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Preview FEBS Letters 1992: Vol 286-314 Index

FEBS/Ea93,%: AN INTERNATIONAL JOURNAL FOR THE RAPID PUBLICATION OF SHORT REPORTS IN BIOCHEMISTRY, BIOPHYSICS AND MOLECULAR CELL BIOLOGY olume 314, Supplement FEBLAL 314( Suppl.) 1 ISSN 00145793 _____ RRS LETTERS An international journal establishefdo r 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 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 As a rule, for example, we do not publish incomplete sequences, or sequences which are known in other species; or incomplete NMR or other spectroscopic assignments; or the conventionally achieved 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 310, No. 3, pp. 284-285 and thereafter at the end of each tenth volume, i.e. at the end of Vol. 320, 330, 340 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. In case of doubt, please contact any editor. The ‘date of receipt’ eventually appearing in the published paper will be that upon which the editor who actually handled the manuscript took receipt of it. The authors are urged to submit, if at all possible, a floppy disk of their manuscript (see under Notes to Authors). This also accelerates the handling process and reduces the danger of misprints eventually appearing. Vote: 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), Eidgendssische 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 1, Postfach 10.2209, D-W-6900 Heidelberg, Germany (49-6221-387306) H.R.V. ARNSTEIN (Editor of book reviews), London, England M. BAGGIOLINI, Th. Kocher-Institut, Universitat Bern, Freiestrasse 1, CH-3012 Berne, Switzerland (41-31-653-799) H. BETZ, MPI fiir Hirnforschung, Deutschordenstr. 46, Postfach 71 60 62, D-W 6000 Frankfurt a/M 71, Germany (49-69-96769-441) 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, Pharmacology Group, King’s College, Chelsea Campus, Manresa Road, London SW3 6LX, England (44-71-333-4949) 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 (49-941-943-3352) H. HOLZER, Biochemisches Institut der Universitat, Hermann-Herder-Str. 7, D-W-7800 Freiburg i.Br., Germany (49-761 -203-3331) P. JOLLES, Laboratory of Proteins/Enzymes/Glycoconjugates, CNRS/Université de Paris V, 45, rue des Saint-Peres, 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) N. MANTEL, Laboratorium fiir Biochemie, ETH Zentrum, Universititstrasse 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. MIRZABEKOV, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov str. 32, 117984 Moscow B-334, Russia* (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, 44 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, Max-Delbriick-Zentrum fiir molekulare Medizin, Robert Réssle-Strasse 10, 1115 D-O-Berlin-Buch, Germany (49-30-949-4161) 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, Russia* (7-095-939-0338) 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) G. TETTAMANTI, Universita degli Studi di Milano, Facolta di Medicina e Chirurgia, Dipartimento di Chimica e Biochimica Medica, Via Saldini, 50, 1 20133 Milano, Italy (39-2-236-3584) M. VAN MONTAGU, Laboratorium voor Genetika, Universiteit Gent, Ledeganckstraat 35, B-9000 Gent, Belgium (32-91-645-349) G. WAGNER, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115, USA (1-617-432-4383) | 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 @azkj LETTERS MASTER INDEX VOLUMES 296-314 FEBLAL 314 (Suppl.) 1 @falzK)J 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 M. Baggiolini, Berne A.D. Mirzabekov, Moscow H. Betz, Frankfurt Sh. Mizushima, Tokyo J.E. Celis, Aarhus M.J. Owen, London S.P. Datta, London, Honorary Chairman P.J. Randle, Oxford J.M. Gancedo, Madrid T.A. Rapoport, Berlin-Buch B. Halliwell, Sacramento M. Saraste, Heidelberg, Reviews Editor P.M. Harrison, Sheffield R. Sato, Osaka J. Hanoune, Créteil G. Semenza, Zirich, Managing Editor M. Hatanaka, Kyoto S. Shaltiel, Rehovot G. Hauska, Regensburg V.P. Skulachev, Moscow H. Holzer, Freiburg i.Br. V.P. Somlyo, Charlottesville P. Jollés, Paris G. Tettamanti, Milan C. Klee, Bethesda M. Van Montagu, Gent N. Mantei, Ziirich G. 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Information for Advertisers. Advertising orders and enquiries can be sent to the Advertising Manager, Elsevier Science Publishers, Advertising Department, Van de Sande, Bakhuyzenstraat 4, 1061 AG Amsterdam, or P.O. Box 211, 1000 AE Amsterdam, The Netherlands, Tel.: 20-5153.220; Fax: 20-6833.041, attn. Advertising Dept; U.K.: T.G. Scott and Son Ltd., Tim Blake, Portland and Canada: Weston Media Associates, Daniel Lipner, P.O. Box 1110, Greens Farms, CT 06436-1110, U.S.A., Tel.: 203-261.2500; Fax: 203-261.0101 FEBS Letters Volumes 296-314 Master Author Index Volumes 296-314 (1992) A Albertyn, J., André van Tonder and B.A. Prior, Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae (308) 130 Albracht, S.P.J. see U. Leutbecher (307) 144 Albracht, S.P.J. see R.A. Schmitz (309) 78 Albracht, S.P.J. seeR . Hedderich (298) 65 Abbink, J.J. see K.M. Dolman (314) 117 Albrecht, J. see F. Stastny9 (300) 247 Abe, K. see H. Kondo (299) 48 Alcain, F.J. see P. Navas (299) 223 Abe, K. see M. Minami (309) 353 Alcayaga, C., R. Venegas, A. Carrasco and D. Wolff, Ion channels AbouHaidar, M.G. see I. Ivanov (307) 173 from the Bacillus subtilis plasma membrane incorporated into Abramenko, I.V., D.F. Gluzman, E.Y. Korchagina, T.V. planar lipid bilayers (311) 246 Zemlyanukhina and N.V. Bovin, Oligosaccharide-binding Aldunate, J., L. Coloma-Torres, P. Spencer, A. Morello, J.M. Ojeda molecules on the surface of human hemopoietic and lymphoid cells and Y. Repetto, Effects of 2(3)-tert-butyl-4-hydroxyanisole (BHA) (307) 283 on in situ mitochondria of Trypanosoma cruzi (303) 73 Abramov, V.M. see A.V. Karlyshev (305) 37 Alegret, M. see R.M. Sanchez (300) 89 Abramov, V.M. see A.V. Karlyshev (297) 77 Alekberova, Z.S. see 1.B. Bronshtein (314) 259 Abramova, T.V. see E.L. Chernolovskaya (303) 269 Alexandrov, A.N. see S.N. Nametkin (309) 330 Adachi, H. see S. Oguchi (308) 22 Alexandrova, R. see I. Ivanov (307) 173 Adachi, M., M. Sekiya, T. Miyachi, K. Matsuno, Y. Hinoda, K. Imai Alexandrushkina, N.I. see M.D. Kirnos (298) 109 and A. Yachi, Molecular cloning of a novel protein-tyrosine Algranati, 1.D. see C. Ceriani (301) 261 phosphatase SH-PTP3 with sequence similarity to the src-homology Ali-Hadji, D. see R. Bischoff (305) 265 region 2 (314) 335 Allakhverdiev, S.1., V.V. Klimov and S. Demeter, Adachi, M., Y.-Y. Yang, A. Trzeciak, Y. Furuichi and C. Miyamoto, Thermoluminescence evidence for light-induced oxidation of Identification of a domain of ET, receptor required for ligand tyrosine and histidine residues in manganese-depleted photosystem binding (311) 179 II particles (297) 51 Adachi, S. see N. Sakai (301) 60 Allard, B., M.-J. Moutin and M. Ronjat, BisG10, a K* channel Adachi, T. see H. Izumi (302) 213 blocker, affects the calcium release channel from skeletal muscle Adam, L.P., C.J. Gapinski and D.R. Hathaway, Phosphorylation sarcoplasmic reticulum (314) 81 sequences in h-caldesmon from phorbol ester-stimulated canine Allee, G. see A.M. Brunati (313) 291 aortas (302) 223 Allen, M.H. see T.W. Hutchens (309) 170 Adami, N. see G. Buell (299) 90 Allende, C.C. see R. Tellez (308) 113 Adams, R.L.P. see M. Bryans (309) 97 Allende, C.C. see A. Jedlicki (297) 280 Adar, R. see E. Rodriguez-Arango (307) 185 Allende, J.E. see A. Jedlicki (297) 280 Adham, N. see H.-T. Kao (307) 324 Allende, J.E. see R. Tellez (308) 113 Adler, J. see A.H. Delcour (304) 216 Alonso, C. see G. Strecker (298) 39 Adlercreutz, P. see M.Y. Gololobov (307) 309 Altieri, F. see A. Ferraro (307) 383 Adolf, G.R. see C.G. Voigt (314) 85 Alvarez, L. see M.A. Pajares (309) 1 Advani, S. see J. Monteiro (300) 105 Alves, J. see A. Jeltsch (304) 4 Adzet, T. see R.M. Sanchez (300) 89 Amabe, Y. see H. Shinohara (304) 69 Adzhubei, I.A. see A.A. Makarov (306) 63 Ambach, E. see P. Klatt (305) 160 Aebersold, R. see B.R. Green (305) 18 Ambe, F. see J. Honda (301) 177 Aebersold, R. see S. Kim (314) 67 Ambrosius, D. see T. Zink (314) 435 Agarwal, M.K. see M. Mirshahi (314) 237 Ameratunga, R.V. see G.W. Krissansen (296) 25 Aggarwal, B.B. see R. Pandita (312) 87 Ames, B.N. see C.E. Cross (298) 269 Agostinis, P., O. Marin, P. James, P. Hendrix, W. Merlevede, J.R. Amess, B., H.A. Manjarrez-Hernandez, S.A. Howell, M. Learmonth Vandenheede and L.A. Pinna, Phosphorylation of the phosphatase and A. Aitken, Multisite phosphorylation of the 80 kDa modulator subunit (inhibitor-2) by casein kinase-1: Identification of (MARCKS) protein kinase C substrate in C3H/10T1/2 fibroblasts: the phosphorylation sites (305) 121 Quantitative analysis of individual sites by solid-phase Agro, A.F. see A. Rossi (301) 253 microsequencing (297) 285 Aguilar, M., K. Kalakoutskii, J. Cardenas and E. Fernandez, Direct Amler, E. see P. Anzenbacher (312) 80 transfer of molybdopterin cofactor to aponitrate reductase from a Amodeo, P. see T. Tancredi (310) 27 carrier protein in Chlamydomonas reinhardtii (307) 162 Amrhein, N. see C. Wanke (301) 271 Aguirre, A. see T.K. Sixma (305) 81 Amselgruber, W. see L. Sanz (300) 213 Ahmed, I. and G. Krishnamoorthy, The non-equivalence of binding Anand-Srivastava, M.B. see C. Thibault (313) 160 sites of coenzyme quinone and rotenone in mitochondrial NADH- Anantharam, V., R.G. Panchal, A. Wilson, V.V. Kolchine, S.N. CoQ reductase (300) 275 Treistman and H. Bayley, Combinatorial RNA splicing alters the Ahnert-Hilger, G. and B. Wiedenmann, The amphicrine pancreatic surface charge on the NMDA receptor (305) 27 cell line, AR42J, secretes GABA and amylase by separate regulated Andersen, B., H.V. Scheller and B.L. Moller, The PSI-E subunit of pathways (314) 41 photosystem I binds ferredoxin: NADP* oxidoreductase (311) 169 Aitken, A. see B. Amess (297) 285 Andersen, J.P. see B. Vilsen (306) 247 Aitken, A. see S. Hirsch (296) 222 Andersen, J.P. see B. Vilsen (306) 213 Akagi, M. see H. Urata (311) 263 Andersen, N.H. see S.R. Krystek Jr. (299) 255 Akasaka, T. see A. Yamaguchi (307) 229 Andersen, P.H. see J.A. Gingrich (312) 115 Akatsuka, H. see Y. Ando (314) 109 Anderson, S., V.D. Appanna, J. Huang and T. Viswanatha, A novel Akazawa, T. see P. Perata (309) 283 role for calcite in calcium homeostasis (308) 94 Akerman, K. see A. Jalava (300) 114 Andersson, B. see J.D.L. Rivas (301) 246 Akerstrém, B. see P. Pierzchalski (298) 165 Andersson, B. see N. Wedel (314) 61 Aki, M., T. Tamura, F. Tokunaga, S. Iwanaga, Y. Kawamura, N. Andersson, I. see N. Bylsma (299) 44 Shimbara, S. Kagawa, K. Tanaka and A. Ichihara, cDNA cloning Andersson, K. see A.M. Eriksson (308) 211 of rat proteasome subunit RCI, a homologue of RING1O located Ando, F. see Y. Sagara (300) 208 in the human MHC class II region (301) 65 Ando, Y., M. Watanabe, H. Akatsuka, H. Tokumitsu and H. Hidaka, Akimenko, Z.A. see A.A. Ilyichev (301) 322 Site-directed mutation makes rabbit calcyclin dimer (314) 109 Akke, M. see N.J. Skelton (303) 136 Andraloje, P.J. and D.A. Harris, Isolation and characterisation of a Aktories, K. see C. Mohr (297) 95 functional af heterodimer from the ATP synthase of Rhodospirillum Akutsu, H. and M. Hirasawa, Non-equivalent natures of the rubrum (310) 187 coordinated imidazole rings of cytochrome c, from D. vulgaris André van Tonder, see J. Albertyn (308) 130 Miyazaki F as studied by 'H NMR (308) 264 Andreansky, M. see J. Urban (298) 9 Alakhov, V.Y. see S.N. Nametkin (309) 330 Andreasen, P.A. see A. Nykjer (300) 13 Albalat, R., Gonzalez-Duarte and S. Atrian, Protein engineering of Andreola, M.-L. see R. El Dirani-Diab (301) 23 Drosophila alcohol dehydrogenase: The hydroxyl group of Tyr'® is involved in the active site of the enzyme (308) 235 Zz Volumes 296-314 (1992) Andreu, D., J. Ubach, A. Boman, B. Wahlin, D. Wade, R.B. Arnaud, S., F. Malatesta and M. Denis, Reduction of carbon Merrifield and H.G. Boman, Shortened cecropin A—melittin monoxide to formaldehyde by the terminal oxidase of the marine hybrids: Significant size reduction retains potent antibiotic activity bacterium Pseudomonas nautica strain 617 (296) 259 (296) 190 Arnberg, A.C. see O. Coux (300) 49 Andreu, D. see I.S. Novella (311) 235 Arndt, E. and C. Steffens, Nucleotide sequence of the genes for Andreu, J.M. see I.S. Novella (311) 235 ribosomal proteins HS15 and HSH from Haloarcula marismortui: Andrews, S.C., D. Shipley, J.N. Keen, J.B.C. Findlay, P.M. Harrison an archaeon-specific gene cluster (314) 211 and J.R. Guest, The haemoglobin-like protein (HMP) of Arnosti, D.N. see E. Brugnera (314) 361 Escherichia coli has ferrisiderophore reductase activity and its C- Aro, E.-M., R. Kettunen and E. Tyystjarvi, ATP and light regulate terminal domain shares homology with ferredoxin NADP* D1 protein modification and degradation: Role of D1 in reductases (302) 247 photoinhibition (297) 29 Animashaun, T. see D. Chawla (298) 291 Arrondo, J.-L.R. see J. Castresana (314) 171 Ankilova, V.N. see V.G. Stepanov (311) 192 Arseniev, A.S. see K.V. Pervushin (308) 190 Annaert, W. see B. Miserez (314) 122 Artymiuk, P.J., H.M. Grindley, J.E. Park, D.W. Rice and P. Willett, Annaix, V. see G. Larcher (308) 65 Three-dimensional structural resemblance between leucine Anselme, J. see D. Madern (299) 85 aminopeptidase and carboxypeptidase A revealed by graph- Antkowiak, B. and K. Kirschfeld, Enflurane is a potent inhibitor of theoretical techniques (303) 48 high conductance Ca**-activated K* channels of Chara australis Asada, K. see R. Harasawa (297) 209 (313) 281 Asada, K. see K. Hiramatsu (298) 133 Antonelli, M. see A. Onate (313) 213 Asahi, M., S. Yanagi, S. Ohta, T. Inazu, K. Sakai, F. Takeuchi, T. Antonini, G. see M. Brunori (314) 191 Taniguchi and H. Yamamura, Thrombin-induced human platelet Antoniu, B. see N.R. Brandt (299) 57 aggregation is inhibited by protein-tyrosine kinase inhibitors, ST638 Antson, A.A., B.V. Strokopytov, G.N. Murshudov, M.N. Isupov, and genistein (309) 10 E.H. Harutyunyan, T.V. Demidkina, D.G. Vassylyev, Z. Dauter, Asakura, T. see M.P. Williamson (302) 185 H. Terry and K.S. Wilson, The polypeptide chain fold in tyrosine Asano, T. see M. Kobayashi (302) 129 phenol-lyase, a pyridoxal-5’-phosphate-dependent enzyme (302) Asano, T., H. Katagiri, K. Tsukuda, J.-L. Lin, H. Ishihara, K. Inukai, 256 Y. Yazaki and Y. Oka, Glucose binding enhances the papain Anuntalabhochai, S. see N. Terryn (299) 287 susceptibility of the intracellular loop of the GLUT] glucose Anzenbacher, P., P. Mojzes, V. Baumruk and E. Amler, Changes in transporter (298) 129 Na*,K*-ATPase structure induced by cation binding: Approach by Asao, H. see S. Kumaki (310) 22 Raman spectroscopy (312) 80 Asao, H., S. Kumaki, T. Takeshita, M. Nakamura and K. Sugamura, Apell, H.-J. see W. Stiirmer (300) | IL-2-dependent in vivo and in vitro tyrosine phosphorylation of Aplin, R.T. see A. Steinkasserer (310) 63 IL-2 receptor y chain (304) 141 Aplin, R.T. see K.J. Lumb (296) 153 Asard, H., N. Horemans and R.J. Caubergs, Transmembrane electron Appanna, V.D. see S. Anderson (308) 94 transport in ascorbate-loaded plasma membrane vesicles from Aquilina, J.A. see J.A. Carver (311) 143 higher plants involves a b-type cytochrome (306) 143 Arai, K.-i. see M.-a. Muramatsu (311) 75 Asashima, M. see S. Nishimatsu (312) 169 Arai, S. see H. Kondo (299) 48 Ascenzi, P. see M. Coletta (296) 184 Araki, K. see M. Yamazaki (300) 39 Ascenzi, P. see E. Menegatti (301) 10 Araki, K. see K. Ikeda (313) 34 Asher, O., S. Fuchs, D. Zuk, D. Rapaport and A. Buonanno, Changes Arand, M. see T. Gebel (309) 37 in the expression of mRNAs for myogenic factors and other muscle- Aranda, A. see A. Sanchez-Pacheco (312) 42 specific proteins in experimental autoimmune myasthenia gravis Aranda-Anzaldo, A. and D. Viza, Human immunodeficiency virus (299) 15 type | productive infection in staurosporine-blocked quiescent cells Ashmarin, I.P., R.A. Danilova, A.V. Pshezhetsky, I.M. Fedorova, (308) 170 M.F. Obukhova and S. Sagimbaeva, Alcohol dehydrogenase Arango, R. see E. Rodriguez-Arango (307) 185 (ADH): Influence of homo- and heterologous ADH administration Aranyi, P. see C. Salamon (308) 215 on albino rats craving for alcohol and on ADH isozyme activity in Arao, M. see T. Yamaguchi (309) 303 the liver (306) 38 Arata, Y., S. Tada and M. Ui, Probable occurrence of toxin- Asou, H. see T. Yazaki (307) 361 susceptible G proteins in the nematode Caenorhabditis elegans (300) Aspenstrém, P., U. Lindberg and R. 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