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  1. AU="O'Brien, Henrik"
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  1. Article ; Online: The promise of copper ionophores as antimicrobials.

    O'Brien, Henrik / Davoodian, Talish / Johnson, Michael D L

    Current opinion in microbiology

    2023  Volume 75, Page(s) 102355

    Abstract: Antibiotic-resistant microbe-mediated deaths are a major worldwide health issue. Unfortunately, due to microbial adaptation to develop resistance, some antibiotics are nullified early in their usage, and worse, resistance is detected before they can even ...

    Abstract Antibiotic-resistant microbe-mediated deaths are a major worldwide health issue. Unfortunately, due to microbial adaptation to develop resistance, some antibiotics are nullified early in their usage, and worse, resistance is detected before they can even be prescribed. Copper's toxicity since antiquity against microbes at the host-pathogen interface offers a fascinating weapon to fight antimicrobial resistance. Here, we briefly review why copper is so effective, how drugs that work with copper are effective antimicrobials, and how compounds such as these could reinvigorate investment in antimicrobial development.
    MeSH term(s) Copper/pharmacology ; Ionophores ; Drug Resistance, Bacterial ; Anti-Infective Agents/pharmacology ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use
    Chemical Substances Copper (789U1901C5) ; Ionophores ; Anti-Infective Agents ; Anti-Bacterial Agents
    Language English
    Publishing date 2023-07-03
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 1418474-6
    ISSN 1879-0364 ; 1369-5274
    ISSN (online) 1879-0364
    ISSN 1369-5274
    DOI 10.1016/j.mib.2023.102355
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5514: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 51: Show issues

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  2. Article: Novel dithiocarbamate derivatives are effective copper-dependent antimicrobials against

    Menghani, Sanjay V / Sanchez-Rosario, Yamil / Pok, Chansorena / Liu, Renshuai / Gao, Feng / O'Brien, Henrik / Neubert, Miranda J / Ochoa, Klariza / Durckel, Meredythe / Hellinger, Riley D / Hackett, Nadia / Wang, Wei / Johnson, Michael D L

    Frontiers in microbiology

    2023  Volume 13, Page(s) 1099330

    Abstract: Despite the availability of several vaccines against multiple disease-causing strains ... ...

    Abstract Despite the availability of several vaccines against multiple disease-causing strains of
    Language English
    Publishing date 2023-01-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2022.1099330
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Identification of sodium channel toxins from marine cone snails of the subgenera Textilia and Afonsoconus.

    McMahon, Kirsten L / O'Brien, Henrik / Schroeder, Christina I / Deuis, Jennifer R / Venkatachalam, Dhananjeyan / Huang, Di / Green, Brad R / Bandyopadhyay, Pradip K / Li, Qing / Yandell, Mark / Safavi-Hemami, Helena / Olivera, Baldomero M / Vetter, Irina / Robinson, Samuel D

    Cellular and molecular life sciences : CMLS

    2023  Volume 80, Issue 10, Page(s) 287

    Abstract: Voltage-gated sodium ( ... ...

    Abstract Voltage-gated sodium (Na
    MeSH term(s) Humans ; Animals ; Conus Snail ; Conotoxins/pharmacology ; Toxins, Biological ; Membrane Proteins ; Sodium Channels/genetics
    Chemical Substances Conotoxins ; Toxins, Biological ; Membrane Proteins ; Sodium Channels
    Language English
    Publishing date 2023-09-09
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-023-04935-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 195: 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)

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  4. Article ; Online: Rules of Expansion: an Updated Consensus Operator Site for the CopR-CopY Family of Bacterial Copper Exporter System Repressors.

    O'Brien, Henrik / Alvin, Joseph W / Menghani, Sanjay V / Sanchez-Rosario, Yamil / Van Doorslaer, Koenraad / Johnson, Michael D L

    mSphere

    2020  Volume 5, Issue 3

    Abstract: Copper is broadly toxic to bacteria. As such, bacteria have evolved specialized copper export systems ( ...

    Abstract Copper is broadly toxic to bacteria. As such, bacteria have evolved specialized copper export systems (
    MeSH term(s) Bacteria/genetics ; Bacterial Proteins/genetics ; Copper/metabolism ; DNA-Binding Proteins ; Gene Expression Regulation, Bacterial ; Operon ; Repressor Proteins/genetics ; Sequence Alignment ; Streptococcus pneumoniae/genetics ; Trans-Activators/genetics
    Chemical Substances Bacterial Proteins ; DNA-Binding Proteins ; Repressor Proteins ; Trans-Activators ; Copper (789U1901C5)
    Language English
    Publishing date 2020-05-27
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2379-5042
    ISSN (online) 2379-5042
    DOI 10.1128/mSphere.00411-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: αM-Conotoxin MIIIJ Blocks Nicotinic Acetylcholine Receptors at Neuromuscular Junctions of Frog and Fish.

    Rybin, Matthew J / O'Brien, Henrik / Ramiro, Iris Bea L / Azam, Layla / McIntosh, J Michael / Olivera, Baldomero M / Safavi-Hemami, Helena / Yoshikami, Doju

    Toxins

    2020  Volume 12, Issue 3

    Abstract: We report the discovery and functional characterization of αM-Conotoxin MIIIJ, a peptide from the venom of the fish-hunting cone ... ...

    Abstract We report the discovery and functional characterization of αM-Conotoxin MIIIJ, a peptide from the venom of the fish-hunting cone snail
    MeSH term(s) Action Potentials/drug effects ; Amino Acid Sequence ; Animals ; Conotoxins/chemistry ; Conotoxins/pharmacology ; Dose-Response Relationship, Drug ; Excitatory Postsynaptic Potentials/drug effects ; Goldfish ; Mice ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/metabolism ; Neuromuscular Junction/drug effects ; Neuromuscular Junction/metabolism ; Nicotinic Antagonists/chemistry ; Nicotinic Antagonists/pharmacology ; Paresis/chemically induced ; Predatory Behavior/drug effects ; Protein Binding ; Receptors, Nicotinic/metabolism ; Sequence Alignment ; Species Specificity ; Xenopus laevis
    Chemical Substances Conotoxins ; Nicotinic Antagonists ; Receptors, Nicotinic
    Language English
    Publishing date 2020-03-21
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518395-3
    ISSN 2072-6651 ; 2072-6651
    ISSN (online) 2072-6651
    ISSN 2072-6651
    DOI 10.3390/toxins12030197
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Ero1-Mediated Reoxidation of Protein Disulfide Isomerase Accelerates the Folding of Cone Snail Toxins.

    O'Brien, Henrik / Kanemura, Shingo / Okumura, Masaki / Baskin, Robert P / Bandyopadhyay, Pradip K / Olivera, Baldomero M / Ellgaard, Lars / Inaba, Kenji / Safavi-Hemami, Helena

    International journal of molecular sciences

    2018  Volume 19, Issue 11

    Abstract: Disulfide-rich peptides are highly abundant in nature and their study has provided fascinating insight into protein folding, structure and function. Venomous cone snails belong to a group of organisms that express one of the largest sets of disulfide- ... ...

    Abstract Disulfide-rich peptides are highly abundant in nature and their study has provided fascinating insight into protein folding, structure and function. Venomous cone snails belong to a group of organisms that express one of the largest sets of disulfide-rich peptides (conotoxins) found in nature. The diversity of structural scaffolds found for conotoxins suggests that specialized molecular adaptations have evolved to ensure their efficient folding and secretion. We recently showed that canonical protein disulfide isomerase (PDI) and a conotoxin-specific PDI (csPDI) are ubiquitously expressed in the venom gland of cone snails and play a major role in conotoxin folding. Here, we identify cone snail endoplasmic reticulum oxidoreductin-1 (
    MeSH term(s) Animals ; Conotoxins/chemistry ; Conus Snail/chemistry ; Oxidation-Reduction ; Oxidoreductases/chemistry ; Protein Disulfide-Isomerases/chemistry ; Protein Folding
    Chemical Substances Conotoxins ; Oxidoreductases (EC 1.-) ; Protein Disulfide-Isomerases (EC 5.3.4.1)
    Language English
    Publishing date 2018-10-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms19113418
    Database MEDical Literature Analysis and Retrieval System OnLINE

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