Relevant bibliographies by topics / Streptogramine

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters

Academic literature on the topic 'Streptogramine'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "Streptogramine"

1

De Gaudio, A. R., and A. Di Filippo. "Quale Ruolo per le Streptogramine in Terapia Intensiva?" Journal of Chemotherapy 15, sup1 (August 2003): 17–22. http://dx.doi.org/10.1080/1120009x.2003.11782355.

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Seoane, Asunción, and Juan M. García Lobo. "Identification of a Streptogramin A Acetyltransferase Gene in the Chromosome of Yersinia enterocolitica." Antimicrobial Agents and Chemotherapy 44, no. 4 (April 1, 2000): 905–9. http://dx.doi.org/10.1128/aac.44.4.905-909.2000.

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ABSTRACT Streptogramins are polypeptide antibiotics inhibiting protein synthesis by the prokaryotic ribosome. Gram-positive organisms are susceptible to streptogramins, while most gram-negative bacteria are intrinsically resistant. We have found a genomic fragment from aYersinia enterocolitica isolate with an open reading frame coding for a polypeptide similar to the virginiamycin acetyltransferases found in various plasmids from gram-positive bacteria. The susceptible Escherichia coli strain DB10 was transformed to resistance to the type A streptogramins and to mixed (A + B) streptogramins upon introduction of a plasmid containing that gene. In addition, we showed streptogramin acetylating activity in vitro dependent on the presence of the Y. enterocolitica sat gene. Southern blot hybridization experiments showed that thesat gene was present in all the Y. enterocolitica isolates examined. These data together show that the gene in the Y. enterocolitica chromosome encoded an active streptogramin acetyltransferase. The deduced sequence of theY. enterocolitica Sat protein was close to those ofsat gene products found in gram-positive bacteria and cyanobacteria, suggesting a common evolutionary origin.
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Foik, Ilona P., Irina Tuszynska, Marcin Feder, Elzbieta Purta, Filip Stefaniak, and Janusz M. Bujnicki. "Novel inhibitors of the rRNA ErmC' methyltransferase to block resistance to macrolides, lincosamides, streptogramine B antibiotics." European Journal of Medicinal Chemistry 146 (February 2018): 60–67. http://dx.doi.org/10.1016/j.ejmech.2017.11.032.

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Noeske, Jonas, Jian Huang, Nelson B. Olivier, Robert A. Giacobbe, Mark Zambrowski, and Jamie H. D. Cate. "Synergy of Streptogramin Antibiotics Occurs Independently of Their Effects on Translation." Antimicrobial Agents and Chemotherapy 58, no. 9 (June 23, 2014): 5269–79. http://dx.doi.org/10.1128/aac.03389-14.

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ABSTRACTStreptogramin antibiotics are divided into types A and B, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A, dalfopristin; type B, quinupristin) and NXL 103 (type A, flopristin; type B, linopristin) with theEscherichia coli70S ribosome by X-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. The streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a nonhydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that the synergistic antimicrobial activity of streptogramins can occur independently of the effects of streptogramin on translation.
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Stogios, Peter J., Misty L. Kuhn, Elena Evdokimova, Patrice Courvalin, Wayne F. Anderson, and Alexei Savchenko. "Potential for Reduction of Streptogramin A Resistance Revealed by Structural Analysis of Acetyltransferase VatA." Antimicrobial Agents and Chemotherapy 58, no. 12 (September 15, 2014): 7083–92. http://dx.doi.org/10.1128/aac.03743-14.

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ABSTRACTCombinations of group A and B streptogramins (i.e., dalfopristin and quinupristin) are “last-resort” antibiotics for the treatment of infections caused by Gram-positive pathogens, including methicillin-resistantStaphylococcus aureusand vancomycin-resistantEnterococcus faecium. Resistance to streptogramins has arisen via multiple mechanisms, including the deactivation of the group A component by the large family of virginiamycinO-acetyltransferase (Vat) enzymes. Despite the structural elucidation performed for the VatD acetyltransferase, which provided a general molecular framework for activity, a detailed characterization of the essential catalytic and antibiotic substrate-binding determinants in Vat enzymes is still lacking. We have determined the crystal structure ofS. aureusVatA inapo, virginiamycin M1- and acetyl-coenzyme A (CoA)-bound forms and provide an extensive mutagenesis and functional analysis of the structural determinants required for catalysis and streptogramin A recognition. Based on an updated genomic survey across the Vat enzyme family, we identified key conserved residues critical for VatA activity that are not part of theO-acetylation catalytic apparatus. Exploiting such constraints of the Vat active site may lead to the development of streptogramin A compounds that evade inactivation by Vat enzymes while retaining binding to their ribosomal target.
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Dupuis, Michel, and Roland Leclercq. "Activity of a New Oral Streptogramin, XRP2868, against Gram-Positive Cocci Harboring Various Mechanisms of Resistance to Streptogramins." Antimicrobial Agents and Chemotherapy 50, no. 1 (January 2006): 237–42. http://dx.doi.org/10.1128/aac.50.1.237-242.2006.

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ABSTRACT The antibacterial activity of XRP2868, a new oral streptogramin composed of a combination of RPR132552 (streptogramin A) and RPR202868 (streptogramin B), was evaluated against a collection of clinical gram-positive isolates with characterized phenotypes and genotypes of streptogramin resistance. The effects of genes for resistance to streptogramin A or B on the activity of XRP2868 and its components were also tested by cloning these genes individually or in various combinations in gram-positive recipient strains susceptible to quinupristin-dalfopristin. The species tested included Staphylococcus aureus, coagulase-negative staphylococci, Enterococcus faecalis, Enterococcus faecium, Streptococcus pneumoniae, and other species of streptococci. XRP2868 was generally fourfold more potent than quinupristin-dalfopristin against S. aureus, E. faecium, and streptococci and had activity against E. faecalis (MICs = 0.25 to 1 μg/ml). XRP2868 appeared to be affected by the same mechanisms of resistance as those to quinupristin-dalfopristin. Nevertheless, the strong activity of factor A of the oral streptogramin enabled the combination to be very potent against streptogramin-susceptible staphylococci, streptococci, and E. faecium (MICs = 0.03 to 0.25 μg/ml) and to retain low MICs against the strains harboring a mechanism of resistance to factor A or factor B of the streptogramin. However, the combination of mechanisms of resistance to factors A and B caused an increase in the MICs of XRP2868, which reached 1 to 4 μg/ml. As with the other streptogramins, there was a reduction in the bactericidal effect of XRPR2868 when the staphylococcal strains acquired a constitutively expressed erm gene.
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Lina, Gerard, Alain Quaglia, Marie-Elisabeth Reverdy, Roland Leclercq, François Vandenesch, and Jerome Etienne. "Distribution of Genes Encoding Resistance to Macrolides, Lincosamides, and Streptogramins among Staphylococci." Antimicrobial Agents and Chemotherapy 43, no. 5 (May 1, 1999): 1062–66. http://dx.doi.org/10.1128/aac.43.5.1062.

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ABSTRACT The relative frequency of 10 determinants of resistance to macrolides, lincosamides, and streptogramins was investigated by PCR in a series of 294 macrolide-, lincosamide-, and/or streptogramin-resistant clinical isolates of Staphylococcus aureus and coagulase-negative staphylococci isolated in 1995 from 32 French hospitals. Resistance was mainly due to the presence ofermA or ermC genes, which were detected in 259 strains (88%), in particular those resistant to methicillin (78% of the strains). Macrolide resistance due to msrA was more prevalent in coagulase-negative staphylococci (14.6%) than inS. aureus (2.1%). Genes related tolinA/linA′ and conferring resistance to lincomycin were detected in one strain of S. aureus and seven strains of coagulase-negative staphylococci. Resistance to pristinamycin and quinupristin-dalfopristin was phenotypically detected in 10 strains ofS. aureus and in three strains of coagulase-negative staphylococci; it was always associated with resistance to type A streptogramins encoded by vat or vatB genes and occurred in association with erm genes. The vgagene conferring decreased susceptibility to type A streptogramins was present alone in three strains of coagulase-negative staphylococci and in combination with erm genes in 10 strains of coagulase-negative staphylococci. A combination ofvga-vgb-vat and ermA genes was found in a single strain of S. epidermidis.
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Haroche, Julien, Jeanine Allignet, and Névine El Solh. "Tn5406, a New Staphylococcal Transposon Conferring Resistance to Streptogramin A and Related Compounds Including Dalfopristin." Antimicrobial Agents and Chemotherapy 46, no. 8 (August 2002): 2337–43. http://dx.doi.org/10.1128/aac.46.8.2337-2343.2002.

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ABSTRACT We characterized a new transposon, Tn5406 (5,467 bp), in a clinical isolate of Staphylococcus aureus (BM3327). It carries a variant of vgaA, which encodes a putative ABC protein conferring resistance to streptogramin A but not to mixtures of streptogramins A and B. It also carries three putative genes, the products of which exhibit significant similarities (61 to 73% amino acid identity) to the three transposases of the staphylococcal transposon Tn554. Like Tn554, Tn5406 failed to generate target repeats. In BM3327, the single copy of Tn5406 was inserted into the chromosomal att554 site, which is the preferential insertion site of Tn554. In three other independent S. aureus clinical isolates, Tn5406 was either present as a single plasmid copy (BM3318), as two chromosomal copies (BM3252), or both in the chromosome and on a plasmid (BM3385). The Tn5406-carrying plasmids also contain two other genes, vgaB and vatB. The insertion sites of Tn5406 in BM3252 were studied: one copy was in att554, and one copy was in the additional SCCmec element. Amplification experiments revealed circular forms of Tn5406, indicating that this transposon might be active. To our knowledge, a transposon conferring resistance to streptogramin A and related compounds has not been previously described.
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Allignet, Jeanine, Nadia Liassine, and Névine El Solh. "Characterization of a Staphylococcal Plasmid Related to pUB110 and Carrying Two Novel Genes, vatC andvgbB, Encoding Resistance to Streptogramins A and B and Similar Antibiotics." Antimicrobial Agents and Chemotherapy 42, no. 7 (July 1, 1998): 1794–98. http://dx.doi.org/10.1128/aac.42.7.1794.

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ABSTRACT We isolated and sequenced a plasmid, named pIP1714 (4,978 bp), which specifies resistance to streptogramins A and B and the mixture of these compounds. pIP1714 was isolated from a Staphylococcus cohnii subsp. cohnii strain found in the environment of a hospital where pristinamycin was extensively used. Resistance to both compounds and related antibiotics is encoded by two novel, probably cotranscribed genes, (i) vatC, encoding a 212-amino-acid (aa) acetyltransferase that inactivates streptogramin A and that exhibits 58.2 to 69.8% aa identity with the Vat, VatB, and SatA proteins, and (ii) vgbB, encoding a 295-aa lactonase that inactivates streptogramin B and that shows 67% aa identity with the Vgb lactonase. pIP1714 includes a 2,985-bp fragment also found in two rolling-circle replication and mobilizable plasmids, pUB110 and pBC16, from gram-positive bacteria. In all three plasmids, the common fragment was delimited by two direct repeats of four nucleotides (GGGC) and included (i) putative genes closely related to repB, which encodes a replication protein, and topre(mob), which encodes a protein required for conjugative mobilization and site-specific recombination, and (ii) sequences very similar to the double- and single-strand origins (dso, ssoU ) and the recombination site, RSA. The antibiotic resistance genes repBand pre(mob) carried by each of these plasmids were found in the same transcriptional orientation.
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10

Pechère, Jean-Claude. "Streptogramins." Drugs 51, Supplement 1 (1996): 13–19. http://dx.doi.org/10.2165/00003495-199600511-00005.

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Dissertations / Theses on the topic "Streptogramine"

1

Boussens, Béatrice. "Sensibilité des mycoplasmes aux antibiotiques : activité in vitro de deux nouvelles molécules, le RP 59500 (streptogramine) et le RP 67829 (fluoroquinolone)." Bordeaux 2, 1991. http://www.theses.fr/1991BOR23035.

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Bassuel, Virginie. "Macrolides, streptogramines et staphylocoques : étude d'une nouvelle résistance à l'érythromycine par efflux et d'une nouvelle streptogramine, injectable, le RP 59500." Paris 5, 1993. http://www.theses.fr/1993PA05P210.

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Chaume, Grégory Ardisson Janick. "Vers la synthèse totale de la griséoviridine, antibiotique de type streptogramine." [S.l.] : [s.n.], 2008. http://biblioweb.u-cergy.fr/theses/03CERG0256.pdf.

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Chaume, Grégory. "Vers la synthèse totale de la griséoviridine, antibiotique de type streptogramine." Cergy-Pontoise, 2003. http://biblioweb.u-cergy.fr/theses/03CERG0256.pdf.

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Les streptogramines sont des macrolides antibiotiques de type apparentés pour lesquels pratiquement aucun germe ne présente actuellement de résistance acquise. Ils sont en fait constitués d'un mélange de deux groupes de composés A et B d'action synergique. L'objectif de ce travail de thèse a consisté en la synthèse totale de la griséoviridine, streptogramine du groupe A. La stratégie reposait sur la préparation initiale des fragments Nord-Est (C11-N23) et Sud-Ouest (C12-C22) en vue de leur couplage. La synthèse du fragment Nord-Est (C11-N23) a été réalisée selon deux approches différentes, soit par réaction de macrolactonisation, soit par couplage acétylénique-soufre dans des conditions réductrices. La synthèse du fragment Sud-Ouest est axée sur une réaction d'aldolisation énantiosélective. A ce jour, le couplage des deux unités est en cours.
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Kuligowski, Carine. "Contribution a la synthese de streptogramines, macrocyles a activite antibiotique (doctorat : pharmacochimie)." Paris 11, 2001. http://www.theses.fr/2001PA114804.

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Demare, Sandrine. "Influence des impuretés du RP7293 sur la perméabilité et la dissolution des pristinamycines." Paris 11, 2005. http://www.theses.fr/2002PA114838.

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Le RP7293 est un antibiotique d'origine naturelle comportant deux principes actifs, pristinamycine IIA et pristinamycine IA, et un grand nombre d'impuretés de fermentation. Son homologue purifié, appelé RP63160 contient les deux principes actifs. Les paramètres pharmacocinétiques de la PIIA et de la PIA administrée par voie orale varient selon qu'elles sont administrées sous formes de R7293 ou de RP63160 et selon l'état à jeun ou nourri des patients. Le sujet de cette thèse consiste à savoir si les impuretés agissent sur la dissolution des pristinamicynes dans le tractus gastro-instestinal et si elle modifient leur perméabilité. La particularité de ces deux produits étant leur forme physique amorphe, nous nous sommes attachés à décrire dans une partie bibliographqiue les principales caractéristiques des solides amorphes afin de mieux appréhender leur dissolution. Lors des travaux expérimentaux, nous avons développés des outils permettant d'étudier séparément l'absorption (modèle de l'intestin de rat perfusé) et la dissolution (différents types de techniques) des pristinamycines en se situant dans des conditions proches de la physiologie, et en simulant l'état à jeun et l'état nourri. Nous avons aussi mis au point ainsi un modèle dynamique couplant la dissolution et l'absorption. En définitive, il apparaît que les impuretés du RP7293 n'affectent pas la perméabilité des pristinamycines mais sont des poisons de cristallisation de la PIIA, modifiant la dissolution des principes actifs dans le tractus digestif et par la même leurs fractions absorbées. Une appréciation critique des différents modèles utilisés aboutit à une estimation de leur domaine d'utilisation. Enfin, une étude de dissolution du RP63160 enrichi avec une ou plusieurs fractions d'impuretés récoltées par la chromatographie préparative, suggère que les isoflavones pourraient être les poisons de critallisation recherchés.
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Bozdogan, Bülent. "Mécanismes de résistance aux lincosamides et aux streptogramines chez les bactéries à Gram positif." Paris 5, 1999. http://www.theses.fr/1999PA05N132.

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Fournet, Marie-Pierre. "Distribution pulmonaire et bactérienne des macrolides lincosamides, streptogramines et tétracyclines /." Grenoble 2 : ANRT, 1987. http://catalogue.bnf.fr/ark:/12148/cb37605180b.

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Fournet, Marie-Pierre. "Distribution pulmonaire et bactérienne des macrolides : lincosamides, streptogramines et tétracyclines." Paris 12, 1987. http://www.theses.fr/1987PA120039.

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Bouhallab, Saïd. "Mecanisme d'action des facteurs i et ii des pristinamycines : etude de leur synergie et localisation du site de fixation de la pristinamycine ia." Paris 6, 1988. http://www.theses.fr/1988PA066095.

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Books on the topic "Streptogramine"

1

Johnston, Nicole J. Prevalence and characterization of the mechanisms of macrolide, lincosamide, and streptogramin resistance among isolates of Streptococcus pneumoniae and viridans streptococci. Ottawa: National Library of Canada, 1999.

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2

1934-, Neu Harold C., and International Conference on the Macrolides, Azalides, and Streptogramins (2nd : 1994 : Venice, Italy), eds. New macrolides, azalides, and streptogramins in clinical practice. New York: M. Dekker, 1995.

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Neu, Harold C. Macrolides, Azolides and Streptogramins in Clinical Practice (Infectious Disease and Therapy). Informa Healthcare, 1995.

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1939-, Zinner Stephen H., and ICMASK (4th : 1998 : Barcelona, Spain), eds. New considerations for macrolides, azalides, streptogramins, and ketolides. New York: Marcel Dekker, 2000.

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1939-, Zinner Stephen H., and International Conference on the Macrolides, Azalides, and Streptogramins (3rd : 1996 : Lisbon, Portugal), eds. Expanding indications for the new macrolides, azalides, and streptogramins. New York: Dekker, 1997.

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1934-, Neu Harold C., Young Lowell S, and Zinner Stephen H. 1939-, eds. The New macrolides, azalides, and streptogramins: Pharmacology and clinical applications. New York: M. Dekker, 1993.

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Book chapters on the topic "Streptogramine"

1

Bryskier, A. "Streptogramins." In Antimicrobial Agents, 570–91. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815929.ch20.

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Leuthner, Kimberly D., and Michael J. Rybak. "Streptogramin." In Antimicrobial Drug Resistance, 241–45. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-180-2_21.

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Cattoir, Vincent, and Roland Leclercq. "Resistance to Macrolides, Lincosamides, and Streptogramins." In Antimicrobial Drug Resistance, 269–80. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-46718-4_18.

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Roberts, Marilyn C., and Joyce Sutcliffe. "Macrolide, Lincosamide, Streptogramin, Ketolide, and Oxazolidinone Resistance." In Frontiers in Antimicrobial Resistance, 66–84. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555817572.ch6.

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Fussenegger, M., B. Von Stockar, C. Fux, M. Rimann, R. Morris, C. J. Thompson, and J. E. Bailey. "A Novel Mammalian Gene Regulation System Responsive to Streptogramin Antibiotics." In Animal Cell Technology: Products from Cells, Cells as Products, 19–22. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/0-306-46875-1_3.

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Roberts, Marilyn C. "rRNA Methylases and Resistance to Macrolide, Lincosamide, Streptogramin, Ketolide, and Oxazolidinone (MLSKO) Antibiotics." In Enzyme-Mediated Resistance to Antibiotics, 53–63. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815615.ch5.

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Barbanti, Fabrizio, François Wasels, and Patrizia Spigaglia. "Transfer of Clostridium difficile Genetic Elements Conferring Resistance to Macrolide–Lincosamide–Streptogramin B (MLSB) Antibiotics." In Methods in Molecular Biology, 187–98. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6361-4_14.

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"Streptogramins." In Meyler's Side Effects of Drugs, 499. Elsevier, 2016. http://dx.doi.org/10.1016/b978-0-444-53717-1.01472-4.

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Soriano, Francisco. "Streptogramins." In Antibiotic and Chemotherapy, 334–36. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-7020-4064-1.00028-2.

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"Streptogramins." In Meyler's Side Effects of Drugs: The International Encyclopedia of Adverse Drug Reactions and Interactions, 3182–85. Elsevier, 2006. http://dx.doi.org/10.1016/b0-44-451005-2/00503-9.

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