LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 315

Search options

  1. Article ; Online: Infectious Disease Research in China.

    Lou, Zhiyong

    ACS infectious diseases

    2020  Volume 6, Issue 5, Page(s) 760

    Keywords covid19
    Language English
    Publishing date 2020-04-24
    Publishing country United States
    Document type Editorial
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.0c00220
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article ; Online: The Life of SARS-CoV-2 Inside Cells: Replication-Transcription Complex Assembly and Function.

    Lou, Zhiyong / Rao, Zihe

    Annual review of biochemistry

    2022  Volume 91, Page(s) 381–401

    Abstract: The persistence of the coronavirus disease 2019 (COVID-19) pandemic has resulted in increasingly disruptive impacts, and it has become the most devastating challenge to global health in a century. The rapid emergence of severe acute respiratory syndrome ... ...

    Abstract The persistence of the coronavirus disease 2019 (COVID-19) pandemic has resulted in increasingly disruptive impacts, and it has become the most devastating challenge to global health in a century. The rapid emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants challenges the currently available therapeutics for clinical application. Nonstructural proteins (also known as replicase proteins) with versatile biological functions play central roles in viral replication and transcription inside the host cells, and they are the most conserved target proteins among the SARS-CoV-2 variants. Specifically, they constitute the replication-transcription complexes (RTCs) dominating the synthesis of viral RNA. Knowledge of themolecular mechanisms of nonstructural proteins and their assembly into RTCs will benefit the development of antivirals targeting them against existing or potentially emerging variants. In this review, we summarize current knowledge of the structures and functions of coronavirus nonstructural proteins as well as the assembly and functions of RTCs in the life cycle of the virus.
    MeSH term(s) COVID-19/drug therapy ; Humans ; RNA, Viral/genetics ; SARS-CoV-2 ; Virus Replication
    Chemical Substances RNA, Viral
    Language English
    Publishing date 2022-06-21
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-052521-115653
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.209: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  4. Article: A Structural View of Negative-Sense RNA Virus Nucleocapsid Protein and Its Functions Beyond.

    Lou, Zhiyong

    Sub-cellular biochemistry

    2018  Volume 88, Page(s) 19–37

    Abstract: Negative-sense single-stranded RNA virus (NSRV) is featured by their ribonucleoprotein (RNP) complex composed by viral polymerase and genomic RNA enwrapped by nucleocapsid protein (NP). The RNP is packaged in virions and plays a central role throughout ... ...

    Abstract Negative-sense single-stranded RNA virus (NSRV) is featured by their ribonucleoprotein (RNP) complex composed by viral polymerase and genomic RNA enwrapped by nucleocapsid protein (NP). The RNP is packaged in virions and plays a central role throughout virus lifecycle. In the past decade, structural biology presents molecular insights into NPs encoded by most representative NSRVs, helping to understand the mechanism of RNP formation. Interestingly, works initiated from structural biology also reveal unexpected biological functions of virus NP beyond a structural protein. All these further the knowledge of virus NP and provide great potential for the discovery of antiviral agents to target virus RNP formation. In this chapter, we will summarize the structures and functions of viral NPs, as well as the attempt of NP-targeted antiviral development.
    MeSH term(s) Genome, Viral ; Nucleocapsid Proteins/chemistry ; Nucleocapsid Proteins/genetics ; Nucleocapsid Proteins/metabolism ; Protein Domains ; RNA Viruses/chemistry ; RNA Viruses/genetics ; RNA Viruses/metabolism ; RNA, Viral/chemistry ; RNA, Viral/genetics ; RNA, Viral/metabolism ; Structure-Activity Relationship
    Chemical Substances Nucleocapsid Proteins ; RNA, Viral
    Language English
    Publishing date 2018-06-13
    Publishing country United States
    Document type Journal Article
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-981-10-8456-0_2
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article: Editorial: Bone targeting nanoparticle drug delivery system in bone metabolism and bone-related tumor diseases.

    Wang, Xing / Meng, Fenghua / Lei, Zhiyong / Fan, Daoyang / Lou, Bo

    Frontiers in pharmacology

    2022  Volume 13, Page(s) 1016631

    Language English
    Publishing date 2022-09-20
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2587355-6
    ISSN 1663-9812
    ISSN 1663-9812
    DOI 10.3389/fphar.2022.1016631
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Structural basis of the recognition of adeno-associated virus by the neurological system-related receptor carbonic anhydrase IV.

    Zhang, Ran / Liu, Yixiao / Yu, Fengxi / Xu, Guangxue / Li, Lili / Li, Baobin / Lou, Zhiyong

    PLoS pathogens

    2024  Volume 20, Issue 2, Page(s) e1011953

    Abstract: Carbonic anhydrase IV (Car4) is a newly identified receptor that allows adeno-associated virus (AAV) 9P31 to cross the blood-brain barrier and achieve efficient infection in the central nervous system (CNS) in mouse models. However, the molecular ... ...

    Abstract Carbonic anhydrase IV (Car4) is a newly identified receptor that allows adeno-associated virus (AAV) 9P31 to cross the blood-brain barrier and achieve efficient infection in the central nervous system (CNS) in mouse models. However, the molecular mechanism by which engineered AAV capsids with 7-mer insertion in the variable region (VR) VIII recognize these novel cellular receptors is unknown. Here we report the cryo-EM structures of AAV9P31 and its complex with Mus musculus Car4 at atomic resolution by utilizing the block-based reconstruction (BBR) method. The structures demonstrated that Car4 binds to the protrusions at 3-fold axes of the capsid. The inserted 7-mer extends into a hydrophobic region near the catalytic center of Car4 to form stable interactions. Mutagenesis studies also identified the key residues in Car4 responsible for the AAV9P31 interaction. These findings provide new insights into the novel receptor recognition mechanism of AAV generated by directed evolution and highlight the application of the BBR method to studying the virus-receptor molecular mechanism.
    MeSH term(s) Animals ; Mice ; Dependovirus/genetics ; Carbonic Anhydrase IV/analysis ; Carbonic Anhydrase IV/metabolism ; Capsid/metabolism ; Capsid Proteins/metabolism ; Blood-Brain Barrier/metabolism ; Genetic Vectors
    Chemical Substances Carbonic Anhydrase IV (EC 4.2.1.-) ; Capsid Proteins
    Language English
    Publishing date 2024-02-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011953
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Reply to: Errors in the deposited SFTSV L protein structure.

    Wang, Panpan / Liu, Lu / Liu, Aijun / Lou, Zhiyong

    Nature microbiology

    2021  Volume 6, Issue 5, Page(s) 551–552

    MeSH term(s) Bunyaviridae Infections ; Humans ; Phlebovirus
    Language English
    Publishing date 2021-04-29
    Publishing country England
    Document type Letter ; Comment
    ISSN 2058-5276
    ISSN (online) 2058-5276
    DOI 10.1038/s41564-021-00902-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  8. Article ; Online: Architecture of severe fever with thrombocytopenia syndrome virus.

    Sun, Zixian / Cheng, Jing / Bai, Yuan / Cao, Lin / Xie, Daoxin / Deng, Fei / Zhang, Xinzheng / Rao, Zihe / Lou, Zhiyong

    Protein & cell

    2023  Volume 14, Issue 12, Page(s) 914–918

    MeSH term(s) Humans ; Severe Fever with Thrombocytopenia Syndrome ; Phlebovirus
    Language English
    Publishing date 2023-01-04
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2543451-2
    ISSN 1674-8018 ; 1674-8018
    ISSN (online) 1674-8018
    ISSN 1674-8018
    DOI 10.1093/procel/pwad019
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article ; Online: Role of ferroptosis in fibrosis diseases.

    Sun, Zhiyong / Zou, Xiaozhou / Bao, Meihua / Huang, Zhongjie / Lou, Yutao / Zhang, Yiwen / Huang, Ping

    The American journal of the medical sciences

    2023  Volume 366, Issue 2, Page(s) 87–95

    Abstract: Ferroptosis is a pervasive non-apoptotic mode of cell death that is different from autophagy or necrosis. It is mainly caused by an imbalance between the production and degradation of lipid reactive oxygen species in cells. Several metabolic pathways and ...

    Abstract Ferroptosis is a pervasive non-apoptotic mode of cell death that is different from autophagy or necrosis. It is mainly caused by an imbalance between the production and degradation of lipid reactive oxygen species in cells. Several metabolic pathways and biochemical processes, such as amino acid and lipid metabolism, iron handling, and mitochondrial respiration, affect and regulate cell sensitivity to peroxidation and ferroptosis. Organ fibrosis, a pathological manifestation of several etiological conditions, leads to chronic tissue injury and is characterized by excessive deposition of extracellular matrix components. Excessive tissue fibrosis can have diverse pathophysiological effects on several organ systems, eventually causing organ dysfunction and failure. The current manuscript provides a review that illustrates the link between ferroptosis and organ fibrosis and to better understand the underlying mechanisms. It provides novel potential therapeutic approaches and targets for fibrosis diseases.
    MeSH term(s) Humans ; Ferroptosis ; Cell Death ; Iron/metabolism ; Necrosis ; Reactive Oxygen Species/metabolism ; Fibrosis ; Lipid Peroxidation/physiology
    Chemical Substances Iron (E1UOL152H7) ; Reactive Oxygen Species
    Language English
    Publishing date 2023-05-14
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 82078-7
    ISSN 1538-2990 ; 0002-9629
    ISSN (online) 1538-2990
    ISSN 0002-9629
    DOI 10.1016/j.amjms.2023.04.024
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Ua VI Zs.2/10: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  10. Article ; Online: Structure basis for allosteric regulation of lymphocytic choriomeningitis virus polymerase function by Z matrix protein.

    Liu, Lu / Wang, Panpan / Liu, Aijun / Zhang, Leike / Yan, Liming / Guo, Yu / Xiao, Gengfu / Rao, Zihe / Lou, Zhiyong

    Protein & cell

    2023  Volume 14, Issue 9, Page(s) 703–707

    MeSH term(s) Lymphocytic choriomeningitis virus/physiology ; Allosteric Regulation ; Nucleotidyltransferases
    Chemical Substances Nucleotidyltransferases (EC 2.7.7.-)
    Language English
    Publishing date 2023-04-11
    Publishing country Germany
    Document type Letter ; Research Support, Non-U.S. Gov't
    ZDB-ID 2543451-2
    ISSN 1674-8018 ; 1674-8018
    ISSN (online) 1674-8018
    ISSN 1674-8018
    DOI 10.1093/procel/pwad018
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top