Gotowe bibliografie tematyczne / Aminoglycoside antibiotics

Gotowa bibliografia na temat „Aminoglycoside antibiotics”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 20 lutego 2023

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Artykuły w czasopismach na temat "Aminoglycoside antibiotics"

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Stogios, Peter J., Peter Spanogiannopoulos, Elena Evdokimova, Olga Egorova, Tushar Shakya, Nick Todorovic, Alfredo Capretta, Gerard D. Wright i Alexei Savchenko. "Structure-guided optimization of protein kinase inhibitors reverses aminoglycoside antibiotic resistance". Biochemical Journal 454, nr 2 (9.08.2013): 191–200. http://dx.doi.org/10.1042/bj20130317.

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Activity of the aminoglycoside phosphotransferase APH(3′)-Ia leads to resistance to aminoglycoside antibiotics in pathogenic Gram-negative bacteria, and contributes to the clinical obsolescence of this class of antibiotics. One strategy to rescue compromised antibiotics such as aminoglycosides is targeting the enzymes that confer resistance with small molecules. We demonstrated previously that ePK (eukaryotic protein kinase) inhibitors could inhibit APH enzymes, owing to the structural similarity between these two enzyme families. However, limited structural information of enzyme–inhibitor complexes hindered interpretation of the results. In addition, cross-reactivity of compounds between APHs and ePKs represents an obstacle to their use as aminoglycoside adjuvants to rescue aminoglycoside antibiotic activity. In the present study, we structurally and functionally characterize inhibition of APH(3′)-Ia by three diverse chemical scaffolds, anthrapyrazolone, 4-anilinoquinazoline and PP (pyrazolopyrimidine), and reveal distinctions in the binding mode of anthrapyrazolone and PP compounds to APH(3′)-Ia compared with ePKs. Using this observation, we identify PP derivatives that select against ePKs, attenuate APH(3′)-Ia activity and rescue aminoglycoside antibiotic activity against a resistant Escherichia coli strain. The structures described in the present paper and the inhibition studies provide an important opportunity for structure-based design of compounds to target aminoglycoside phosphotransferases for inhibition, potentially overcoming this form of antibiotic resistance.
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Trylska, Joanna, i Marta Kulik. "Interactions of aminoglycoside antibiotics with rRNA". Biochemical Society Transactions 44, nr 4 (15.08.2016): 987–93. http://dx.doi.org/10.1042/bst20160087.

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Aminoglycoside antibiotics are protein synthesis inhibitors applied to treat infections caused mainly by aerobic Gram-negative bacteria. Due to their adverse side effects they are last resort antibiotics typically used to combat pathogens resistant to other drugs. Aminoglycosides target ribosomes. We describe the interactions of aminoglycoside antibiotics containing a 2-deoxystreptamine (2-DOS) ring with 16S rRNA. We review the computational studies, with a focus on molecular dynamics (MD) simulations performed on RNA models mimicking the 2-DOS aminoglycoside binding site in the small ribosomal subunit. We also briefly discuss thermodynamics of interactions of these aminoglycosides with their 16S RNA target.
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Toth, Marta, Hilary Frase, Nuno T. Antunes i Sergei B. Vakulenko. "Novel Aminoglycoside 2″-Phosphotransferase Identified in a Gram-Negative Pathogen". Antimicrobial Agents and Chemotherapy 57, nr 1 (5.11.2012): 452–57. http://dx.doi.org/10.1128/aac.02049-12.

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ABSTRACTAminoglycoside 2″-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci. We describe a novel aminoglycoside 2″-phosphotransferase from the Gram-negative pathogenCampylobacter jejuni, which shares 78% amino acid sequence identity with the APH(2″)-Ia domain of the bifunctional aminoglycoside-modifying enzyme aminoglycoside (6′) acetyltransferase-Ie/aminoglycoside 2″-phosphotransferase-Ia or AAC(6′)-Ie/APH(2″)-Ia from Gram-positive cocci, which we called APH(2″)-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin, but not to any of the 4,5-disubstituted antibiotics tested. Steady-state kinetic studies demonstrated that GTP, and not ATP, is the preferred cosubstrate for APH(2″)-If. The enzyme phosphorylates the majority of 4,6-disubstituted aminoglycosides with high catalytic efficiencies (kcat/Km= 105to 107M−1s−1), while the catalytic efficiencies against the 4,6-disubstituted antibiotics amikacin and isepamicin are 1 to 2 orders of magnitude lower, due mainly to the low apparent affinities of these substrates for the enzyme. Both 4,5-disubstituted antibiotics and the atypical aminoglycoside neamine are not substrates of APH(2″)-If, but are inhibitors. The antibiotic susceptibility and substrate profiles of APH(2″)-If are very similar to those of the APH(2″)-Ia phosphotransferase domain of the bifunctional AAC(6′)-Ie/APH(2″)-Ia enzyme.
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Li, Zhongyan, Fengqi Sun, Xinmiao Fu i Yajuan Chen. "5-Methylindole kills various bacterial pathogens and potentiates aminoglycoside against methicillin-resistant Staphylococcus aureus". PeerJ 10 (14.09.2022): e14010. http://dx.doi.org/10.7717/peerj.14010.

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Antibiotic resistance of bacterial pathogens has become a severe threat to human health. To counteract antibiotic resistance, it is of significance to discover new antibiotics and also improve the efficacy of existing antibiotics. Here we show that 5-methylindole, a derivative of the interspecies signaling molecule indole, is able to directly kill various Gram-positive pathogens (e.g., Staphylococcus aureus and Enterococcus faecalis) and also Gram-negative ones (e.g., Escherichia coli and Pseudomonas aeruginosa), with 2-methylindole being less potent. Particularly, 5-methylindole can kill methicillin-resistant S. aureus, multidrug-resistant Klebsiella pneumoniae, Mycobacterium tuberculosis, and antibiotic-tolerant S. aureus persisters. Furthermore, 5-methylindole significantly potentiates aminoglycoside antibiotics, but not fluoroquinolones, killing of S. aureus. In addition, 5-iodoindole also potentiates aminoglycosides. Our findings open a new avenue to develop indole derivatives like 5-methylindole as antibacterial agents or adjuvants of aminoglycoside.
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Stefan-Mikic, Sandra, Ana Sabo, Ana Gobor-Fodor i Marija Vasovic. "Aminoglycoside antibiotics and postantibiotic effect". Medical review 55, nr 1-2 (2002): 19–22. http://dx.doi.org/10.2298/mpns0202019s.

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Man has been fighting diseases for centuries. One of the major battles is against microorganisms and diseases they cause. A health education course was organized on prescribing aminoglycoside antibiotics and postantibiotic effect. The aim of the course was to change the prescription habits in our colleagues. The postantibiotic effect of aminoglycoside antibiotics as well as impact of subinhibiting doses on duration of postantibiotic effect requires modification of previous therapeutic protocols. Single daily dose has the same or even greater effect than multiple daily doses. The toxicity of aminoglycosides is not increased and remains the same or smaller in single daily regimens. Results The single daily dose regimen of aminoglycosides has been used in 63.6% of cases in Clinic for Infectious Diseases of the Clinical Center of Novi Sad, 41.2% in Outpatient Health Care Center of Novi Sad "Liman" and this regimen has not been used in General Practice Department, Children's Health Care Department and Ear, Nose and Throat Clinic at all. The twice daily regimen has been used instead. Conclusion Doctors are aware of the postantibiotic effect, but vast majority are still bound to their old habits in regard to prescribing antibiotics. Our educational course failed to achieve its goal.
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Forge, Andrew, i Jochen Schacht. "Aminoglycoside Antibiotics". Audiology and Neuro-Otology 5, nr 1 (2000): 3–22. http://dx.doi.org/10.1159/000013861.

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Caldwell, Shane, i Albert Berghuis. "A catalytic switch uncovered in gentamicin resistance kinase APH(2'')-Ia". Acta Crystallographica Section A Foundations and Advances 70, a1 (5.08.2014): C704. http://dx.doi.org/10.1107/s205327331409295x.

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The APH(2'')-Ia domain of the bifunctional aminoglycoside resistance enzyme AAC(6')-Ie/APH(2'')-Ia confers high-level resistance to aminoglycoside antibiotics. Crystal structures of this kinase domain in complex with GTP analogues and acceptor substrates have uncovered a surprising conformational bistability of the GTP substrate, which may reduce futile hydrolysis of the cofactor by the enzyme. This conformational switch is influenced by the binding of aminoglycosides, and may represent an adaptive feature of the enzyme, improving its evolutionary fitness in bacterial populations. This mechanism combines with a remarkable flexibility observed in the binding of diverse aminoglycoside substrates to make this enzyme a formidable antibiotic resistance machine.
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Henley, Charles M. "Kanamycin Depletes Cochlear Polyamines in the Developing Rat". Otolaryngology–Head and Neck Surgery 110, nr 1 (styczeń 1994): 103–9. http://dx.doi.org/10.1177/019459989411000112.

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Developing mammals are more sensitive to aminoglycoside antibiotics and other ototoxic agents than adults, with maximum sensitivity occurring during the period of anatomic and functional maturation of the cochlea. For the aminoglycoside antibiotics, the hypersensitive period in rats occurs during the second and third postnatal weeks. Toxicity is initially expressed as outer hair cell (OHC) damage in the high-frequency, basal region of the cochlea. Distortion-product otoacoustic emissions (DPOAEs), physiologic measures of OHC function, are particularly sensitive to aminoglycoside exposure during the period of rapid cochlear physiologic development. Toxicity is characterized by increased DPOAE thresholds and decreased amplitudes. The mechanism of developmental sensitivity to aminoglycosides is unknown. A potential biochemical target of aminoglycosides is the ornithine decarboxylase (ODC)-polyamine pathway. ODC activity is elevated in the developing rat cochlea, aminoglycosides inhibit cochlear ODC in developing rats, and α-difluoromethylornithine (a specific ODC inhibitor) impairs development of cochlear function. In the present study we demonstrate an incomplete polyamnine response to aminoglycoside damage, characterized by inhibition of the polyamines spermidine and spermine and accumulation of putrescine in the organ of Corti. Aminoglycoside inhibition of polyamine synthesis may mediate developmental ototoxic hypersensitivity by interfering with developmental and repair processes.
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Fong, Desiree H., i Albert M. Berghuis. "Structural Basis of APH(3′)-IIIa-Mediated Resistance to N1-Substituted Aminoglycoside Antibiotics". Antimicrobial Agents and Chemotherapy 53, nr 7 (11.05.2009): 3049–55. http://dx.doi.org/10.1128/aac.00062-09.

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ABSTRACT Butirosin is unique among the naturally occurring aminoglycosides, having a substituted amino group at position 1 (N1) of the 2-deoxystreptamine ring with an (S)-4-amino-2-hydroxybutyrate (AHB) group. While bacterial resistance to aminoglycosides can be ascribed chiefly to drug inactivation by plasmid-encoded aminoglycoside-modifying enzymes, the presence of an AHB group protects the aminoglycoside from binding to many resistance enzymes, and hence, the antibiotic retains its bactericidal properties. Consequently, several semisynthetic N1-substituted aminoglycosides, such as amikacin, isepamicin, and netilmicin, were developed. Unfortunately, butirosin, amikacin, and isepamicin are not resistant to inactivation by 3′-aminoglycoside O-phosphotransferase type IIIa [APH(3′)-IIIa]. We report here the crystal structure of APH(3′)-IIIa in complex with an ATP analog, AMPPNP [adenosine 5′-(β,γ-imido)triphosphate], and butirosin A to 2.4-Å resolution. The structure shows that butirosin A binds to the enzyme in a manner analogous to other 4,5-disubstituted aminoglycosides, and the flexible antibiotic-binding loop is key to the accommodation of structurally diverse substrates. Based on the crystal structure, we have also constructed a model of APH(3′)-IIIa in complex with amikacin, a commonly used semisynthetic N1-substituted 4,6-disubstituted aminoglycoside. Together, these results suggest a strategy to further derivatize the AHB group in order to generate new aminoglycoside derivatives that can elude inactivation by resistance enzymes while maintaining their ability to bind to the ribosomal A site.
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Carvalho, André, Didier Mazel i Zeynep Baharoglu. "Deficiency in cytosine DNA methylation leads to high chaperonin expression and tolerance to aminoglycosides in Vibrio cholerae". PLOS Genetics 17, nr 10 (20.10.2021): e1009748. http://dx.doi.org/10.1371/journal.pgen.1009748.

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Antibiotic resistance has become a major global issue. Understanding the molecular mechanisms underlying microbial adaptation to antibiotics is of keen importance to fight Antimicrobial Resistance (AMR). Aminoglycosides are a class of antibiotics that target the small subunit of the bacterial ribosome, disrupting translational fidelity and increasing the levels of misfolded proteins in the cell. In this work, we investigated the role of VchM, a DNA methyltransferase, in the response of the human pathogen Vibrio cholerae to aminoglycosides. VchM is a V. cholerae specific orphan m5C DNA methyltransferase that generates cytosine methylation at 5’-RCCGGY-3’ motifs. We show that deletion of vchM, although causing a growth defect in absence of stress, allows V. cholerae cells to cope with aminoglycoside stress at both sub-lethal and lethal concentrations of these antibiotics. Through transcriptomic and genetic approaches, we show that groESL-2 (a specific set of chaperonin-encoding genes located on the second chromosome of V. cholerae), are upregulated in cells lacking vchM and are needed for the tolerance of vchM mutant to lethal aminoglycoside treatment, likely by fighting aminoglycoside-induced misfolded proteins. Interestingly, preventing VchM methylation of the four RCCGGY sites located in groESL-2 region, leads to a higher expression of these genes in WT cells, showing that the expression of these chaperonins is modulated in V. cholerae by DNA methylation.
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Rozprawy doktorskie na temat "Aminoglycoside antibiotics"

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Zhu, Hongkun. "Studies of Aminoglycoside Antibiotics". The Ohio State University, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=osu1462802472.

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Yung, Man Wah. "Aminoglycoside ototoxicity". Thesis, University of Liverpool, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235543.

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Wang, Hai. "Design, synthesis and RNA binding of aminoglycoside antibiotics /". Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1998. http://wwwlib.umi.com/cr/ucsd/fullcit?p9820848.

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McKay, Geoffrey A. "Characterization of aminoglycoside phosphotransferase APH(3')-IIIa : an enterococcal enzyme conferring resistance to aminoglycoside antibiotics /". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0034/NQ66223.pdf.

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Perez, Fernandez Déborah. "Aminoglycoside antibiotics to selectively target bacterial 16S ribosomal RNA /". Zürich : ETH, 2007. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17284.

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Ball, J. M. "Antibiotic production and inactivation by a producing organism". Thesis, University of Southampton, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.234469.

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Nessim, Gergawy Mourad A. "Effects of aminoglycoside antibiotics on intracellular processes in cerebral vasospasm". Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/mq22646.pdf.

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Savic, Miloje. "Structural basis of aminoglycoside antibiotics resistance through ribosomal RNA methylation". Thesis, University of Manchester, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.503020.

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Zent, Clive Steven, i Clive Steven Zent. "The use of aminoglycoside antibiotic therapy in neutropaenic patients with haematological disease". Master's thesis, University of Cape Town, 1991. http://hdl.handle.net/11427/24969.

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The use of aminoglycosides in the treatment of the febrile neutropaenic patient with haematological disease is difficult and often suboptimal. This study reviews the available literature to establish therapeutic guidelines in this population and then reports the use of a Bayesian statistics based predictive model to implement and manage therapy in 10 patients. A review of the literature on aminoglycoside Pharmacology and clinical use is essential to determine therapeutic guidelines for this population. Aminoglycosides are amino sugars in glycosidic linkage and are polycations at physiological PH. The antibiotic effect is mediated through inhibition of protein synthesis and disruption of cell membrane integrity. Principal use is in treatment of Gram negative infection although aminoglycosides have activity against some Gram positive organisms including staphylococci. Aminoglycosides are inactive against anaerobes. Acquired resistance is mediated by bacterial enzymatic drug metabolism. Aminoglycosides are nephro- and ototoxic, this is the major constraint in clinical use.
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Mikkelsen, Helga. "Influence of growth mode and aminoglycoside antibiotics on Pseudomonas aeruginosa physiology". Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611950.

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Książki na temat "Aminoglycoside antibiotics"

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Arya, D. P. Aminoglycoside antibiotics: From chemical biology to drug discovery. Hoboken, N.J: Wiley-Interscience, 2007.

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Lazenby, Charles Mark. The effect of aminoglycoside antibiotics on erythrocyte membrane potassium ion transport. Birmingham: Aston University. Department of Pharmaceutical Sciences, 1989.

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Umezawa, Hamao, i Irving R. Hooper. Aminoglycoside Antibiotics. Brand: Springer, 2011.

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Arya, Dev P., red. Aminoglycoside Antibiotics. Wiley, 2007. http://dx.doi.org/10.1002/9780470149676.

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Koeda, T., Y. Ito, Hamao Umezawa i Irving R. Hooper. Aminoglycoside Antibiotics. Springer London, Limited, 2012.

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Barnes, William G., i Glenn R. Hodges. Aminoglycoside Antibiotics a Guide to Therapy. Taylor & Francis Group, 2019.

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Barnes, William G., i Glenn R. Hodges. Aminoglycoside Antibiotics a Guide to Therapy. Taylor & Francis Group, 2019.

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Barnes, William G., i Glenn R. Hodges. Aminoglycoside Antibiotics a Guide to Therapy. Taylor & Francis Group, 2019.

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Barnes, William G., i Glenn R. Hodges. Aminoglycoside Antibiotics: A Guide to Therapy. Taylor & Francis Group, 2019.

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Barnes, William G., i Glenn R. Hodges. Aminoglycoside Antibiotics a Guide to Therapy. Taylor & Francis Group, 2019.

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Części książek na temat "Aminoglycoside antibiotics"

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Wright, Gerard D., Albert M. Berghuis i Shahriar Mobashery. "Aminoglycoside Antibiotics". W Resolving the Antibiotic Paradox, 27–69. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-4897-3_4.

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Majumder, Kanchana, Lianhu Wei, Subhash C. Annedi i Lakshmi P. Kotra. "Aminoglycoside Antibiotics". W Enzyme-Mediated Resistance to Antibiotics, 7–20. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815615.ch2.

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Dax, Scott L. "Aminoglycoside antibiotics". W Antibacterial Chemotherapeutic Agents, 206–40. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-009-0097-4_5.

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Kirst, Herbert A., i Flavia Marinelli. "Aminoglycoside Antibiotics". W Antimicrobials, 193–209. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-662-45786-3_10.

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Puglisi, Joseph D., Scott C. Blanchard, Kam D. Dahlquist, Robert G. Eason, Dominique Fourmy, Stephen R. Lynch, Michael I. Recht i Satoko Yoshizawa. "Aminoglycoside Antibiotics and Decoding". W The Ribosome, 419–29. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818142.ch34.

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Kondo, Jiro, i Eric Westhof. "Aminoglycoside Antibiotics: Structural Decoding of Inhibitors Targeting the Ribosomal Decoding A Site". W Antibiotics, 453–70. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527659685.ch19.

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Wright, Gerard D., i Albert M. Berghuis. "Structural Aspects of Aminoglycoside-Modifying Enzymes". W Enzyme-Mediated Resistance to Antibiotics, 21–33. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815615.ch3.

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Hanko, Valoran P., i Jeffrey S. Rohrer. "Ion Chromatography Analysis of Aminoglycoside Antibiotics". W Applications of Ion Chromatography for Pharmaceutical and Biological Products, 175–92. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9781118147009.ch8.

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S., Daniel, Malvika Kaul i Christopher M. Barbieri. "Ribosomal RNA Recognition by Aminoglycoside Antibiotics". W Topics in Current Chemistry, 179–204. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/b100447.

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Schroeder, R., i U. von Ahsen. "Interaction of Aminoglycoside Antibiotics with RNA". W Nucleic Acids and Molecular Biology, 53–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61202-2_4.

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Streszczenia konferencji na temat "Aminoglycoside antibiotics"

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Chung, Donghoon, Woohyun Choi, Yungoo Song i Changyun Park. "Adsorption and Disorption Characteristics of Smectites and Aminoglycoside Antibiotics". W Goldschmidt2020. Geochemical Society, 2020. http://dx.doi.org/10.46427/gold2020.444.

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Tiwow, Vanny M. A. "Determination of stability constants of aminoglycoside antibiotics with their metal complexes". W 4TH INTERNATIONAL CONFERENCE ON MATHEMATICS AND NATURAL SCIENCES (ICMNS 2012): Science for Health, Food and Sustainable Energy. AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4868835.

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Chung, Donghoon, Il-Mo Kang, Il-Mo Kang, Young Goo Song, Young Goo Song, Changyun Park, Changyun Park, Yungoo Song i Yungoo Song. "THE CHARACTERISTICS OF CLAY MINERALS AFFECT CLAY-ANTIBIOTIC HYBRIDS : SMECTITE GROUP MINERALS AND AMINOGLYCOSIDE SERIES ANTIBIOTICS". W GSA Annual Meeting in Phoenix, Arizona, USA - 2019. Geological Society of America, 2019. http://dx.doi.org/10.1130/abs/2019am-336368.

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Wu, Lingzhi, Lihua Tang, Xiaofei Hu i Dong Hu. "Thermodynamic studies of the interaction of phosphatidylinositol phosphate with aminoglycosides antibiotics". W 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5966304.

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Raporty organizacyjne na temat "Aminoglycoside antibiotics"

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McCarthy, Noel, Eileen Taylor, Martin Maiden, Alison Cody, Melissa Jansen van Rensburg, Margaret Varga, Sophie Hedges i in. Enhanced molecular-based (MLST/whole genome) surveillance and source attribution of Campylobacter infections in the UK. Food Standards Agency, lipiec 2021. http://dx.doi.org/10.46756/sci.fsa.ksj135.

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This human campylobacteriosis sentinel surveillance project was based at two sites in Oxfordshire and North East England chosen (i) to be representative of the English population on the Office for National Statistics urban-rural classification and (ii) to provide continuity with genetic surveillance started in Oxfordshire in October 2003. Between October 2015 and September 2018 epidemiological questionnaires and genome sequencing of isolates from human cases was accompanied by sampling and genome sequencing of isolates from possible food animal sources. The principal aim was to estimate the contributions of the main sources of human infection and to identify any changes over time. An extension to the project focussed on antimicrobial resistance in study isolates and older archived isolates. These older isolates were from earlier years at the Oxfordshire site and the earliest available coherent set of isolates from the national archive at Public Health England (1997/8). The aim of this additional work was to analyse the emergence of the antimicrobial resistance that is now present among human isolates and to describe and compare antimicrobial resistance in recent food animal isolates. Having identified the presence of bias in population genetic attribution, and that this was not addressed in the published literature, this study developed an approach to adjust for bias in population genetic attribution, and an alternative approach to attribution using sentinel types. Using these approaches the study estimated that approximately 70% of Campylobacter jejuni and just under 50% of C. coli infection in our sample was linked to the chicken source and that this was relatively stable over time. Ruminants were identified as the second most common source for C. jejuni and the most common for C. coli where there was also some evidence for pig as a source although less common than ruminant or chicken. These genomic attributions of themselves make no inference on routes of transmission. However, those infected with isolates genetically typical of chicken origin were substantially more likely to have eaten chicken than those infected with ruminant types. Consumption of lamb’s liver was very strongly associated with infection by a strain genetically typical of a ruminant source. These findings support consumption of these foods as being important in the transmission of these infections and highlight a potentially important role for lamb’s liver consumption as a source of Campylobacter infection. Antimicrobial resistance was predicted from genomic data using a pipeline validated by Public Health England and using BIGSdb software. In C. jejuni this showed a nine-fold increase in resistance to fluoroquinolones from 1997 to 2018. Tetracycline resistance was also common, with higher initial resistance (1997) and less substantial change over time. Resistance to aminoglycosides or macrolides remained low in human cases across all time periods. Among C. jejuni food animal isolates, fluoroquinolone resistance was common among isolates from chicken and substantially less common among ruminants, ducks or pigs. Tetracycline resistance was common across chicken, duck and pig but lower among ruminant origin isolates. In C. coli resistance to all four antimicrobial classes rose from low levels in 1997. The fluoroquinolone rise appears to have levelled off earlier and among animals, levels are high in duck as well as chicken isolates, although based on small sample sizes, macrolide and aminoglycoside resistance, was substantially higher than for C. jejuni among humans and highest among pig origin isolates. Tetracycline resistance is high in isolates from pigs and the very small sample from ducks. Antibiotic use following diagnosis was relatively high (43.4%) among respondents in the human surveillance study. Moreover, it varied substantially across sites and was highest among non-elderly adults compared to older adults or children suggesting opportunities for improved antimicrobial stewardship. The study also found evidence for stable lineages over time across human and source animal species as well as some tighter genomic clusters that may represent outbreaks. The genomic dataset will allow extensive further work beyond the specific goals of the study. This has been made accessible on the web, with access supported by data visualisation tools.
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