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  1. Artikel ; Online: Structural Insights into SARS-CoV-2 Nonstructural Protein 1 Interaction with Human Cyclophilin and FKBP1 to Regulate Interferon Production.

    Vankadari, Naveen / Ghosal, Debnath

    The journal of physical chemistry letters

    2024  Band 15, Heft 4, Seite(n) 919–924

    Abstract: The ongoing coronavirus disease 2019 (COVID-19) pandemic caused by the SARS-CoV-2 coronavirus and the perpetual rise of new variants warrant investigation of the molecular and structural details of the infection process and modulation of the host defense ...

    Abstract The ongoing coronavirus disease 2019 (COVID-19) pandemic caused by the SARS-CoV-2 coronavirus and the perpetual rise of new variants warrant investigation of the molecular and structural details of the infection process and modulation of the host defense by viral proteins. This Letter reports the combined experimental and computational approaches to provide key insights into the structural and functional basis of Nsp1's association with different cyclophilins and FKBPs in regulating COVID-19 infection. We demonstrated the real-time stability and functional dynamics of the Nsp1-CypA/FKBP1A complex and investigated the repurposing of potential inhibitors that could block these interactions. Overall, we provided insights into the inhibitory role Nsp1 in downstream interferon production, a key aspect for host defense that prevents the SARS-CoV-2 or related family of corona virus infection.
    Mesh-Begriff(e) Humans ; SARS-CoV-2/metabolism ; COVID-19 ; Cyclophilins ; Viral Nonstructural Proteins/metabolism ; Interferons
    Chemische Substanzen Cyclophilins (EC 5.2.1.-) ; Viral Nonstructural Proteins ; Interferons (9008-11-1)
    Sprache Englisch
    Erscheinungsdatum 2024-01-19
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1948-7185
    ISSN (online) 1948-7185
    DOI 10.1021/acs.jpclett.3c02959
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Structure of Furin Protease Binding to SARS-CoV-2 Spike Glycoprotein and Implications for Potential Targets and Virulence.

    Vankadari, Naveen

    The journal of physical chemistry letters

    2020  Band 11, Heft 16, Seite(n) 6655–6663

    Abstract: The COVID-19 pandemic is an urgent global health emergency, and the presence of Furin site in the SARS-CoV-2 spike glycoprotein alters virulence and warrants further molecular, structural, and biophysical studies. Here we report the structure of Furin in ...

    Abstract The COVID-19 pandemic is an urgent global health emergency, and the presence of Furin site in the SARS-CoV-2 spike glycoprotein alters virulence and warrants further molecular, structural, and biophysical studies. Here we report the structure of Furin in complex with SARS-CoV-2 spike glycoprotein, demonstrating how Furin binds to the S1/S2 region of spike glycoprotein and eventually cleaves the viral protein using experimental functional studies, molecular dynamics, and docking. The structural studies underline the mechanism and mode of action of Furin, which is a key process in host cell entry and a hallmark of enhanced virulence. Our whole-exome sequencing analysis shows the genetic variants/alleles in Furin were found to alter the binding affinity for viral spike glycoprotein and could vary in infectivity in humans. Unravelling the mechanisms of Furin action, binding dynamics, and the genetic variants opens the growing arena of bona fide antibodies and development of potential therapeutics targeting the blockage of Furin cleavage.
    Mesh-Begriff(e) Amino Acid Sequence ; Animals ; Betacoronavirus/chemistry ; Betacoronavirus/pathogenicity ; CHO Cells ; Catalytic Domain ; Cricetulus ; Furin/chemistry ; Furin/genetics ; Furin/metabolism ; Gene Expression/physiology ; Hexosamines/metabolism ; Humans ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Binding ; Proteolysis ; SARS-CoV-2 ; Serine Proteinase Inhibitors/metabolism ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism ; Virulence/physiology
    Chemische Substanzen 2,5-dideoxystreptamine ; Hexosamines ; Serine Proteinase Inhibitors ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; FURIN protein, human (EC 3.4.21.75) ; Furin (EC 3.4.21.75)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-08-05
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 1948-7185
    ISSN (online) 1948-7185
    DOI 10.1021/acs.jpclett.0c01698
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Overwhelming mutations or SNPs of SARS-CoV-2: A point of caution.

    Vankadari, Naveen

    Gene

    2020  Band 752, Seite(n) 144792

    Abstract: The morbidity of SARS-CoV-2 (COVID-19) is reaching 3 Million landmark causing and a serious public health concern globally and it is enigmatic how several antiviral and antibody treatments were not effective in the different period across the globe. With ...

    Abstract The morbidity of SARS-CoV-2 (COVID-19) is reaching 3 Million landmark causing and a serious public health concern globally and it is enigmatic how several antiviral and antibody treatments were not effective in the different period across the globe. With the drastic increasing number of positive cases around the world WHO raised the importance in the assessment of the risk of spread and understanding genetic modifications that could have occurred in the SARS-CoV-2. Using all available deep sequencing data of complete genome from all over the world (NCBI repository), we identified several hundreds of point mutations or SNPs in SARS-CoV-2 all across the genome. This could be the cause for the constant change and differed virulence with an increase in mortality and morbidity. Among the 12 different countries (one sequence from each country) with complete genome sequencing data, we noted the 47 key point mutations or SNPs located along the entire genome that might have impact in the virulence and response to different antivirals against SARS-CoV-2. In this regard, key viral proteins of spike glycoprotein, Nsp1, RdRp and the ORF8 region got heavily mutated within these 3 months via person-to-person passage. We also discuss what could be the possible cause of this rapid mutation in the SARS-CoV-2.
    Mesh-Begriff(e) Americas/epidemiology ; Asia/epidemiology ; Betacoronavirus/genetics ; COVID-19 ; Coronavirus Infections/epidemiology ; Coronavirus Infections/virology ; Drug Resistance, Viral ; Europe/epidemiology ; Genome, Viral ; Humans ; Pandemics ; Phylogeny ; Pneumonia, Viral/epidemiology ; Pneumonia, Viral/virology ; Point Mutation ; Polymorphism, Single Nucleotide ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/genetics ; Viral Proteins/classification ; Viral Proteins/genetics
    Chemische Substanzen Spike Glycoprotein, Coronavirus ; Viral Proteins ; spike protein, SARS-CoV-2
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-05-20
    Erscheinungsland Netherlands
    Dokumenttyp Letter
    ZDB-ID 391792-7
    ISSN 1879-0038 ; 0378-1119
    ISSN (online) 1879-0038
    ISSN 0378-1119
    DOI 10.1016/j.gene.2020.144792
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Arbidol: A potential antiviral drug for the treatment of SARS-CoV-2 by blocking trimerization of the spike glycoprotein.

    Vankadari, Naveen

    International journal of antimicrobial agents

    2020  Band 56, Heft 2, Seite(n) 105998

    Abstract: The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) pandemic is a global public health emergency, and new therapeutics are needed. This article reports the potential drug target and mechanism of action of Arbidol (umifenovir) to treat ... ...

    Abstract The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) pandemic is a global public health emergency, and new therapeutics are needed. This article reports the potential drug target and mechanism of action of Arbidol (umifenovir) to treat coronavirus disease 2019 (COVID-19). Molecular dynamics and structural analysis were used to show how Arbidol targets the SARS-CoV-2 spike glycoprotein and impedes its trimerization, which is key for host cell adhesion and hijacking, indicating the potential of Arbidol to treat COVID-19. It is hoped that knowledge of the potential drug target and mechanism of action of Arbidol will help in the development of new therapeutics for SARS-CoV-2.
    Mesh-Begriff(e) Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Betacoronavirus/drug effects ; Betacoronavirus/isolation & purification ; Biopolymers/chemistry ; COVID-19 ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Humans ; Indoles/chemistry ; Indoles/pharmacology ; Pandemics ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/virology ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/antagonists & inhibitors
    Chemische Substanzen Antiviral Agents ; Biopolymers ; Indoles ; Spike Glycoprotein, Coronavirus ; umifenovir (93M09WW4RU)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-04-28
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 1093977-5
    ISSN 1872-7913 ; 0924-8579
    ISSN (online) 1872-7913
    ISSN 0924-8579
    DOI 10.1016/j.ijantimicag.2020.105998
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 3368: Hefte anzeigen Standort:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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  5. Artikel ; Online: Structure of Furin Protease Binding to SARS-CoV-2 Spike Glycoprotein and Implications for Potential Targets and Virulence

    Vankadari, Naveen

    The Journal of Physical Chemistry Letters

    2020  Band 11, Heft 16, Seite(n) 6655–6663

    Schlagwörter General Materials Science ; covid19
    Sprache Englisch
    Verlag American Chemical Society (ACS)
    Erscheinungsland us
    Dokumenttyp Artikel ; Online
    ISSN 1948-7185
    DOI 10.1021/acs.jpclett.0c01698
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  6. Artikel: Structure of Furin Protease Binding to SARS-CoV-2 Spike Glycoprotein and Implications for Potential Targets and Virulence

    Vankadari, Naveen

    J Phys Chem Lett

    Abstract: The COVID-19 pandemic is an urgent global health emergency, and the presence of Furin site in the SARS-CoV-2 spike glycoprotein alters virulence and warrants further molecular, structural, and biophysical studies. Here we report the structure of Furin in ...

    Abstract The COVID-19 pandemic is an urgent global health emergency, and the presence of Furin site in the SARS-CoV-2 spike glycoprotein alters virulence and warrants further molecular, structural, and biophysical studies. Here we report the structure of Furin in complex with SARS-CoV-2 spike glycoprotein, demonstrating how Furin binds to the S1/S2 region of spike glycoprotein and eventually cleaves the viral protein using experimental functional studies, molecular dynamics, and docking. The structural studies underline the mechanism and mode of action of Furin, which is a key process in host cell entry and a hallmark of enhanced virulence. Our whole-exome sequencing analysis shows the genetic variants/alleles in Furin were found to alter the binding affinity for viral spike glycoprotein and could vary in infectivity in humans. Unravelling the mechanisms of Furin action, binding dynamics, and the genetic variants opens the growing arena of bona fide antibodies and development of potential therapeutics targeting the blockage of Furin cleavage.
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #678528
    Datenquelle COVID19

    Kategorien

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  7. Artikel: Arbidol: A potential antiviral drug for the treatment of SARS-CoV-2 by blocking trimerization of the spike glycoprotein

    Vankadari, Naveen

    Int J Antimicrob Agents

    Abstract: The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) pandemic is a global public health emergency, and new therapeutics are needed. This article reports the potential drug target and mechanism of action of Arbidol (umifenovir) to treat ... ...

    Abstract The severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) pandemic is a global public health emergency, and new therapeutics are needed. This article reports the potential drug target and mechanism of action of Arbidol (umifenovir) to treat coronavirus disease 2019 (COVID-19). Molecular dynamics and structural analysis were used to show how Arbidol targets the SARS-CoV-2 spike glycoprotein and impedes its trimerization, which is key for host cell adhesion and hijacking, indicating the potential of Arbidol to treat COVID-19. It is hoped that knowledge of the potential drug target and mechanism of action of Arbidol will help in the development of new therapeutics for SARS-CoV-2.
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #291695
    Datenquelle COVID19

    Kategorien

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  8. Artikel: Overwhelming mutations or SNPs of SARS-CoV-2: A point of caution

    Vankadari, Naveen

    Gene

    Abstract: The morbidity of SARS-CoV-2 (COVID-19) is reaching 3 Million landmark causing and a serious public health concern globally and it is enigmatic how several antiviral and antibody treatments were not effective in the different period across the globe. With ...

    Abstract The morbidity of SARS-CoV-2 (COVID-19) is reaching 3 Million landmark causing and a serious public health concern globally and it is enigmatic how several antiviral and antibody treatments were not effective in the different period across the globe. With the drastic increasing number of positive cases around the world WHO raised the importance in the assessment of the risk of spread and understanding genetic modifications that could have occurred in the SARS-CoV-2. Using all available deep sequencing data of complete genome from all over the world (NCBI repository), we identified several hundreds of point mutations or SNPs in SARS-CoV-2 all across the genome. This could be the cause for the constant change and differed virulence with an increase in mortality and morbidity. Among the 12 different countries (one sequence from each country) with complete genome sequencing data, we noted the 47 key point mutations or SNPs located along the entire genome that might have impact in the virulence and response to different antivirals against SARS-CoV-2. In this regard, key viral proteins of spike glycoprotein, Nsp1, RdRp and the ORF8 region got heavily mutated within these 3 months via person-to-person passage. We also discuss what could be the possible cause of this rapid mutation in the SARS-CoV-2.
    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #324620
    Datenquelle COVID19

    Kategorien

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  9. Artikel ; Online: Structural interactions between pandemic SARS-CoV-2 spike glycoprotein and human Furin protease

    Vankadari, Naveen

    bioRxiv

    Abstract: The SARS-CoV-2 pandemic is an urgent global public health emergency and warrants investigating molecular and structural studies addressing the dynamics of viral proteins involved in host cell adhesion. The recent comparative genomic studies highlight the ...

    Abstract The SARS-CoV-2 pandemic is an urgent global public health emergency and warrants investigating molecular and structural studies addressing the dynamics of viral proteins involved in host cell adhesion. The recent comparative genomic studies highlight the insertion of Furin protease site in the SARS-CoV-2 spike glycoprotein alerting possible modification in the viral spike protein and its eventual entry to host cell and presence of Furin site implicated to virulence. Here we structurally show how Furin interacts with the SARS-CoV-2 spike glycoprotein homotrimer at S1/S2 region, which underlined the mechanism and mode of action, which is a key for host cell entry. Unravelling the structural features of biding site opens the arena in rising bonafide antibodies targeting to block the Furin cleavage and have great implications in the development of Furin inhibitors or therapeutics.
    Schlagwörter covid19
    Verlag BioRxiv; WHO
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.04.10.036533
    Datenquelle COVID19

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  10. Artikel ; Online: Arbidol: A potential antiviral drug for the treatment of SARS-CoV-2 by blocking the trimerization of viral spike glycoprotein ?

    Vankadari, Naveen

    International Journal of Antimicrobial Agents

    Abstract: Abstract The SARS-CoV-2 pandemic is an urgent global public health emergency and warrants investigating studies on bonafide antivirals for combat. Here we report the drug target and mechanism of action of potential antiviral drug Arbidol for SARS-CoV-2 ... ...

    Abstract Abstract The SARS-CoV-2 pandemic is an urgent global public health emergency and warrants investigating studies on bonafide antivirals for combat. Here we report the drug target and mechanism of action of potential antiviral drug Arbidol for SARS-CoV-2 infections. Our structural and molecular dynamics studies show how Arbidol targets the SARS-CoV-2 spike glycoprotein and impede the trimerization of spike glycoprotein, which is a key for host cell adhesion and hijacking, thus placing Arbidol as a potential drug for repurposing. This study also abets in the development of other new therapeutics for COIVD-19 disease based on Arbidol binding mode and using structure-guided drug designing.
    Schlagwörter covid19
    Verlag Elsevier
    Dokumenttyp Artikel ; Online
    DOI 10.1016/j.ijantimicag.2020.105998
    Datenquelle COVID19

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