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  1. Book ; Online: Unheimliche Inskriptionen : Eine Studie zu Körperbildern im postklassischen Horrorfilm

    Shelton, Catherine

    2008  

    Keywords Films, cinema ; Horrorfilm ; Körper ; Tod ; Krankheit ; Monstrum ; Film ; Medienwissenschaft ; Body ; Media Studies
    Size 1 electronic resource (384 pages)
    Publisher transcript Verlag
    Publishing place Bielefeld
    Document type Book ; Online
    Note German ; Open Access
    HBZ-ID HT021030873
    ISBN 9783899428339 ; 3899428331
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Gut Epithelial Metabolism as a Key Driver of Intestinal Dysbiosis Associated with Noncommunicable Diseases.

    Shelton, Catherine D / Byndloss, Mariana X

    Infection and immunity

    2020  Volume 88, Issue 7

    Abstract: In high-income countries, the leading causes of death are noncommunicable diseases (NCDs), such as obesity, cancer, and cardiovascular disease. An important feature of most NCDs is inflammation-induced gut dysbiosis characterized by a shift in the ... ...

    Abstract In high-income countries, the leading causes of death are noncommunicable diseases (NCDs), such as obesity, cancer, and cardiovascular disease. An important feature of most NCDs is inflammation-induced gut dysbiosis characterized by a shift in the microbial community structure from obligate to facultative anaerobes such as
    MeSH term(s) Animals ; Colon/metabolism ; Colon/microbiology ; Disease Susceptibility ; Dysbiosis ; Energy Metabolism ; Enterobacteriaceae/metabolism ; Gastrointestinal Microbiome ; Humans ; Intestinal Mucosa/metabolism ; Intestinal Mucosa/microbiology ; Noncommunicable Diseases/epidemiology ; Obesity/complications ; Obesity/metabolism ; Oxidation-Reduction ; Risk Assessment ; Risk Factors
    Language English
    Publishing date 2020-06-22
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/IAI.00939-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Unraveling the Structure and Mechanism of the MST(ery) Enzymes.

    Shelton, Catherine L / Lamb, Audrey L

    Trends in biochemical sciences

    2018  Volume 43, Issue 5, Page(s) 342–357

    Abstract: The menaquinone, siderophore, and tryptophan (MST) enzymes transform chorismate to generate precursor molecules for the biosynthetic pathways defined in their name. Kinetic data, both steady-state and transient-state, and X-ray crystal structures ... ...

    Abstract The menaquinone, siderophore, and tryptophan (MST) enzymes transform chorismate to generate precursor molecules for the biosynthetic pathways defined in their name. Kinetic data, both steady-state and transient-state, and X-ray crystal structures indicate that these enzymes are highly conserved both in mechanism and in structure. Because these enzymes are found in pathogens but not in humans, there is considerable interest in these enzymes as drug design targets. While great progress has been made in defining enzyme structure and mechanism, inhibitor design has lagged behind. This review provides a detailed description of the evidence that begins to unravel the mystery of how the MST enzymes work, and how that information has been used in inhibitor design.
    MeSH term(s) Humans ; Kinetics ; Lyases/chemistry ; Lyases/metabolism ; Models, Molecular ; Siderophores/chemistry ; Siderophores/metabolism ; Tryptophan/chemistry ; Tryptophan/metabolism ; Vitamin K 2/chemistry ; Vitamin K 2/metabolism
    Chemical Substances Siderophores ; Vitamin K 2 (11032-49-8) ; Tryptophan (8DUH1N11BX) ; Lyases (EC 4.-)
    Language English
    Publishing date 2018-03-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2018.02.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Correction for Shelton et al., "Deletion of Rv2571c Confers Resistance to Arylamide Compounds in Mycobacterium tuberculosis".

    Shelton, Catherine D / McNeil, Matthew B / Early, Julie V / Ioerger, Thomas R / Parish, Tanya

    Antimicrobial agents and chemotherapy

    2022  Volume 66, Issue 8, Page(s) e0096222

    Language English
    Publishing date 2022-07-25
    Publishing country United States
    Document type Journal Article ; Published Erratum
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/aac.00962-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Deletion of Rv2571c confers resistance to arylamide compounds in

    Shelton, Catherine D / McNeil, Matthew B / Early, Julie V / Ioerger, Thomas R / Parish, Tanya

    Antimicrobial agents and chemotherapy

    2021  Volume 65, Issue 5

    Abstract: Tuberculosis, caused ... ...

    Abstract Tuberculosis, caused by
    Language English
    Publishing date 2021-02-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/AAC.02334-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD.

    Shelton, Catherine L / Meneely, Kathleen M / Ronnebaum, Trey A / Chilton, Annemarie S / Riley, Andrew P / Prisinzano, Thomas E / Lamb, Audrey L

    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

    2022  Volume 27, Issue 6, Page(s) 541–551

    Abstract: Pseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide ... ...

    Abstract Pseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11 Å when co-crystallized with the adenylation inhibitor 5'-O-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69 Å with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from Acinetobacter baumannii.
    MeSH term(s) Anti-Bacterial Agents/metabolism ; Anti-Bacterial Agents/pharmacology ; Phenols ; Pseudomonas aeruginosa/metabolism ; Salicylates/metabolism ; Siderophores/chemistry ; Thiazoles
    Chemical Substances Anti-Bacterial Agents ; Phenols ; Salicylates ; Siderophores ; Thiazoles ; pyochelin (69772-54-9)
    Language English
    Publishing date 2022-05-05
    Publishing country Germany
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1464026-0
    ISSN 1432-1327 ; 0949-8257
    ISSN (online) 1432-1327
    ISSN 0949-8257
    DOI 10.1007/s00775-022-01941-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Triazolopyrimidines Target Aerobic Respiration in Mycobacterium tuberculosis.

    Shelton, Catherine / McNeil, Matthew / Allen, Renee / Flint, Lindsay / Russell, Dara / Berube, Bryan / Korkegian, Aaron / Ovechkina, Yulia / Parish, Tanya

    Antimicrobial agents and chemotherapy

    2022  Volume 66, Issue 4, Page(s) e0204121

    Abstract: We previously identified a series of triazolopyrimidines with antitubercular activity. We determined that Mycobacterium tuberculosis strains with mutations in QcrB, a subunit of the ... ...

    Abstract We previously identified a series of triazolopyrimidines with antitubercular activity. We determined that Mycobacterium tuberculosis strains with mutations in QcrB, a subunit of the cytochrome
    MeSH term(s) Antitubercular Agents/pharmacology ; Cytochromes ; Electron Transport Complex IV/genetics ; Electron Transport Complex IV/metabolism ; Humans ; Mycobacterium tuberculosis/genetics ; Mycobacterium tuberculosis/metabolism ; Respiration
    Chemical Substances Antitubercular Agents ; Cytochromes ; Electron Transport Complex IV (EC 1.9.3.1)
    Language English
    Publishing date 2022-03-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/aac.02041-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Functional consequences of B-repeat sequence variation in the staphylococcal biofilm protein Aap: deciphering the assembly code.

    Shelton, Catherine L / Conrady, Deborah G / Herr, Andrew B

    The Biochemical journal

    2016  Volume 474, Issue 3, Page(s) 427–443

    Abstract: Staphylococcus epidermidis is an opportunistic pathogen that can form robust biofilms that render the bacteria resistant to antibiotic action and immune responses. Intercellular adhesion in S. epidermidis biofilms is mediated by the cell wall-associated ... ...

    Abstract Staphylococcus epidermidis is an opportunistic pathogen that can form robust biofilms that render the bacteria resistant to antibiotic action and immune responses. Intercellular adhesion in S. epidermidis biofilms is mediated by the cell wall-associated accumulation-associated protein (Aap), via zinc-mediated self-assembly of its B-repeat region. This region contains up to 17 nearly identical sequence repeats, with each repeat assumed to be functionally equivalent. However, Aap B-repeats exist as two subtypes, defined by a cluster of consensus or variant amino acids. These variable residues are positioned near the zinc-binding (and dimerization) site and the stability determinant for the B-repeat fold. We have characterized four B-repeat constructs to assess the functional relevance of the two Aap B-repeat subtypes. Analytical ultracentrifugation experiments demonstrated that constructs with the variant sequence show reduced or absent Zn
    MeSH term(s) Amino Acid Sequence ; Bacterial Adhesion/physiology ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Biofilms/growth & development ; Cloning, Molecular ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Variation ; Kinetics ; Models, Molecular ; Protein Binding ; Protein Denaturation ; Protein Folding ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Stability ; Protein Structure, Secondary ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Staphylococcus epidermidis/physiology ; Static Electricity ; Zinc/chemistry ; Zinc/metabolism
    Chemical Substances Bacterial Proteins ; Recombinant Proteins ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2016-11-21
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20160675
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Book ; Thesis: Unheimliche Inskriptionen

    Shelton, Catherine

    eine Studie zu Körperbildern im postklassischen Horrorfilm

    (Film)

    2008  

    Author's details Catherine Shelton
    Series title Film
    Keywords Körper ; Horrorfilm
    Language German
    Size 380 S.
    Publisher Transcript-Verl
    Publishing place Bielefeld
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Univ., Diss.--Köln
    ISBN 3899428331 ; 9783899428339
    Database Former special subject collection: coastal and deep sea fishing

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  10. Book ; Online: Unheimliche Inskriptionen

    Shelton, Catherine

    Eine Studie zu Körperbildern im postklassischen Horrorfilm

    (Film)

    2008  

    Abstract: Der Horrorfilm lässt Erscheinungsformen des Körpers sichtbar werden, die in übrigen Diskursen meist ausgeschlossen oder verworfen werden. Diese genrespezifischen Strategien der Visualisierung zeigen ein »Unzeigbares«, das nicht nur zum abweichenden ... ...

    Author's details Catherine Shelton
    Series title Film
    Abstract Der Horrorfilm lässt Erscheinungsformen des Körpers sichtbar werden, die in übrigen Diskursen meist ausgeschlossen oder verworfen werden. Diese genrespezifischen Strategien der Visualisierung zeigen ein »Unzeigbares«, das nicht nur zum abweichenden Gegenbild des Körpers, sondern auch zum Faszinosum und Spektakel erhoben wird. Die Studie deutet diese Körperbilder vor dem Hintergrund kultureller Konzeptionen des Körperlichen und erschließt die heterogenen und historischen Dimensionen, die sich in ihnen einzeichnen. Im Zentrum stehen dabei die Themenfelder Monstrosität, phantastische Krankheit und Tod
    Keywords Horror films/History ; Motion pictures/Plots, themes, etc
    Language German
    Size Online-Ressource (384 pages), illustrations
    Edition 1. Aufl
    Publisher transcript Verlag
    Publishing place Bielefeld
    Document type Book ; Online
    Note In German ; open access
    ISBN 9783839408339 ; 3839408334
    DOI 10.14361/9783839408339
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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