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  1. Article ; Online: COVID-19

    TRINDADE, GUILHERME G. / CAXITO, SAMYRA M.C. / XAVIER, ALESSANDRA REJANE E.O. / XAVIER, MAURO A.S. / BRANDÃO, FABIANA

    Anais da Academia Brasileira de Ciências v.92 n.2 2020

    therapeutic approaches description and discussion

    2020  

    Abstract: Abstract Abstract: COVID-19 emerged in December 2019 in China, and since then, has disrupted global public health and changed economic paradigms. In dealing with the new Coronavirus, SARS-CoV-2, the world has not faced such extreme global fragility since ...

    Abstract Abstract Abstract: COVID-19 emerged in December 2019 in China, and since then, has disrupted global public health and changed economic paradigms. In dealing with the new Coronavirus, SARS-CoV-2, the world has not faced such extreme global fragility since the “Spanish flu” pandemic in 1918. Researchers globally are dedicating efforts to the search for an effective treatment for COVID-19. Drugs already used in a clinical setting for other pathologies have been tested as a new therapeutic approach against SARS-CoV-2, setting off a frenzy over the preliminary data of different studies. This work aims to compile and discuss the data published thus far. Despite the potential effects of some antivirals and antiparasitic against COVID-19, clinical studies must confirm real effectiveness. However, non-pharmacological approaches have proven to be the most efficient strategy to date.
    Keywords antivirals ; antiparasitic ; COVID-19 ; SARS-CoV-2 ; therapeutic approaches ; covid19
    Language English
    Publishing date 2020-01-01
    Publisher Academia Brasileira de Ciências
    Publishing country br
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: COVID-19: therapeutic approaches description and discussion.

    Trindade, Guilherme G / Caxito, Samyra M C / Xavier, Alessandra Rejane E O / Xavier, Mauro A S / BrandÃo, Fabiana

    Anais da Academia Brasileira de Ciencias

    2020  Volume 92, Issue 2, Page(s) e20200466

    Abstract: COVID-19 emerged in December 2019 in China, and since then, has disrupted global public health and changed economic paradigms. In dealing with the new Coronavirus, SARS-CoV-2, the world has not faced such extreme global fragility since the "Spanish flu" ... ...

    Abstract COVID-19 emerged in December 2019 in China, and since then, has disrupted global public health and changed economic paradigms. In dealing with the new Coronavirus, SARS-CoV-2, the world has not faced such extreme global fragility since the "Spanish flu" pandemic in 1918. Researchers globally are dedicating efforts to the search for an effective treatment for COVID-19. Drugs already used in a clinical setting for other pathologies have been tested as a new therapeutic approach against SARS-CoV-2, setting off a frenzy over the preliminary data of different studies. This work aims to compile and discuss the data published thus far. Despite the potential effects of some antivirals and antiparasitic against COVID-19, clinical studies must confirm real effectiveness. However, non-pharmacological approaches have proven to be the most efficient strategy to date.
    MeSH term(s) Anti-Bacterial Agents/administration & dosage ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Antiparasitic Agents/administration & dosage ; Antiparasitic Agents/chemistry ; Antiparasitic Agents/pharmacology ; Antiviral Agents/administration & dosage ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Betacoronavirus/drug effects ; COVID-19 ; Coronavirus Infections/drug therapy ; Humans ; Macrolides/administration & dosage ; Macrolides/chemistry ; Macrolides/pharmacology ; Pandemics ; Pneumonia, Viral/drug therapy ; SARS-CoV-2 ; Serine Proteinase Inhibitors/administration & dosage ; Serine Proteinase Inhibitors/chemistry ; Serine Proteinase Inhibitors/pharmacology
    Chemical Substances Anti-Bacterial Agents ; Antiparasitic Agents ; Antiviral Agents ; Macrolides ; Serine Proteinase Inhibitors
    Keywords covid19
    Language English
    Publishing date 2020-06-15
    Publishing country Brazil
    Document type Journal Article ; Review
    ZDB-ID 2046885-4
    ISSN 1678-2690 ; 0001-3765
    ISSN (online) 1678-2690
    ISSN 0001-3765
    DOI 10.1590/0001-3765202020200466
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: COVID-19: therapeutic approaches description and discussion

    Trindade, Guilherme G / Caxito, Samyra M C / Xavier, Alessandra Rejane E O / Xavier, Mauro A S / BrandÃo, Fabiana

    An Acad Bras Cienc

    Abstract: COVID-19 emerged in December 2019 in China, and since then, has disrupted global public health and changed economic paradigms. In dealing with the new Coronavirus, SARS-CoV-2, the world has not faced such extreme global fragility since the "Spanish flu" ... ...

    Abstract COVID-19 emerged in December 2019 in China, and since then, has disrupted global public health and changed economic paradigms. In dealing with the new Coronavirus, SARS-CoV-2, the world has not faced such extreme global fragility since the "Spanish flu" pandemic in 1918. Researchers globally are dedicating efforts to the search for an effective treatment for COVID-19. Drugs already used in a clinical setting for other pathologies have been tested as a new therapeutic approach against SARS-CoV-2, setting off a frenzy over the preliminary data of different studies. This work aims to compile and discuss the data published thus far. Despite the potential effects of some antivirals and antiparasitic against COVID-19, clinical studies must confirm real effectiveness. However, non-pharmacological approaches have proven to be the most efficient strategy to date.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #32556054
    Database COVID19

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  4. Article: A new Paracoccidioides brasiliensis 70-kDa heat shock protein reacts with sera from paracoccidioidomycosis patients.

    Bisio, Laura C / Silva, Silvana P / Pereira, Ildinete Silva / Xavier, Mauro A S / Venâncio, Emerson J / Puccia, Rosana / Soares, Célia M A / Felipe, Maria Sueli S

    Medical mycology

    2005  Volume 43, Issue 6, Page(s) 495–503

    Abstract: A cDNA coding for a new member of the 70-kDa heat shock proteins (HSP70) family from the dimorphic and pathogenic fungus, Paracoccidioides brasiliensis, was cloned and characterized. The cDNA-deduced sequence coded for 655 amino acid residues and showed ... ...

    Abstract A cDNA coding for a new member of the 70-kDa heat shock proteins (HSP70) family from the dimorphic and pathogenic fungus, Paracoccidioides brasiliensis, was cloned and characterized. The cDNA-deduced sequence coded for 655 amino acid residues and showed 95% identity to a previously described P. brasiliensis hsp70 gene. Cytoplasmic and typical nuclear localization signals, which indicate induction upon stress, were identified in the deduced peptide. The complete hsp70 cDNA coding region was cloned into a pGEX 4T-3 plasmid and expressed in Escherichia coli as a glutathione-S-transferase-tagged fusion protein. The recombinant protein reacted with a rabbit polyclonal antibody against HSP70. Western immunoblot experiments demonstrated that sera from paracoccidioidomycosis patients recognized the purified recombinant protein, suggesting an immunological role for this protein in the infectious process. The antigenicity analysis of rHSP70 detected three internal peptides that could act as activators of T-cell proliferation.
    MeSH term(s) Amino Acid Sequence ; Antibodies, Fungal/blood ; Antigens, Fungal/chemistry ; Antigens, Fungal/genetics ; Antigens, Fungal/immunology ; Base Sequence ; HSP70 Heat-Shock Proteins/chemistry ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/immunology ; Humans ; Immunoblotting ; Molecular Sequence Data ; Paracoccidioides/immunology ; Paracoccidioides/metabolism ; Paracoccidioidomycosis/blood ; Paracoccidioidomycosis/immunology ; Protein Structure, Secondary ; RNA, Fungal/chemistry ; RNA, Fungal/genetics ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Alignment ; Sequence Analysis, DNA ; Surface Properties
    Chemical Substances Antibodies, Fungal ; Antigens, Fungal ; HSP70 Heat-Shock Proteins ; RNA, Fungal ; Recombinant Proteins
    Language English
    Publishing date 2005-10-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1421796-x
    ISSN 1460-2709 ; 1369-3786
    ISSN (online) 1460-2709
    ISSN 1369-3786
    DOI 10.1080/13693780400029478
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Analysis of Bothrops jararacussu venomous gland transcriptome focusing on structural and functional aspects: I--gene expression profile of highly expressed phospholipases A2.

    Kashima, Simone / Roberto, Patrícia G / Soares, Andreimar M / Astolfi-Filho, Spartaco / Pereira, José O / Giuliati, Silvana / Faria, Milton / Xavier, Mauro A S / Fontes, Marcos R M / Giglio, José R / França, Suzelei C

    Biochimie

    2004  Volume 86, Issue 3, Page(s) 211–219

    Abstract: Snake venom glands are a rich source of bioactive molecules such as peptides, proteins and enzymes that show important pharmacological activity leading to in local and systemic effects as pain, edema, bleeding and muscle necrosis. Most studies on ... ...

    Abstract Snake venom glands are a rich source of bioactive molecules such as peptides, proteins and enzymes that show important pharmacological activity leading to in local and systemic effects as pain, edema, bleeding and muscle necrosis. Most studies on pharmacologically active peptides and proteins from snake venoms have been concerned with isolation and structure elucidation through methods of classical biochemistry. As an attempt to examine the transcripts expressed in the venom gland of Bothrops jararacussu and to unveil the toxicological and pharmacological potential of its products at the molecular level, we generated 549 expressed sequence tags (ESTs) from a directional cDNA library. Sequences obtained from single-pass sequencing of randomly selected cDNA clones could be identified by similarities searches on existing databases, resulting in 197 sequences with significant similarity to phospholipase A(2) (PLA(2)), of which 83.2% were Lys49-PLA(2) homologs (BOJU-I), 0.1% were basic Asp49-PLA(2)s (BOJU-II) and 0.6% were acidic Asp49-PLA(2)s (BOJU-III). Adjoining this very abundant class of proteins we found 88 transcripts codifying for putative sequences of metalloproteases, which after clustering and assembling resulted in three full-length sequences: BOJUMET-I, BOJUMET-II and BOJUMET-III; as well as 25 transcripts related to C-type lectin like protein including a full-length cDNA of a putative galactose binding C-type lectin and a cluster of eight serine-proteases transcripts including a full-length cDNA of a putative serine protease. Among the full-length sequenced clones we identified a nerve growth factor (Bj-NGF) with 92% identity with a human NGF (NGHUBM) and an acidic phospholipase A(2) (BthA-I-PLA(2)) displaying 85-93% identity with other snake venom toxins. Genetic distance among PLA(2)s from Bothrops species were evaluated by phylogenetic analysis. Furthermore, analysis of full-length putative Lys49-PLA(2) through molecular modeling showed conserved structural domains, allowing the characterization of those proteins as group II PLA(2)s. The constructed cDNA library provides molecular clones harboring sequences that can be used to probe directly the genetic material from gland venom of other snake species. Expression of complete cDNAs or their modified derivatives will be useful for elucidation of the structure-function relationships of these toxins and peptides of biotechnological interest.
    MeSH term(s) Amino Acid Sequence ; Animals ; Base Sequence ; Bothrops/genetics ; Expressed Sequence Tags ; Gene Expression Profiling ; Gene Library ; Lectins, C-Type/genetics ; Metalloproteases/genetics ; Metalloproteases/metabolism ; Models, Molecular ; Molecular Sequence Data ; Phospholipases A/chemistry ; Phospholipases A/genetics ; Phospholipases A/metabolism ; Phylogeny ; Protein Structure, Tertiary ; Sequence Alignment ; Serine Endopeptidases/genetics ; Serine Endopeptidases/metabolism ; Viper Venoms/chemistry ; Viper Venoms/enzymology ; Viper Venoms/genetics
    Chemical Substances Lectins, C-Type ; Viper Venoms ; Phospholipases A (EC 3.1.1.32) ; Metalloproteases (EC 3.4.-) ; Serine Endopeptidases (EC 3.4.21.-)
    Language English
    Publishing date 2004-03
    Publishing country France
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120345-9
    ISSN 0300-9084
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2004.02.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.135: Show issues Location:
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