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  1. AU="de Oliveira, Guilherme Xavier Lyra Malcher" AU="de Oliveira, Guilherme Xavier Lyra Malcher"
  2. AU="Afaneh, Hasheemah"
  3. AU="Galicia-Hernández, Victoria"
  4. AU="Daniel A. Haber"
  5. AU=Bu Fangfang
  6. AU="Fox, Kevin J"
  7. AU="Nawazish Naqvi"
  8. AU="Marquardt, Viktoria"
  9. AU="Watts, Robyn"
  10. AU="Caballero, Susana J"
  11. AU="van Dijk, J Hessel M"
  12. AU=Della Guardia Lucio
  13. AU="Zhilich V.N."
  14. AU="George, Darren"
  15. AU=Lin Xiukun
  16. AU="Kanwal Gujral"
  17. AU="Christian Young"
  18. AU=Takeuchi Kaoru
  19. AU="Wiślicki, W."
  20. AU="Veiga, Susana"
  21. AU="Reynolds, Matthew W."
  22. AU="Oates, Stephen B"
  23. AU=Okubo K
  24. AU="Behnood, Sanaz"

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  1. Artikel ; Online: Physiological relevance of ACOT8-Nef interaction in HIV infection.

    Palmeira, Julys da Fonseca / Argañaraz, Gustavo A / de Oliveira, Guilherme Xavier Lyra Malcher / Argañaraz, Enrique R

    Reviews in medical virology

    2019  Band 29, Heft 5, Seite(n) e2057

    Abstract: During human immunodeficiency virus (HIV) infection, Nef viral protein plays a crucial role in viral pathogenesis and progression of acquired immunodeficiency syndrome. Nef is expressed in the early stages of infection and alters the cellular environment ...

    Abstract During human immunodeficiency virus (HIV) infection, Nef viral protein plays a crucial role in viral pathogenesis and progression of acquired immunodeficiency syndrome. Nef is expressed in the early stages of infection and alters the cellular environment increasing infectivity, viral replication, and the evasion of host immune response through several mechanisms. Nef has numerous functional domains that allow it to interact with a number of proteins, interfering with intracellular traffic. Among these proteins, human peroxisomal thioesterase 8, ACOT8, has been shown to be an important cellular partner of Nef. It has been suggested that this interaction may be involved in Nef-dependent endocytosis and also in the modulation of lipid composition in membrane rafts. However, the actual role of this interaction, as well as the mechanisms involved, has not yet been fully elucidated. In this review, we focused on the interplay between Nef and ACOT8 proteins, highlighting the possible physiological relevance in HIV infection.
    Mesh-Begriff(e) Biomarkers ; HIV Infections/metabolism ; HIV Infections/virology ; HIV-1/physiology ; Host-Pathogen Interactions ; Humans ; Palmitoyl-CoA Hydrolase/metabolism ; Protein Binding ; nef Gene Products, Human Immunodeficiency Virus/metabolism
    Chemische Substanzen Biomarkers ; nef Gene Products, Human Immunodeficiency Virus ; ACOT8 protein, human (EC 3.1.2.2) ; Palmitoyl-CoA Hydrolase (EC 3.1.2.2)
    Sprache Englisch
    Erscheinungsdatum 2019-06-09
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1086043-5
    ISSN 1099-1654 ; 1052-9276
    ISSN (online) 1099-1654
    ISSN 1052-9276
    DOI 10.1002/rmv.2057
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

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    Verfügbar in ZB MED Köln/Königswinter

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  2. Artikel ; Online: Alpha-1-antitrypsin: A possible host protective factor against Covid-19.

    de Loyola, Mariana Braccialli / Dos Reis, Thaís Tereza Aguiar / de Oliveira, Guilherme Xavier Lyra Malcher / da Fonseca Palmeira, Julys / Argañaraz, Gustavo A / Argañaraz, Enrique R

    Reviews in medical virology

    2020  Band 31, Heft 2, Seite(n) e2157

    Abstract: Understanding Covid-19 pathophysiology is crucial for a better understanding of the disease and development of more effective treatments. Alpha-1-antitrypsin (A1AT) is a constitutive tissue protector with antiviral and anti-inflammatory properties. A1AT ... ...

    Abstract Understanding Covid-19 pathophysiology is crucial for a better understanding of the disease and development of more effective treatments. Alpha-1-antitrypsin (A1AT) is a constitutive tissue protector with antiviral and anti-inflammatory properties. A1AT inhibits SARS-CoV-2 infection and two of the most important proteases in the pathophysiology of Covid-19: the transmembrane serine protease 2 (TMPRSS2) and the disintegrin and metalloproteinase 17 (ADAM17). It also inhibits the activity of inflammatory molecules, such as IL-8, TNF-α, and neutrophil elastase (NE). TMPRSS2 is essential for SARS-CoV-2-S protein priming and viral infection. ADAM17 mediates ACE2, IL-6R, and TNF-α shedding. ACE2 is the SARS-CoV-2 entry receptor and a key component for the balance of the renin-angiotensin system, inflammation, vascular permeability, and pulmonary homeostasis. In addition, clinical findings indicate that A1AT levels might be important in defining Covid-19 outcomes, potentially partially explaining associations with air pollution and with diabetes. In this review, we focused on the interplay between A1AT with TMPRSS2, ADAM17 and immune molecules, and the role of A1AT in the pathophysiology of Covid-19, opening new avenues for investigating effective treatments.
    Mesh-Begriff(e) ADAM17 Protein/metabolism ; Animals ; COVID-19/metabolism ; Humans ; Protective Factors ; Serine Endopeptidases/metabolism ; alpha 1-Antitrypsin/metabolism
    Chemische Substanzen alpha 1-Antitrypsin ; Serine Endopeptidases (EC 3.4.21.-) ; ADAM17 Protein (EC 3.4.24.86)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-08-26
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1086043-5
    ISSN 1099-1654 ; 1052-9276
    ISSN (online) 1099-1654
    ISSN 1052-9276
    DOI 10.1002/rmv.2157
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 3308: Hefte anzeigen Standort:
    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)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  3. Artikel: Alpha-1-antitrypsin: A possible host protective factor against Covid-19

    de Loyola, Mariana Braccialli / Dos Reis, Thaís Tereza Aguiar / de Oliveira, Guilherme Xavier Lyra Malcher / da Fonseca Palmeira, Julys / Argañaraz, Gustavo A / Argañaraz, Enrique R

    Rev Med Virol

    Abstract: Understanding Covid-19 pathophysiology is crucial for a better understanding of the disease and development of more effective treatments. Alpha-1-antitrypsin (A1AT) is a constitutive tissue protector with antiviral and anti-inflammatory properties. A1AT ... ...

    Abstract Understanding Covid-19 pathophysiology is crucial for a better understanding of the disease and development of more effective treatments. Alpha-1-antitrypsin (A1AT) is a constitutive tissue protector with antiviral and anti-inflammatory properties. A1AT inhibits SARS-CoV-2 infection and two of the most important proteases in the pathophysiology of Covid-19: the transmembrane serine protease 2 (TMPRSS2) and the disintegrin and metalloproteinase 17 (ADAM17). It also inhibits the activity of inflammatory molecules, such as IL-8, TNF-α, and neutrophil elastase (NE). TMPRSS2 is essential for SARS-CoV-2-S protein priming and viral infection. ADAM17 mediates ACE2, IL-6R, and TNF-α shedding. ACE2 is the SARS-CoV-2 entry receptor and a key component for the balance of the renin-angiotensin system, inflammation, vascular permeability, and pulmonary homeostasis. In addition, clinical findings indicate that A1AT levels might be important in defining Covid-19 outcomes, potentially partially explaining associations with air pollution and with diabetes. In this review, we focused on the interplay between A1AT with TMPRSS2, ADAM17 and immune molecules, and the role of A1AT in the pathophysiology of Covid-19, opening new avenues for investigating effective treatments.
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #731139
    Datenquelle COVID19

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