The Journal of Antibiotics
Online ISSN : 1881-1469
Print ISSN : 0021-8820
ISSN-L : 0021-8820
Volume 45 , Issue 5
Showing 1-31 articles out of 31 articles from the selected issue
  • I. TAXONOMY, FERMENTATION, ISOLATION AND CHARACTERIZATION
    SATOSHI YAGINUMA, ATSUKI MORISHITA, KENYA ISHIZAWA, SAKAE MUROFUSHI, M ...
    1992 Volume 45 Issue 5 Pages 599-606
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    Sporeamicin A, a novel antibiotic, was isolated from the culture nitrate of an actinomycete. The producing organism, strain L53-18, was taxonomically assigned as a species of the genus Saccaropolyspora. The antibiotic was extracted with chloroform and was then purified by crystallization. It was obtained as colorless prisms from ethanolic solutions. Sporeamicin A exhibited a strong UV absorption peak at 276 nm. The molecular formula of sporeamicin A was determined to be C37H63NO12.
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  • II. STRUCTURE DETERMINATION
    ATSUKI MORISHITA, KENYA ISHIZAWA, NAOKI MUTOH, TAMOTSU YAMAMOTO, MITSU ...
    1992 Volume 45 Issue 5 Pages 607-612
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    Structure of a novel antibiotic, sporeamicin A (SRM-A), was determined by a combination of spectroscopic and X-ray crystallographic studies. SRM-A has a unique structure containing a 2, 3-dihydro-3-oxofuran moiety as part of a 14-membered macrolide ring.
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  • III. BIOLOGICAL PROPERTIES
    ATSUKI MORISHITA, NAOKI MUTOH, KENYA ISHIZAWA, TADAKIYO SUZUKI, SHIGEY ...
    1992 Volume 45 Issue 5 Pages 613-617
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    Sporeamicin A is a new erythromycin-type antibiotic isolated from a species of Saccharopolyspora. It was active in vitro against a wide variety of Gram-positive bacteria. In vitro studies indicated that the sporeamicin A was stable in the presence of human serum, although it was bound to serum proteins. Sporeamicin A was effective in the mouse protection test against Staphylococcus aureus, Streptococcuspyogenes and Streptococcuspneumoniae. Sporeamicin A attained higher plasma and tissue levels in the rat than did erythromycin stearate.
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  • TRIPTIKUMAR MUKHOPADHYAY, KIRITY ROY, R. G. BHAT, S. N. SAWANT, J. BLU ...
    1992 Volume 45 Issue 5 Pages 618-623
    Published: May 25, 1992
    Released: April 19, 2006
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    A new echinocandin type antifungal antibiotic, deoxymulundocandin, C48H77N7O15, was isolated from the culture filtrate and mycelia of a fungal culture, Aspergillus sydowii (Bainier and Sartory) Thorn and Church var. nov. mulundensis Roy (Culture No. Y-30462). The structure was established by comparative GC-MS analyses of the derivatized acid hydrolysates of deoxymulundocandin and mulundocandin as well as by the high field NMR experiments (COSY, NOESY and DEPT).
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  • V. HEGDE, M. PATEL, A. HORAN, V. GULLO, J. MARQUEZ, I. GUNNARSSON, F. ...
    1992 Volume 45 Issue 5 Pages 624-632
    Published: May 25, 1992
    Released: April 19, 2006
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    Three novel antifungal antibiotics, Sch 38518, Sch 39185 and Sch 38516 were isolated from the fermentation broths of two actinomycetes identified by chemical, morphological and physiological analysis as a new species of Actinomadura. The compounds were isolated from broth by solvent extraction and purified by silica gel chromatography. Physico-chemical properties, mass spectral analysis, IR and UV suggested the compounds were similar. Sch 38518 and Sch 39185 have a molecular formula of C25H48N2O5. 1H NMR, 13C NMR and hydrolysis indicated the aglycones were identical, however the compounds differed in containing isomeric sugar moieties. Sch 38518 contains mycosamine while Sch 39185 contains 3, 6-dideoxy-3-amino-L-talopyranose. Sch 38516 has a molecular formula of C24H46N2O5 and is a lower homolog of Sch 39185. The three compounds, Sch 38518 (1), Sch 39185 (2), and Sch 38516 (3) exhibit similar activity against Candida spp. with geometric mean MICs of 1.81, 2.00 and 0.91 μg/ml, respectively.
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  • R. COOPER, I. TRUUMEES, R. YARBOROUGH, D. LOEBENBERG, J. MARQUEZ, A. H ...
    1992 Volume 45 Issue 5 Pages 633-638
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    Eight antifungal compounds were identified from the fermentation of Actinomadura sp. SCC 1778. This culture produces four homologous compounds (C22H42N2O5-C25H48N2O5) containing the sugar, mycosamine, and four homologous compounds (C22H42N2O5-C25H48N2O5) containing the sugar, 3, 6-dideoxy-3-amino-L-talopyranose. Five of the compounds identified were novel macrolactams. All these compounds exhibit antifungal activity against Candida spp. with geometric mean MICs ranging from approximately 1.0 μg/ml for the higher homologs to 30 μg/ml for the lower homologs.
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  • I. TAXONOMY, FERMENTATION, ISOLATION, PHYSICO-CHEMICAL PROPERTIES AND BIOLOGICAL ACTIVITY
    MICHAEL J. DAWSON, JOHN E. FARTHING, PETER S. MARSHALL, ROBERT F. MIDD ...
    1992 Volume 45 Issue 5 Pages 639-647
    Published: May 25, 1992
    Released: April 19, 2006
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    During the screening of fungi for inhibitors of squalene synthase, Phoma sp. C2932 was found to produce three structurally related novel inhibitors. These compounds, designated the squalestatins, exhibited potent activity against both mammalian (rat liver) and fungal (Candida albicans) squalene synthase. Furthermore, they also had broad spectrum in vitro antifungal activity.
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  • II. STRUCTURE ELUCIDATION
    PHILIP J. SIDEBOTTOM, RONA M. HIGHCOCK, STEPHEN J. LANE, PAN A. PROCOP ...
    1992 Volume 45 Issue 5 Pages 648-658
    Published: May 25, 1992
    Released: April 19, 2006
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    Three novel fungal metabolites 1-3 isolated from cultures of a Phoma sp. C2932, are potent and selective inhibitors of squalene synthase. Their structures have been determined by a combination of spectroscopic, X-ray crystallographic and chemical methods; these natural products incorporate the highly functionalised bicyclic core, [1S-(1α, 3α, 4β, 5α, 6α, 7β)]-4, 6, 7-trihydroxy-2, 8-dioxabicyclo[3.2.l]octane-3, 4, 5-tricarboxylic acid.
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  • DISCOVERY, STRUCTURAL DETERMINATION AND BIOLOGICAL PROPERTIES
    MARK A. MAXELL, BERNARD F. BISHOP, PATRICIA BRYCE, KENNETH A. F. ORATI ...
    1992 Volume 45 Issue 5 Pages 659-670
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    A family of novel milbemycins possessing C-13β-acyloxy substitution was produced by Streptomyces hygroscopicus ATCC 53718. These compounds were detected by HPLC diode array analysis and possess anthelmintic and ectoparasiticidal activity. The origin of the oxygen atom at C-13 is discussed.
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  • I. THE PRODUCING ORGANISM AND ITS FERMENTATION
    ANNE W. DOMBROWSKI, GERALD F. BILLS, GLORY SABNIS, LAWRENCE R. KOUPAL, ...
    1992 Volume 45 Issue 5 Pages 671-678
    Published: May 25, 1992
    Released: April 19, 2006
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    A novel cytochalasin, L-696, 474, (18-dehydroxy cytochalasin H) that inhibits HIV-1 protease was discovered in fermentations of a bark-inhabiting Ascomycete, Hypoxylon fragiforme. The product was first identified from extracts of an agar medium. Fermentation studies on a number of media indicated that the product can be made on several solid and liquid media. Optimum production was obtained from growth in a complex medium composed of glycerol, glucose, citrate, Ardamine, soybean meal, tomato paste, and inorganic salts. Other Hypoxylon spp., related species of Xylariales, and other fungi known to produce cytochalasins, were also surveyed for their ability to make L-696, 474. Only one other Hypoxylon fragiforme isolate was found to make this novel cytochalasin; none of the other cultures surveyed made L-696, 474 or any other compounds which inhibit HIV-1 protease.
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  • II. ISOLATION AND STRUCTURE
    J. ONDEYKA, O. D. HENSENS, D. ZINK, R. BALL, R. B. LINGHAM, G. BILLS, ...
    1992 Volume 45 Issue 5 Pages 679-685
    Published: May 25, 1992
    Released: April 19, 2006
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    A novel HIV-1 protease inhibitor, L-696, 474 (C30H39NO4, 477), was isolated from the fermentations of the fungus Hypoxylon fragiforme (ATCC 20995, MF5511) and purified by silica gel chromatography followed by crystallization. Spectroscopic studies have shown the competitive inhibitor L-696, 474 to be a novel cytochalasin. Two related novel cytochalasins were also isolated and had no effect on the enzyme.
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  • III. BIOLOGICAL ACTIVITY
    RUSSELL B. LINGHAM, AMY HSU, KEITH C. SILVERMAN, GERALD F. BILLS, ANNE ...
    1992 Volume 45 Issue 5 Pages 686-691
    Published: May 25, 1992
    Released: April 19, 2006
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    L-696, 474, an inhibitor of the HIV-1 protease, was discovered in extracts of the fungal culture Hypoxylon fragiforme (MF5511; ATCC 20995). L-696, 474 is a novel cytochalasin with a molecular weight of 411 and an empirical formula of C30H39NO4. L-696, 474 inhibited HIV-1 protease activity with an IC50 of 3μM and the mode of inhibition was competitive with respect to substrate (apparent Ki=1μM). Furthermore, L-696, 474 was not a slow-binding inhibitor. The inhibition due to L-696, 474 was also independent of the HIV-1 protease concentration. L-696, 474 was inactive against pepsin, another aspartyl protease; stromelysin, a zinc-metalloproteinase; papain, a cysteine-specific protease or human leucocyte elastase, a serine-specific protease. Two other novel cytochalasins (L-697, 318 and L-696, 475) isolated from the same culture were inactive against the HIV-1 protease. Commercially available cytochalasins B, C, D, E, F, H and J were inactive while cytochalasin A was as active as L-696, 474 against the HIV-1 protease.
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  • TORU SASAKI, MASAYUKI TAKAGI, TAKASI YAGUCHI, SHINJI MIYADOH, TADAAKI ...
    1992 Volume 45 Issue 5 Pages 692-697
    Published: May 25, 1992
    Released: April 19, 2006
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    The novel anthelmintic cyclodepsipeptide PF1022A was isolated from cultured mycelia of Mycelia Sterilia PF1022 (PERM BP-2671). It showed strong anthelmintic activities against Ascaridia galli in chickens. The structure of PF1022A was determined to be cyclo(D-lactyl-L-N-methylleucyl-D-3-phenyllactyl-L-N-methylleucyl-D-lactyl-L-N-methylleucyl-D-3-phenyllactyl-L-N-methylleucyl) by spectroscopic analyses and chemical studies.
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  • I. PRODUCING STRAIN, FERMENTATION, ISOLATION AND BIOLOGICAL ACTIVITY
    EISAKU TSUJII, YASUHISA TSURUMI, SUSUMU MIYATA, KEIKO FUJIE, AKIKO KAW ...
    1992 Volume 45 Issue 5 Pages 698-703
    Published: May 25, 1992
    Released: April 19, 2006
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    WF11605, a new antagonist of leukotriene B4 (LTB4) was isolated as a product of fungal strain F11605. The molecular formula of WF11605 was determined to be C38H60O11 WF11605 inhibited LTB4-induced chemotaxis of rabbit polymorphonuclear leukocytes (PMNLs) with an IC50 value of 1.7×10-7 M and blocked 3H-LTB4 binding to PMNL membranes at 5.6×10-6 M (IC50). WF11605 also inhibited LTB4-induced degranulation of rabbit PMNLs at 3.0×10-6M (IC50). However, WF11605 did not show any inhibitory effect on platelet activating factor (PAF)- and N-formyl-L-methionyl-L-leucyl-L-phenylalanine (FMLP)-induced degranulation at concentrations up to 10-4M. These results suggest that WF11605 is a specific antagonist of LTB4.
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  • II. STRUCTURE DETERMINATION
    NOBUHARU SHIGEMATSU, EISAKU TSUJII, NATSUKO KAYAKIRI, SHIGEHIRO TAKASE ...
    1992 Volume 45 Issue 5 Pages 704-708
    Published: May 25, 1992
    Released: April 19, 2006
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    The structure of WF11605, a novel tetracyclic triterpene glucoside, was determined to be 1. The plane structure of deacetyl-WF11605 aglycone was elucidated as 2 through the concerted application of a series of 2D NMR techniques. The relative configurations were established by X-ray crystallographic analysis of bis(p-bromobenzoyl) derivative 3 and absolute stereochemistry by CD exciton chirality method.
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  • IV. SYNTHESIS AND ANTIBACTERIAL ACTIVITY OF 7β-[2-(5-AMINO-1, 2, 4-THIADIAZOL-3-YL)-2(Z)-ALKOXYIMINOACETAMIDO]-3-(CONDENSED-HETEROCYCLIC AZOLIUM)METHYL CEPHALOSPORINS INCLUDING SCE-2787
    AKIO MIYAKE, YOSHINOBU YOSHIMURA, MASAYOSHI YAMAOKA, TATSUO NISHIMURA, ...
    1992 Volume 45 Issue 5 Pages 709-720
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    The synthesis and in vitro antibacterial activity of 7β-[2-(5-amino-1, 2, 4-thiadiazol-3-yl)-2(Z)-alkoxyiminoacetamido] cephalosporins bearing various condensed-heterocyclic azolium groups at the 3 position in the cephalosporin nucleus are described. The thiadiazolyl cephalosporins showed good antibacterial activity against both Gram-positive and Gram-negative bacteria and the MICs of the thiadiazolyl cephalosporins against Pseudomonas aeruginosa was more potent than that of the corresponding 7β-[2-(2-aminothiazol-4-yl)-2(Z)-alkoxyiminoacetamido]-3-(condensed-heterocyclic azolium)methyl cephalosporins. Also, the thiadiazolyl cephalosporins bearing (imidazo[1, 2-b]-pyridazinium-1-yl)methyl groups at the 3 position showed antibacterial activity against methicillinresistant Staphylococcus aureus (MRSA). Among the cephalosporins tested, 7β-[2-(5-amino-1, 2, 4-thiadiazol-3-yl)-2(Z)-methoxyiminoacetamido]-3-(imidazo[1, 2-b]pyridazinium-l-yl)methyl-3-cephem-4-carboxylate (4, SCE-2787) which exhibited the most potent antibacterial activity and the broadest antibacterial spectrum was selected as a parenteral cephalosporin candidate for further biological evaluation.
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  • V. SYNTHESIS AND ANTIBACTERIAL ACTIVITY OF 3-(CONDENSED-TRIAZOLO-PYRIDINIUM, -PYRIMIDINIUM, AND -PYRIDAZINIUM)-METHYL CEPHALOSPORINS
    YOSHINOBU YOSHIMURA, KIMINORI TOMIMATSU, TATSUO NISHIMURA, AKIO MIYAKE ...
    1992 Volume 45 Issue 5 Pages 721-734
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    As a part of our studies on cephalosporins bearing condensed-heterocyclic azolium methyl groups at the 3 position in the cephalosporin nucleus, we describe here the synthesis and antibacterial activity of 7β-[2-(2-aminothiazol-4-yl)-2(Z)-methoxyiminoacetamido] cephalosporins (1-16), 7β-[2-(2-amino-5-chlorothiazol-4-yl)-2(Z)-methoxyiminoacetamido] cephalosporins (17, 18) and 7β-[2-(5-amino-1, 2, 4-thiadiazol-3-yl)-2(Z)-methoxyiminoacetamido] cephalosporins (19-23) containing a variety of condensed-heterocyclic triazolium methyl groups at the 3 position in the cephalosporin nucleus. These cephalosporins exhibited potent antibacterial activity, and it appears that condensed-heterocyclic triazolium as well as condensed-heterocyclic imidazolium rings are effective moieties for improving antibacterial activity and the spectrum of activity. Among the cephalosporins tested, 7β-[2-(2-aminothiazol-4-yl)-2(Z)-methoxyiminoacetamido]-3-(5-methyl[1, 2, 3]triazolo[1, 5-α]pyridinium-1-yl)methyl-3-cephem-4-carboxylate (9) and 7β-[2-(2-aminothiazol-4-yl)-2(Z)-methoxyiminoacetamido]-3-(6-methoxy[1, 2, 4]triazolo[1, 5-α]pyridinium-1-yl)methyl-3-cephem-4-carboxylate (11) showed good antibacterial activity.
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  • YOSHIO NISHIMURA, SHINICHI KONOO, TOMIO TAKEUCHI
    1992 Volume 45 Issue 5 Pages 735-741
    Published: May 25, 1992
    Released: April 19, 2006
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    Some derivatives of bactobolin were prepared from bactobolin by dehydration or substitution reactions through tris(dimethylamino)alkoxyphosphonium salt formation. A derivative with low toxicity, 6-deoxybactobolin, showed moderate activity against Gram-positive and Gram-negative bacteria including methicillin-resistant Staphylococcus aureus.
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  • YUKIO KIMURA, HISAMI MATSUNAGA, MARTTI VAARA
    1992 Volume 45 Issue 5 Pages 742-749
    Published: May 25, 1992
    Released: April 19, 2006
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    Polymyxin B octapeptide (PBOP) and polymyxin B heptapeptide (PBHP) were found to be effective permeabilizers of the outer membrane of Escherichia coli and Salmonella typhimurium. PBOP was as effective as polymyxin B nonapeptide (PMBN), the known very potent permeabilizer. As low a PBOP concentration as 1μg/ml sensitized E. coli to rifampicin by a factor of 100. Three μg of PBOP per ml was sufficient to sensitize this target to all the other tested hydrophobic antibiotics (erythromycin, fusidic acid, clindamycin, and novobiocin) by a factor of 30. Only a slightly higher (3-fold) concentration of PBHP was required for a similar sensitizing effect.
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  • HIROSHI YAMAKI, MAKI YAMAGUCHI, TAKASHI TSURUO, HIDEYO YAMAGUCHI
    1992 Volume 45 Issue 5 Pages 750-755
    Published: May 25, 1992
    Released: April 19, 2006
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    An antifungal antibiotic (S) 2-amino-4-oxo-5-hydroxypentanoic acid, inhibited the biosynthesis of the aspartate family of amino acids (methionine, isoleucine and threonine) followed by the inhibition of protein biosynthesis in Saccharomyces cerevisiae. This inhibition was effected by impeding the biosynthesis of their common intermediate precursor, homoserine. The inhibition of biosynthesis of homoserine by the antibiotic was attributable to inactivation of homoserine dehydrogenase [EC 1.1.1.3], which is involved in the conversion of aspartate semialdehyde to homoserine in the metabolic pathway leading to threonine, methionine and isoleucine. Since such enzymic activity is not present in animal cells, the selective antifungal activity of the antibiotic is thus explained.
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  • I. CHEMICAL SYNTHESIS OF 2-DEOXY-SCFLLO-INOSOSE AND [2, 2-2H2]-2-DEOXY-SCYLLO-INOSOSE
    NORIAKI YAMAUCHI, KATSUMI KAKINUMA
    1992 Volume 45 Issue 5 Pages 756-766
    Published: May 25, 1992
    Released: April 19, 2006
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    A practical preparative method for 2-deoxy-scyllo-inosose, the earliest key intermediate leading to 2-deoxystreptamine, was devised as a prerequisite to more detailed biochemical studies on the biosynthesis of 2-deoxystreptamine. [2, 2-2H2]-2-Deoxy-scyllo-inosose was also synthesized through a modified Ferrier reaction.
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  • II. QUANTITATIVE ANALYSIS OF 2-DEOXY-SCYLLO-INOSOSE
    NORIAKI YAMAUCHI, KATSUMI KAKINUMA
    1992 Volume 45 Issue 5 Pages 767-773
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
    A practical quantitative analysis of 2-deoxy-scyllo-inosose by means of GC-MS selected-ion monitoring (SIM) was exploited in order to assay the enzymatic 2-deoxy-scyllo-inosose formation, the first stage of the 2-deoxystreptamine biosynthesis. Mass spectral fragmentations of 2-deoxy-scyllo-inosose tetra-O-trimethylsilyl (TMS) ether was also investigated by the use of [2, 2-2H2]-2-deoxy-scyllo-inosose.
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  • NORIAKI YAMAUCHI, KATSUMI KAKINUMA
    1992 Volume 45 Issue 5 Pages 774-780
    Published: May 25, 1992
    Released: April 19, 2006
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    The in vitro activity of formation of 2-deoxy-scyllo-inosose, the earliest intermediate of the 2-deoxystreptamine biosynthesis, was confirmed in the precipitate fraction obtained by 30-45% saturation of ammonium sulfate from the 15, 000×g supernatant of the sonicated Streptomyces fradiae IFO 13147 cells.
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  • C-P BOND FORMATION MECHANISM OF BIALAPHOS: DISCOVERY OF A P-METHYLATION ENZYME
    KAZUMA KAMIGIRI, TOMOMI HIDAKA, SATOSHI IMAI, TAKESHI MURAKAM, HARUO S ...
    1992 Volume 45 Issue 5 Pages 781-787
    Published: May 25, 1992
    Released: April 19, 2006
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    An enzymatic activity catalyzing P-methylation of N-acetyldemethylphosphinothricin, a biosynthetic intermediate of the herbicide bialaphos, was detected in a cell extract of Streptomyces hygroscopicus SF-1293, a bialaphos producing organism. The gene coding for this P-methylation enzyme in the bialaphos biosynthetic gene cluster was also expressed in Streptomyces lividans. The methyl donor of the reaction was determined to be methylcobalamin. The P-methylation enzyme utilized both N-acetyldemethylbialaphos and N-acetyldemethylphosphinothricin as substrates.
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  • III. STRUCTURES OF WS-7338 A, B, C AND D AND TOTAL SYNTHESIS OF WS-7338 B
    SUSUMU MIYATA, NAOKI FUKAMI, MASAHIRO NEVA, SHIGEHIRO TAKASE, SUMIO KI ...
    1992 Volume 45 Issue 5 Pages 788-791
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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  • I. 1H AND 13C NMR ASSIGNMENTS OF BOTTROMYCIN A2, THE MAIN COMPONENT OF THE COMPLEX
    MIYUKI KANEDA
    1992 Volume 45 Issue 5 Pages 792-796
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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  • MARCO ALPEGIANI, ANGELO BEDESCHI, FRANCO ZARINI, COSTANTINO DELLA BRUN ...
    1992 Volume 45 Issue 5 Pages 797-801
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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  • KEIKO NAKAGAWA, KAZUO SATO, YOSHIHISA TSUKAMOTO, AKIO TORIKATA
    1992 Volume 45 Issue 5 Pages 802-805
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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  • YUJI YOSHIYAMA, TERUAKI KOBAYASHI, FUMIYA TOMONAGA, SHIGEYUKI NAKANO
    1992 Volume 45 Issue 5 Pages 806-808
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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  • ATSUKI MORISHITA, SAKAE MUROFUSHI, KENYA ISHIZAWA, NAOKI MUTOH, SATOSH ...
    1992 Volume 45 Issue 5 Pages 809-812
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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  • EDWARD J. TYNAN, THEODORE H. NELSON, RICHARD A. DAVIES, WILLIAM C. WER ...
    1992 Volume 45 Issue 5 Pages 813-815
    Published: May 25, 1992
    Released: April 19, 2006
    JOURNALS FREE ACCESS
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