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  1. Article ; Online: Nucleocapsid Structure of Negative Strand RNA Virus.

    Luo, Ming / Terrell, James Ross / Mcmanus, Shelby Ashlyn

    Viruses

    2020  Volume 12, Issue 8

    Abstract: Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. ... ...

    Abstract Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. In NSVs, the single strand RNA genome is encapsidated in the linear nucleocapsid throughout the viral replication cycle. Subunits of the nucleocapsid protein are parallelly aligned along the RNA genome that is sandwiched between two domains composed of conserved helix motifs. The viral RNA-dependent-RNA polymerase (vRdRp) must recognize the protein-RNA complex of the nucleocapsid and unveil the protected genomic RNA in order to initiate viral RNA synthesis. In addition, vRdRp must continuously translocate along the protein-RNA complex during elongation in viral RNA synthesis. This unique mechanism of viral RNA synthesis suggests that the nucleocapsid may play a regulatory role during NSV replication.
    MeSH term(s) Genome, Viral ; Models, Molecular ; Negative-Sense RNA Viruses/chemistry ; Negative-Sense RNA Viruses/genetics ; Negative-Sense RNA Viruses/physiology ; Negative-Sense RNA Viruses/ultrastructure ; Nucleocapsid/chemistry ; Nucleocapsid/genetics ; Nucleocapsid/physiology ; Nucleocapsid/ultrastructure ; Nucleocapsid Proteins/chemistry ; Nucleocapsid Proteins/metabolism ; Protein Conformation ; Protein Folding ; RNA, Viral/biosynthesis ; RNA, Viral/genetics ; RNA, Viral/metabolism ; RNA-Dependent RNA Polymerase/metabolism
    Chemical Substances Nucleocapsid Proteins ; RNA, Viral ; RNA-Dependent RNA Polymerase (EC 2.7.7.48)
    Language English
    Publishing date 2020-07-30
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12080835
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Nucleocapsid Structure of Negative Strand RNA Virus

    Luo, Ming / Terrell, James Ross / Mcmanus, Shelby Ashlyn

    Viruses. 2020 July 30, v. 12, no. 8

    2020  

    Abstract: Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. ... ...

    Abstract Negative strand RNA viruses (NSVs) include many important human pathogens, such as influenza virus, Ebola virus, and rabies virus. One of the unique characteristics that NSVs share is the assembly of the nucleocapsid and its role in viral RNA synthesis. In NSVs, the single strand RNA genome is encapsidated in the linear nucleocapsid throughout the viral replication cycle. Subunits of the nucleocapsid protein are parallelly aligned along the RNA genome that is sandwiched between two domains composed of conserved helix motifs. The viral RNA-dependent-RNA polymerase (vRdRp) must recognize the protein–RNA complex of the nucleocapsid and unveil the protected genomic RNA in order to initiate viral RNA synthesis. In addition, vRdRp must continuously translocate along the protein–RNA complex during elongation in viral RNA synthesis. This unique mechanism of viral RNA synthesis suggests that the nucleocapsid may play a regulatory role during NSV replication.
    Keywords Ebolavirus ; Orthomyxoviridae ; RNA ; RNA-directed RNA polymerase ; Rabies lyssavirus ; animal pathogens ; genome ; genomics ; nucleocapsid ; nucleocapsid proteins ; virus replication
    Language English
    Dates of publication 2020-0730
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12080835
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Hemoglobin crystals immersed in liquid oxygen reveal diffusion channels.

    Terrell, James Ross / Gumpper, Ryan H / Luo, Ming

    Biochemical and biophysical research communications

    2018  Volume 495, Issue 2, Page(s) 1858–1863

    Abstract: Human hemoglobin (HbA) transports molecular oxygen ( ... ...

    Abstract Human hemoglobin (HbA) transports molecular oxygen (O
    MeSH term(s) Binding Sites ; Crystallization/methods ; Diffusion ; Hemoglobins/chemistry ; Hemoglobins/ultrastructure ; Molecular Dynamics Simulation ; Oxygen/chemistry ; Porosity ; Protein Binding ; Protein Conformation
    Chemical Substances Hemoglobins ; Oxygen (S88TT14065)
    Language English
    Publishing date 2018--08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2017.12.038
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: Hemoglobin crystals immersed in liquid oxygen reveal diffusion channels

    Terrell, James Ross / Gumpper, Ryan H / Luo, Ming

    Biochemical and biophysical research communications. 2018 Jan. 08, v. 495, no. 2

    2018  

    Abstract: Human hemoglobin (HbA) transports molecular oxygen (O₂) from the lung to tissues where the partial pressure of O₂ is lower. O₂ binds to HbA at the heme cofactor and is stabilized by a distal histidine (HisE7). HisE7 has been observed to occupy opened and ...

    Abstract Human hemoglobin (HbA) transports molecular oxygen (O₂) from the lung to tissues where the partial pressure of O₂ is lower. O₂ binds to HbA at the heme cofactor and is stabilized by a distal histidine (HisE7). HisE7 has been observed to occupy opened and closed conformations, and is postulated to act as a gate controlling the binding/release of O₂. However, it has been suggested that HbA also contains intraprotein oxygen channels for entrances/exits far from the heme. In this study, we developed a novel method of crystal immersion in liquid oxygen prior to X-ray data collection. In the crystals immersed in liquid oxygen, the heme center was oxidized to generate aquomethemoglobin. Increases of structural flexibility were also observed in regions that are synonymous with previously postulated oxygen channels. These regions also correspond to medically relevant mutations which affect O₂ affinity. The way HbA utilizes these O₂ channels could have a profound impact on understanding the relationship of HbA O₂ transport within these disease conditions. Finally, the liquid oxygen immersion technique can be utilized as a new tool to crystallographically examine proteins and protein complexes which utilize O₂ for enzyme catalysis or transport.
    Keywords X-radiation ; catalytic activity ; data collection ; enzymes ; heme ; hemoglobin ; histidine ; humans ; liquids ; lungs ; oxygen ; partial pressure ; research
    Language English
    Dates of publication 2018-0108
    Size p. 1858-1863.
    Publishing place Elsevier Inc.
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2017.12.038
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 71/706: Show issues
    Z 3.8: Show issues

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  5. Article ; Online: Structural studies of antitumor compounds that target the RING domain of MDM2.

    Terrell, James Ross / Tang, Sijia / Faniyi, Oluwafoyinsola Omobodunde / Jeong, In Ho / Yin, Jun / Nijampatnam, Bhavitavya / Velu, Sadanandan E / Wang, Wei / Zhang, Ruiwen / Luo, Ming

    publication RETRACTED

    Protein science : a publication of the Protein Society

    2021  Volume 31, Issue 8, Page(s) e4367

    Abstract: Mouse double minute 2 homolog (MDM2) is an E3 ubiquitin-protein ligase that is involved in the transfer of ubiquitin to p53 and other protein substrates. The expression of MDM2 is elevated in cancer cells and inhibitors of MDM2 showed potent anticancer ... ...

    Abstract Mouse double minute 2 homolog (MDM2) is an E3 ubiquitin-protein ligase that is involved in the transfer of ubiquitin to p53 and other protein substrates. The expression of MDM2 is elevated in cancer cells and inhibitors of MDM2 showed potent anticancer activities. Many inhibitors target the p53 binding domain of MDM2. However, inhibitors such as Inulanolide A and MA242 are found to bind the RING domain of MDM2 to block ubiquitin transfer. In this report, crystal structures of MDM2 RING domain in complex with Inulanolide A and MA242 were solved. These inhibitors primarily bind in a hydrophobic site centered at the sidechain of Tyr489 at the C-terminus of MDM2 RING domain. The C-terminus of MDM2 RING domain, especially residue Tyr489, is required for ubiquitin discharge induced by MDM2. The binding of these inhibitors at Tyr489 may interrupt interactions between the MDM2 RING domain and the E2-Ubiquitin complex to inhibit ubiquitin transfer, regardless of what the substrate is. Our results suggest a new mechanism of inhibition of MDM2 E3 activity for a broad spectrum of substrates.
    MeSH term(s) Animals ; Mice ; Protein Binding ; Protein Structure, Tertiary ; Proto-Oncogene Proteins c-mdm2/metabolism ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Ubiquitin/chemistry ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Tumor Suppressor Protein p53 ; Ubiquitin ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2021-12-03
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Retracted Publication
    ZDB-ID 1106283-6
    ISSN 1469-896X ; 0961-8368
    ISSN (online) 1469-896X
    ISSN 0961-8368
    DOI 10.1002/pro.4367
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3407: Show issues Location:
    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)
    Zs.MO 1: Show issues

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