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  1. Article ; Online: Modulating TRADD to restore cellular homeostasis and inhibit apoptosis.

    Xu, Daichao / Zhao, Heng / Jin, Minzhi / Zhu, Hong / Shan, Bing / Geng, Jiefei / Dziedzic, Slawomir A / Amin, Palak / Mifflin, Lauren / Naito, Masanori Gomi / Najafov, Ayaz / Xing, Jing / Yan, Lingjie / Liu, Jianping / Qin, Ying / Hu, Xinqian / Wang, Huibing / Zhang, Mengmeng / Manuel, Vica Jean /
    Tan, Li / He, Zhuohao / Sun, Zhenyu J / Lee, Virginia M Y / Wagner, Gerhard / Yuan, Junying

    Nature

    2020  Volume 587, Issue 7832, Page(s) 133–138

    Abstract: Cell death in human diseases is often a consequence of disrupted cellular homeostasis. If cell death is prevented without restoring cellular homeostasis, it may lead to a persistent dysfunctional and pathological state. Although mechanisms of cell death ... ...

    Abstract Cell death in human diseases is often a consequence of disrupted cellular homeostasis. If cell death is prevented without restoring cellular homeostasis, it may lead to a persistent dysfunctional and pathological state. Although mechanisms of cell death have been thoroughly investigated
    MeSH term(s) Animals ; Apoptosis/drug effects ; Autophagy/drug effects ; Baculoviral IAP Repeat-Containing 3 Protein/metabolism ; Beclin-1/chemistry ; Beclin-1/metabolism ; Bortezomib/antagonists & inhibitors ; Bortezomib/pharmacology ; Cell Line ; Homeostasis/drug effects ; Humans ; Huntingtin Protein/metabolism ; Inhibitor of Apoptosis Proteins/metabolism ; Male ; Mice ; Models, Molecular ; Neurofibrillary Tangles/metabolism ; Proteome/metabolism ; Receptor-Interacting Protein Serine-Threonine Kinases/chemistry ; Receptor-Interacting Protein Serine-Threonine Kinases/metabolism ; TNF Receptor-Associated Death Domain Protein/antagonists & inhibitors ; TNF Receptor-Associated Death Domain Protein/chemistry ; TNF Receptor-Associated Death Domain Protein/deficiency ; TNF Receptor-Associated Death Domain Protein/metabolism ; TNF Receptor-Associated Factor 2/metabolism ; Ubiquitination ; alpha-Synuclein/metabolism ; tau Proteins/metabolism
    Chemical Substances Beclin-1 ; Huntingtin Protein ; Inhibitor of Apoptosis Proteins ; Proteome ; TNF Receptor-Associated Death Domain Protein ; TNF Receptor-Associated Factor 2 ; alpha-Synuclein ; tau Proteins ; Bortezomib (69G8BD63PP) ; Baculoviral IAP Repeat-Containing 3 Protein (EC 2.3.2.27) ; Receptor-Interacting Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2020-09-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-020-2757-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Cm-p5: an antifungal hydrophilic peptide derived from the coastal mollusk Cenchritis muricatus (Gastropoda: Littorinidae).

    López-Abarrategui, Carlos / McBeth, Christine / Mandal, Santi M / Sun, Zhenyu J / Heffron, Gregory / Alba-Menéndez, Annia / Migliolo, Ludovico / Reyes-Acosta, Osvaldo / García-Villarino, Mónica / Nolasco, Diego O / Falcão, Rosana / Cherobim, Mariana D / Dias, Simoni C / Brandt, Wolfgang / Wessjohann, Ludger / Starnbach, Michael / Franco, Octavio L / Otero-González, Anselmo J

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2015  Volume 29, Issue 8, Page(s) 3315–3325

    Abstract: Antimicrobial peptides form part of the first line of defense against pathogens for many organisms. Current treatments for fungal infections are limited by drug toxicity and pathogen resistance. Cm-p5 (SRSELIVHQRLF), a peptide derived from the marine ... ...

    Abstract Antimicrobial peptides form part of the first line of defense against pathogens for many organisms. Current treatments for fungal infections are limited by drug toxicity and pathogen resistance. Cm-p5 (SRSELIVHQRLF), a peptide derived from the marine mollusk Cenchritis muricatus peptide Cm-p1, has a significantly increased fungistatic activity against pathogenic Candida albicans (minimal inhibitory concentration, 10 µg/ml; EC50, 1.146 µg/ml) while exhibiting low toxic effects against a cultured mammalian cell line. Cm-p5 as characterized by circular dichroism and nuclear magnetic resonance revealed an α-helical structure in membrane-mimetic conditions and a tendency to random coil folding in aqueous solutions. Additional studies modeling Cm-p5 binding to a phosphatidylserine bilayer in silico and isothermal titration calorimetry using lipid monophases demonstrated that Cm-p5 has a high affinity for the phospholipids of fungal membranes (phosphatidylserine and phosphatidylethanolamine), only moderate interactions with a mammalian membrane phospholipid, low interaction with ergosterol, and no interaction with chitin. Adhesion of Cm-p5 to living C. albicans cells was confirmed by fluorescence microscopy with FITC-labeled peptide. In a systemic candidiasis model in mice, intraperitoneal administration of Cm-p5 was unable to control the fungal kidney burden, although its low amphiphaticity could be modified to generate new derivatives with improved fungicidal activity and stability.
    MeSH term(s) Animals ; Antifungal Agents/pharmacology ; Candida albicans/drug effects ; Candidiasis/drug therapy ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Circular Dichroism/methods ; Female ; Gastropoda/metabolism ; Hydrophobic and Hydrophilic Interactions ; Mice ; Mice, Inbred BALB C ; Microbial Sensitivity Tests/methods ; Mollusca/metabolism ; Peptides/pharmacology ; Phosphatidylethanolamines/metabolism ; Phosphatidylserines/metabolism ; Phospholipids/metabolism ; Protein Structure, Secondary
    Chemical Substances Antifungal Agents ; Peptides ; Phosphatidylethanolamines ; Phosphatidylserines ; Phospholipids ; phosphatidylethanolamine (39382-08-6)
    Language English
    Publishing date 2015-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.14-269860
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2266: Show issues Location:
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