insulin and somatostatin release (281) 227 induced modifications facilitate the separation of EF-Tu species and Agerberth, B. see T. Bergman (283) 100 reveal intermolecular interactions (292) 232 Ahlner, J. see V. Chhajlani (290) 157 Andersen, T.M.M. see S.R. Krystek (281) 212 Ahmad, H. see S.S. Singhal (281) 255 Andersen, J.K. see P. Urban (286) 142 Ahmed, K. see S.A. Goueli (282) 445 Andersen, G.R., L. Jacobsen, S. Thirup, J. Nyborg and L. Sottrup- Ahsan, C.R. and J. Sasaki, A 64 kDa protein from Mycobacterium Jensen, Crystallization and preliminary X-ray analysis of bovis BCG shares the same antigenic determinants with line 10 methylamine-treated a,-macroglobulin and 3 a@,-macroglo- hepatoma cells and has anti-line 10 tumor activity (288) 77 bulin—proteinase complexes (292) 267 Aicardi, G., A. Pollo, E. Sher and E. Carbone, Noradrenergic Anderson, C.M. and J. Gray, Cleavage of the precursor of pea inhibition and voltage-dependent facilitation of Q-conotoxin- chloroplast cytochrome f by leader peptidase from Escherichia coli sensitive Ca channels in insulin-secreting RINmSF cells (281) 201 (280) 383 Aimoto, S. see I. Fujimoto (287) 15 Anderson, L. see K.A. Eidne (292) 243 Aimoto, S. see K. Ramalingam (295) 200 Anderson, K. see W. Meikrantz (291) 192 Aimoto, S. see R. Takayanagi (282) 103 Anderson, J.M. see B.R. Jordan (284) 5 Aissani, B. see A. De Sario (295) 22 Anderson, L.E. see C.L. Skrukrud (280) 259 Aitken, A. see H.A. Manjarrez-Hernandez (292) 121 Andersson, M., J.-C. Marie, M. Carlquist and V. Mutt, The Aiyar, J. see A. Karschin (278) 229 preparation of biotinyl-€-aminocaproylated forms of the vasoactive Akagi, H., K. Hirai and F. Hishinuma, Cloning of a glycine receptor intestinal polypeptide (VIP) as probes for the VIP receptor (282) 35 subtype expressed in rat brain and spinal cord during a specific Andersson, B. see I. Virgin (287) 125 period of neuronal development (281) 160 Andersson, A.-M. see H. Gaardsvoll (294) 94 Akasaka, K. see R. Ishima (294) 64 Ando, H. see K. Taniyama (278) 222 Akazawa, T. see J. Pozueta-Romero (287) 62 Ando, A. see M. Fukunaga (285) 265 Akazawa, T. see J. Pozueta-Romero (291) 233 André, L., A. Hemming and L. Adler, Osmoregulation in Akimaru, J. see H. Tokuda (279) 233 Saccharomyces cerevisiae: Studies on the osmotic induction of Akita, H. see K. Hirata (287) 181 glycerol production and glycerol 3-phosphate dehydrogenase Akiyoshi-Shibata, M., E. Usui, T. Sakaki, Y. Yabusaki, M. Noshiro, (NAD) (286) 13 K. Okuda and H. Ohkawa, Expression of rat liver vitamin D, Andreansky, Martin, O. Hruskova-Heidingsfeldova, J. Sedlacek, J. Konvalinka, I. Blaha, Petr Jeémen, M. Hofejgi, P. Strop and M. 25-hydroxylase cDNA in Saccharomyces cerevisiae (280) 367 Akizuki, N., K. Kangawa, N. Minamino and H. Matsuo, Cloning and Fabry, High-level expression of enzymatically active bovine sequence analysis of complementary DNA encoding a precursor for leukemia virus proteinase in E. coli (287) 129 chicken natriuretic peptide (280) 357 Andreasen, P.A. see M. Munch (295) 102 Aksenova, M.V., G.S. Burbaeva, K.V. Kandror, D.V. Kapkov and Andreasen, J.J. see M. Bersani (283) 189 A.S. Stepanov, The decreased level of casein kinase 2 in brain cortex Andrews, S.C., J.M.A. Smith, S.J. Yewdall, J.R. Guest and P.M. of schizophrenic and Alzheimer’s disease patients (279) 55 Harrison, Bacterioferritins and ferritins are distantly related in Aktories, K. see G. Koch (291) 336 evolution: Conservation of ferroxidase-centre residues (293) 164 Aktories, K. see K.H. Reuner (286) 100 Andrews, E.R., J.M. Pratt and K.L. Brown, Molecular recognition in Akutsu, H. see J.-S. Park (285) 149 the binding of vitamin B,, by the cobalamin-specific Intrinsic Factor Alakhov, Y. see G.G. Jokhadze (289) 190 (281) 90 Andronico, F. see E. Sarubbi (279) 265 2 Volumes 278-295 (1991) Andronova, T.M. see M.V. Sumaroka (295) 48 Arrol, S. see M.I. Mackness (286) 152 Anemiiller, S. see P. Hildebrandt (283) 131 Aruoma, O.I. see B. Halliwell (281) 9 Ankilova, V.N. see E.V. Bobkova (290) 95 Aryee, D. see D.L. Lewis (290) 17 Anselme, J. and M. Hartlein, Tyr-426 of the Escherichia coli Asahi, M. see K. Sakai (294) 104 asparaginyl-tRNA synthetase, an amino acid in a C-terminal Asaka, J. see H. Suzuki (283) 281 conserved motif, is involved in ATP binding (280) 163 Asano, T. see M. Kobayashi (293) 106 Antonenko, Y.N. see O.N. Kovbasnjuk (289) 176 Ascenzi, P. see F. Cutruzzola (282) 281 Antonenko, Yu.N., K.W. Kinnally, S. Perini and H. Tedeschi, Asher, O., C. Provenzano and S. Fuchs, Regulation of acetylcholine Selective effect of inhibitors on inner mitochondrial membrane receptor gene expression in rats treated with a-bungarotoxin (282) channels (285) 89 242 Antonioli, S. see I. Giambanco (290) 131 Ashton, D.S., C.R. Beddell, D.J. Cooper, B.N. Green, R.W.A. Oliver Antonov, V.K. see A.Yu. Amerik (287) 211 and K.J. Welham, Some electrospray mass spectrometric evidence Antonov, V.K. see E.P. Sablina (283) 291 for the existence of covalent O-acyl enzyme intermediates (292) 201 Aoki, I., Y. Shindoh, T. Nishida, S. Nakai, Y.-M. Hong, M. Mio, T. Aslanian, D. see M. Négrerie (292) 249 Saito and K. Tasaka, Comparison of the amino acid and nucleotide Aslanidi, K.B., L.J. Boitsova, L.M. Chailakhyan, L.N. Kublik, LI. sequences between human and two guinea pig major basic proteins Marachova, T.V. Potapova and T.A. Vinogradova, Energetic (282) 56 cooperation via ion-permeable junctions in mixed animal cell Aoki, I., Y. Shindoh, T. Nishida, S. Nakai, Y.-M. Hong, M. Mio, cultures (283) 295 Tadayuki Saito and K. Tasaka, Sequencing and cloning of the Asuncion, M. see L. Alvarez (290) 142 cDNA of guinea pig eosinophil major basic protein (279) 330 Aszodi, A. see P. Friedrich (295) 5 Aono, Y. see S. Orita (295) 127 Athauda, S.B.P., T. Takahashi, H. Inoue, M. Ichinose and K. Appella, E. see J.G. Omichinski (292) 25 Takahashi, Proteolytic activity and cleavage specificity of cathepsin Apps, D. see J. Gillespie (282) 69 E at the physiological pH as examined towards the B chain of Apte, S., M.-G. Mattei and B.R. Olsen, Cloning of human @1(X) oxidized insulin (292) 53 collagen DNA and localization of the COLIOAI gene to the q21-— Atkins, A.R. see R.G. Mills (282) 247 q22 region of human chromosome 6 (282) 393 Atomi, H. see Yu. Fukuda (286) 61 Arad, R. see R. Brandes (285) 63 Atreyi, M. see M.V.R. Rao (278) (1990) 63 Arad, T. see S. Weiner (285) 49 Aubert, J.-P. see K. Tokatlidis (282) 205 Arai, M. see H. Ide (284) 161 Aubert, J.-P. see K. Tokatlidis (291) 185 Arai, S. see H. Kondo (278) 87 Audigier, S. see A. Schmidt (282) 77 Arai, H. see Y. Sato (288) 41 Augier, N. see F. Pons (282) 161 Arai, H., Ya. Igarashi and T. Kodama, Anaerobically induced Augustyn, O.P.H. see M.S. van Dyk (283) 195 expression of the nitrite reductase cytochrome c-551 operon from Aung, H. -P. see E. Harms (285) 55 Pseudomonas aeruginosa (280) 351 Ausio, J. see C. Mogensen (282) 273 Arai, H., Y. Igarashi and T. Kodama, Nitrite activates the Austin, R.C., R.A. Rachubinski and M.A. Blajchman, Site-directed transcription of the Pseudomonas aeruginosa nitrite reductase and mutagenesis of alanine-382 of human antithrombin III (280) 254 cytochrome c-551 operon under anaerobic conditions (288) 227 Autilio-Gambetti, L. see A.C. LeBlanc (292) 171 Arand, M., M. Knehr, H. Thomas, H.-D. Zeller and F. Oesch, An Autuori, F. see L. Fesus (284) 109 impaired peroxisomal targeting sequence leading to an unusual Avalos, J., L.M. Corrochano and S. Brenner, Cysteinyl-tRNA bicompartmental distribution of cytosolic epoxide hydrolase (294) synthetase is a direct descendant of the firstaminoacyl-tRNA 19 synthetase (286) 176 Aranda, A., R.P. Copp, A. Pascual and H.H. Samuels, Influence of Avdonin, V.B. see S.V. Minina (289) 224 thyroid hormone on ADP-ribosylation of nuclear proteins in Avjioglu, A. see I.J. Griffith (279) 210 cultured GH1 cells (279) 179 Avron, M. see G. Braun (280) 57 Arata, Y. see C. Nishimura (281) 167 Avron, A., F.H. Reeve, J.M. Lickorish and R.W. Carrell, Effect of Archakov, A.I. see A.N. Khokhlov (290) 171 alanine insertion (P";) on the reactive centre of a,-antitrypsin (280) Archambault de Vencay, J., Y. Cenatiempo and R. Julien, Evidence 4] for a ribosome-associated thiol protease cleaving wheat germ Avvakumov, G.V. see S.A. 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