LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 2 of total 2

Search options

  1. Article ; Online: Ensemble cryo-EM reveals conformational states of the nsp13 helicase in the SARS-CoV-2 helicase replication-transcription complex.

    Chen, James / Wang, Qi / Malone, Brandon / Llewellyn, Eliza / Pechersky, Yakov / Maruthi, Kashyap / Eng, Ed T / Perry, Jason K / Campbell, Elizabeth A / Shaw, David E / Darst, Seth A

    Nature structural & molecular biology

    2022  Volume 29, Issue 3, Page(s) 250–260

    Abstract: The SARS-CoV-2 nonstructural proteins coordinate genome replication and gene expression. Structural analyses revealed the basis for coupling of the essential nsp13 helicase with the RNA-dependent RNA polymerase (RdRp) where the holo-RdRp and RNA ... ...

    Abstract The SARS-CoV-2 nonstructural proteins coordinate genome replication and gene expression. Structural analyses revealed the basis for coupling of the essential nsp13 helicase with the RNA-dependent RNA polymerase (RdRp) where the holo-RdRp and RNA substrate (the replication-transcription complex or RTC) associated with two copies of nsp13 (nsp13
    MeSH term(s) COVID-19 ; Cryoelectron Microscopy ; Humans ; RNA Helicases/chemistry ; SARS-CoV-2 ; Viral Nonstructural Proteins/chemistry ; Virus Replication
    Chemical Substances Viral Nonstructural Proteins ; RNA Helicases (EC 3.6.4.13)
    Language English
    Publishing date 2022-03-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-022-00734-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: Structural basis for substrate selection by the SARS-CoV-2 replicase.

    Malone, Brandon F / Perry, Jason K / Olinares, Paul Dominic B / Lee, Hery W / Chen, James / Appleby, Todd C / Feng, Joy Y / Bilello, John P / Ng, Honkit / Sotiris, Johanna / Ebrahim, Mark / Chua, Eugene Y D / Mendez, Joshua H / Eng, Ed T / Landick, Robert / Götte, Matthias / Chait, Brian T / Campbell, Elizabeth A / Darst, Seth A

    Nature

    2023  Volume 614, Issue 7949, Page(s) 781–787

    Abstract: The SARS-CoV-2 RNA-dependent RNA polymerase coordinates viral RNA synthesis as part of an assembly known as the replication-transcription complex (RTC) ...

    Abstract The SARS-CoV-2 RNA-dependent RNA polymerase coordinates viral RNA synthesis as part of an assembly known as the replication-transcription complex (RTC)
    MeSH term(s) Humans ; Antiviral Agents/chemistry ; Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; Coronavirus RNA-Dependent RNA Polymerase/chemistry ; Coronavirus RNA-Dependent RNA Polymerase/metabolism ; Coronavirus RNA-Dependent RNA Polymerase/ultrastructure ; COVID-19/virology ; Cryoelectron Microscopy ; Nucleosides/metabolism ; Nucleosides/pharmacology ; RNA, Viral/biosynthesis ; RNA, Viral/chemistry ; RNA, Viral/metabolism ; SARS-CoV-2/enzymology ; Substrate Specificity ; Guanosine Triphosphate/metabolism ; RNA Caps
    Chemical Substances Antiviral Agents ; Coronavirus RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; NSP12 protein, SARS-CoV-2 (EC 2.7.7.48) ; Nucleosides ; RNA, Viral ; remdesivir (3QKI37EEHE) ; Guanosine Triphosphate (86-01-1) ; RNA Caps ; GS-441524 triphosphate (AEL0YED4SU)
    Language English
    Publishing date 2023-02-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-022-05664-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top