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  1. Book: Antimicrobial therapeutics reviews

    Bush, Karen

    the bacterial cell wall as an antimicrobial target

    (Annals of the New York Academy of Sciences ; 1277)

    2013  

    Author's details iss. ed.: Karen Bush
    Series title Annals of the New York Academy of Sciences ; 1277
    Collection
    Language English
    Size VII, 159 S. : Ill., graph. Darst.
    Publisher Wiley Periodicals
    Publishing place Malden, Mass
    Publishing country United States
    Document type Book
    HBZ-ID HT017705933
    ISBN 978-1-57331-879-2 ; 1-57331-879-5
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

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    Se 110 -1277- verfügbar in Königswinter Königswinter

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  2. Article ; Online: Classification for β-lactamases: historical perspectives.

    Bush, Karen

    Expert review of anti-infective therapy

    2023  Volume 21, Issue 5, Page(s) 513–522

    Abstract: Introduction: β-Lactamases are some of the most prevalent and well-studied families of enzymes, especially in the area of antibiotic resistance. Early attempts to categorize them used either functional names, such as penicillinase or cephalosporinase or ...

    Abstract Introduction: β-Lactamases are some of the most prevalent and well-studied families of enzymes, especially in the area of antibiotic resistance. Early attempts to categorize them used either functional names, such as penicillinase or cephalosporinase or structural designations into classes A and B. Increasing diversity of the properties of these enzymes has required a more expansive approach to nomenclature.
    Areas covered: Historical designations for early β-lactamases relied heavily on functional names based on the biochemical properties of purified enzymes. As amino acid sequences began to be reported for a select group of these enzymes, classes of β-lactamases were defined, with a major lumping of enzymes into those that had active site serine residues (class A, C, and D) and those that were metallo-β-lactamases (MBLs or class B). More recent classification schemes, as determined through a Medline search, have attempted to incorporate both functional and structural features, using functional groups and subgroups to name β-lactamases within the same structural class. Nomenclature of these enzymes is now under the purview of the NCBI (National Center for Biotechnology Information).
    Expert opinion: β-Lactamase nomenclature will continue to evolve with the identification of new enzymes and new functionalities.
    MeSH term(s) Humans ; beta-Lactamases/genetics ; beta-Lactamase Inhibitors ; Anti-Bacterial Agents/pharmacology
    Chemical Substances beta-Lactamases (EC 3.5.2.6) ; beta-Lactamase Inhibitors ; Anti-Bacterial Agents
    Language English
    Publishing date 2023-04-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 2181279-2
    ISSN 1744-8336 ; 1478-7210
    ISSN (online) 1744-8336
    ISSN 1478-7210
    DOI 10.1080/14787210.2023.2194633
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6106: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Book: Antimicrobial therapeutics reviews

    Bush, Karen

    antibiotics that target the ribosome

    (Annals of the New York Academy of Sciences ; 1241)

    2011  

    Author's details iss. ed.: Karen Bush
    Series title Annals of the New York Academy of Sciences ; 1241
    Collection
    Language English
    Size 169 S. : Ill., graph. Darst., Kt.
    Publisher Wiley Periodicals
    Publishing place Boston, Mass
    Publishing country United States
    Document type Book
    HBZ-ID HT017118276
    ISBN 978-1-57331-848-8 ; 1-57331-848-5
    Database Catalogue ZB MED Medicine, Health

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  4. Book: Antimicrobial therapeutics reviews

    Bush, Karen

    (Annals of the New York Academy of Sciences ; 1213)

    2010  

    Author's details iss. ed. Karen Bush
    Series title Annals of the New York Academy of Sciences ; 1213
    Collection
    Language English
    Size 136 S. : Ill., graph. Darst.
    Publisher Wiley u.a.
    Publishing place Hoboken, NJ
    Publishing country United States
    Document type Book
    HBZ-ID HT016661516
    ISBN 1-57331-788-8 ; 978-1-57331-788-7
    Database Catalogue ZB MED Medicine, Health

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    Se 110 -1213- verfügbar in Königswinter Königswinter

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  5. Book: What is influencing pharmaceutical company decisions to conduct anti-infective drug discovery?

    Bush, Karen

    (Clinical microbiology and infection ; 10, Suppl. 4)

    2004  

    Author's details guest ed. K. Bush
    Series title Clinical microbiology and infection ; 10, Suppl. 4
    Collection
    Language English
    Size 36 S. : graph. Darst.
    Publisher Blackwell Science
    Publishing place Oxford
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT014205643
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    Zs A 4541 -10,Suppl.4- not available for loan Zeitschriften-Lesesaal

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  6. Article ; Online: A Meandering Path from Biochemist to Microbiologist.

    Bush, Karen

    ACS infectious diseases

    2018  Volume 5, Issue 1, Page(s) 1–3

    Abstract: Not all career paths are clearly defined from the beginning. In my case, biochemistry training in enzymology provided the tools to move from a basic research beginning in biophysical/bioorganic chemistry to an applied microbiology career in antibiotic ... ...

    Abstract Not all career paths are clearly defined from the beginning. In my case, biochemistry training in enzymology provided the tools to move from a basic research beginning in biophysical/bioorganic chemistry to an applied microbiology career in antibiotic drug discovery and development. This pathway required essential contributions from family, professional colleagues, co-workers, and mentors who all provided input at critical times during changes in career directions. As a result of applying skills from previous research positions to new sets of challenges, my contributions to various antibiotic research programs led to the introduction of valuable antimicrobial agents currently used in the treatment of infected patients.
    MeSH term(s) Biochemistry ; Career Choice ; History, 20th Century ; History, 21st Century ; Humans ; Microbiology ; Research/history
    Language English
    Publishing date 2018-12-04
    Publishing country United States
    Document type Autobiography ; Historical Article ; Journal Article ; Personal Narrative
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.8b00261
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Past and Present Perspectives on β-Lactamases.

    Bush, Karen

    Antimicrobial agents and chemotherapy

    2018  Volume 62, Issue 10

    Abstract: β-Lactamases, the major resistance determinant for β-lactam antibiotics in Gram-negative bacteria, are ancient enzymes whose origins can be traced back millions of years ago. These well-studied enzymes, currently numbering almost 2,800 unique proteins, ... ...

    Abstract β-Lactamases, the major resistance determinant for β-lactam antibiotics in Gram-negative bacteria, are ancient enzymes whose origins can be traced back millions of years ago. These well-studied enzymes, currently numbering almost 2,800 unique proteins, initially emerged from environmental sources, most likely to protect a producing bacterium from attack by naturally occurring β-lactams. Their ancestors were presumably penicillin-binding proteins that share sequence homology with β-lactamases possessing an active-site serine. Metallo-β-lactamases also exist, with one or two catalytically functional zinc ions. Although penicillinases in Gram-positive bacteria were reported shortly after penicillin was introduced clinically, transmissible β-lactamases that could hydrolyze recently approved cephalosporins, monobactams, and carbapenems later became important in Gram-negative pathogens. Nomenclature is based on one of two major systems. Originally, functional classifications were used, based on substrate and inhibitor profiles. A later scheme classifies β-lactamases according to amino acid sequences, resulting in class A, B, C, and D enzymes. A more recent nomenclature combines the molecular and biochemical classifications into 17 functional groups that describe most β-lactamases. Some of the most problematic enzymes in the clinical community include extended-spectrum β-lactamases (ESBLs) and the serine and metallo-carbapenemases, all of which are at least partially addressed with new β-lactamase inhibitor combinations. New enzyme variants continue to be described, partly because of the ease of obtaining sequence data from whole-genome sequencing studies. Often, these new enzymes are devoid of any phenotypic descriptions, making it more difficult for clinicians and antibiotic researchers to address new challenges that may be posed by unusual β-lactamases.
    MeSH term(s) Bacterial Proteins/metabolism ; Cephalosporins/pharmacology ; Gram-Negative Bacteria/drug effects ; Gram-Positive Bacteria/drug effects ; Penicillinase/metabolism ; beta-Lactamases/metabolism ; beta-Lactams/pharmacology
    Chemical Substances Bacterial Proteins ; Cephalosporins ; beta-Lactams ; Penicillinase (EC 3.5.2.-) ; beta-Lactamases (EC 3.5.2.6) ; carbapenemase (EC 3.5.2.6)
    Language English
    Publishing date 2018-09-24
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/AAC.01076-18
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 809: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Einzelsignatur: Show issues

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  8. Book: The drama of DNA

    Rothenberg, Karen H. / Bush, Lynn Wein

    narrative genomics

    2014  

    Author's details Karen H. Rothenberg and Lynn Wein Bush
    Keywords Genomics ; Drama ; Teaching / methods
    Language English
    Size XIII, 211 S.
    Publisher Oxford Univ. Press
    Publishing place Oxford u.a.
    Publishing country Great Britain
    Document type Book
    Note Includes bibliographical references
    HBZ-ID HT018303647
    ISBN 978-0-19-930935-1 ; 0-19-930935-3
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    2014 A 2503 available for loan (reading room) Lesesaal EG

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  9. Article ; Online: Game Changers: New β-Lactamase Inhibitor Combinations Targeting Antibiotic Resistance in Gram-Negative Bacteria.

    Bush, Karen

    ACS infectious diseases

    2017  Volume 4, Issue 2, Page(s) 84–87

    Abstract: Recent regulatory approvals for the β-lactam inhibitor combinations of ceftazidime-avibactam and meropenem-vaborbactam have provided two novel therapeutic options for the treatment of multidrug-resistant infections caused by Gram-negative bacteria. Most ... ...

    Abstract Recent regulatory approvals for the β-lactam inhibitor combinations of ceftazidime-avibactam and meropenem-vaborbactam have provided two novel therapeutic options for the treatment of multidrug-resistant infections caused by Gram-negative bacteria. Most importantly, these combination agents have satisfied an important medical need related to antibiotic-resistant Klebsiella pneumoniae that produce serine carbapenemases, especially the Klebsiella pneumoniae carbapenemase (KPC) enzymes. Both combinations contain non-β-lactam β-lactamase inhibitors of novel chemical classes not previously developed as antibacterial agents, the diazabicyclooctanes and cyclic boronic acid derivatives. Their rapid development and approval programs have spurred a number of similar inhibitor combinations that will need to differentiate themselves for commercial success. Gaps still exist for the treatment of infections caused by multidrug-resistant Pseudomonas aeruginosa, Acinetobacter spp., and metallo-β-lactamase-producing pathogens. Overall, the new β-lactamase inhibitor combinations have infused new life into the search for new antibacterial agents to treat multidrug-resistant bacteria.
    MeSH term(s) Drug Resistance, Bacterial ; Gram-Negative Bacteria/drug effects ; Molecular Structure ; beta-Lactamase Inhibitors/chemistry ; beta-Lactamase Inhibitors/pharmacology
    Chemical Substances beta-Lactamase Inhibitors
    Language English
    Publishing date 2017-12-12
    Publishing country United States
    Document type Letter ; Research Support, Non-U.S. Gov't
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.7b00243
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Overcoming β-lactam resistance in Gram-negative pathogens.

    Bush, Karen

    Future medicinal chemistry

    2016  Volume 8, Issue 9, Page(s) 921–924

    Language English
    Publishing date 2016-06
    Publishing country England
    Document type Journal Article
    ISSN 1756-8927
    ISSN (online) 1756-8927
    DOI 10.4155/fmc-2016-0076
    Database MEDical Literature Analysis and Retrieval System OnLINE

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