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  1. Article ; Online: Erratum

    Blombery, Piers / Fox, Lucy / Ryland, Georgina L / Thompson, Ella R / Lickiss, Jennifer / McBean, Michelle / Yerneni, Satwica / Trainer, Alison / Hughes, David / Greenway, Anthea / Mechinaud, Francoise / Wood, Erica M / Lieschke, Graham J / Szer, Jeff / Barbaro, Pasquale / Roy, John / Wight, Joel / Lynch, Elly / Martyn, Melissa /
    Gaff, Clara / Ritchie, David

    Haematologica

    2024  Volume 109, Issue 4, Page(s) 1311

    Language English
    Publishing date 2024-04-01
    Publishing country Italy
    Document type Journal Article
    ZDB-ID 2333-4
    ISSN 1592-8721 ; 0017-6567 ; 0390-6078
    ISSN (online) 1592-8721
    ISSN 0017-6567 ; 0390-6078
    DOI 10.3324/haematol.2023.284760
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article: HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.

    Greenway, Alison L / Holloway, Gavan / McPhee, Dale A / Ellis, Phoebe / Cornall, Alyssa / Lidman, Michael

    Journal of biosciences

    2003  Volume 28, Issue 3, Page(s) 323–335

    Abstract: HIV-1 has at its disposal numerous proteins encoded by its genome which provide the required arsenal to establish and maintain infection in its host for a considerable number of years. One of the most important and enigmatic of these proteins is Nef. The ...

    Abstract HIV-1 has at its disposal numerous proteins encoded by its genome which provide the required arsenal to establish and maintain infection in its host for a considerable number of years. One of the most important and enigmatic of these proteins is Nef. The Nef protein of HIV-1 plays a fundamental role in the virus life cycle. This small protein of approximately 27 kDa is required for maximal virus replication and disease progression. The mechanisms by which it is able to act as a positive factor during virus replication is an area of intense research and although some controversy surrounds Nef much has been gauged as to how it functions. Its ability to modulate the expression of key cellular receptors important for cell activation and control signal transduction elements and events by interacting with numerous cellular kinases and signalling molecules, including members of the Src family kinases, leading to an effect on host cell function is likely to explain at least in part its role during infection and represents a finely tuned mechanism where this protein assists HIV-1 to control its host.
    MeSH term(s) Animals ; Apoptosis ; Gene Products, nef/metabolism ; HIV Infections/metabolism ; HIV-1/physiology ; Humans ; Protein Kinases/metabolism ; Receptors, Cell Surface/metabolism ; Signal Transduction/physiology ; Virion/metabolism ; Virion/pathogenicity ; Virus Replication ; nef Gene Products, Human Immunodeficiency Virus
    Chemical Substances Gene Products, nef ; Receptors, Cell Surface ; nef Gene Products, Human Immunodeficiency Virus ; Protein Kinases (EC 2.7.-)
    Language English
    Publishing date 2003-04-28
    Publishing country India
    Document type Journal Article ; Review
    ZDB-ID 756157-x
    ISSN 0250-5991
    ISSN 0250-5991
    DOI 10.1007/bf02970151
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Studies with GFP-Vpr fusion proteins: induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization.

    Waldhuber, Megan G / Bateson, Michael / Tan, Judith / Greenway, Alison L / McPhee, Dale A

    Virology

    2003  Volume 313, Issue 1, Page(s) 91–104

    Abstract: The human immunodeficiency virus type 1 (HIV-1) Vpr protein is known to arrest the cell cycle in G(2)/M and induce apoptosis following arrest. The functions of Vpr relative to its location in the cell remain unresolved. We now demonstrate that the ... ...

    Abstract The human immunodeficiency virus type 1 (HIV-1) Vpr protein is known to arrest the cell cycle in G(2)/M and induce apoptosis following arrest. The functions of Vpr relative to its location in the cell remain unresolved. We now demonstrate that the location and function of Vpr are dependent on the makeup of fusion proteins and that the functions of G(2)/M arrest and apoptosis are separable. Using green fluorescence protein mutants (EGFP or EYFP), we found that fusion at either the N- or C-terminus compromised the ability of Vpr to arrest cell cycling, relative to that of His-Vpr or wild-type protein. Additionally, utilizing the ability to specifically identify cells expressing the fusion proteins, we confirm that Vpr can induce apoptosis, but appears to be independent of cell-cycle arrest in G(2)/M. Both N- and C-terminal Vpr/EYFP fusion proteins induced apoptosis but caused minimal G(2)/M arrest. These studies with Vpr fusion proteins indicate that the functions of Vpr leading to G(2)/M arrest and apoptosis are separable and that fusion of Vpr to EGFP or EYFP affected the localization of the protein. Our findings suggest that nuclear membrane localization and nuclear import and export are strongly governed by modification of the N-terminus of Vpr.
    MeSH term(s) Apoptosis ; Cell Cycle/drug effects ; Cell Cycle/physiology ; Cell Nucleus/metabolism ; Flow Cytometry ; G2 Phase ; Gene Products, vpr/analysis ; Gene Products, vpr/chemistry ; Gene Products, vpr/metabolism ; Green Fluorescent Proteins ; HIV-1 ; HeLa Cells ; Humans ; Luminescent Proteins/analysis ; Luminescent Proteins/chemistry ; Luminescent Proteins/metabolism ; Mitosis ; Nuclear Envelope/metabolism ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/metabolism ; Recombinant Fusion Proteins/pharmacology ; Time Factors ; Transfection ; vpr Gene Products, Human Immunodeficiency Virus
    Chemical Substances Gene Products, vpr ; Luminescent Proteins ; Recombinant Fusion Proteins ; vpr Gene Products, Human Immunodeficiency Virus ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2003-08-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 200425-2
    ISSN 1096-0341 ; 0042-6822
    ISSN (online) 1096-0341
    ISSN 0042-6822
    DOI 10.1016/s0042-6822(03)00258-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.172: Show issues Location:
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  4. Article: HIV-1 Nef control of cell signalling molecules: Multiple strategies to promote virus replication

    Greenway, Alison L / Holloway, Gavan / McPhee, Dale A / Ellis, Phoebe / Cornall, Alyssa / Lidman, Michael

    Journal of biosciences. 2003 Apr., v. 28, no. 3

    2003  

    Abstract: HIV-1 has at its disposal numerous proteins encoded by its genome which provide the required arsenal to establish and maintain infection in its host for a considerable number of years. One of the most important and enigmatic of these proteins is Nef. The ...

    Abstract HIV-1 has at its disposal numerous proteins encoded by its genome which provide the required arsenal to establish and maintain infection in its host for a considerable number of years. One of the most important and enigmatic of these proteins is Nef. The Nef protein of HIV-1 plays a fundamental role in the virus life cycle. This small protein of approximately 27 kDa is required for maximal virus replication and disease progression. The mechanisms by which it is able to act as a positive factor during virus replication is an area of intense research and although some controversy surrounds Nef much has been gauged as to how it functions. Its ability to modulate the expression of key cellular receptors important for cell activation and control signal transduction elements and events by interacting with numerous cellular kinases and signalling molecules, including members of the Src family kinases, leading to an effect on host cell function is likely to explain at least in part its role during infection and represents a finely tuned mechanism where this protein assists HIV-1 to control its host.
    Keywords Human immunodeficiency virus 1 ; disease course ; genome ; phosphotransferases (kinases) ; receptors ; signal transduction ; virus replication ; viruses
    Language English
    Dates of publication 2003-04
    Size p. 323-335.
    Publishing place Springer India
    Document type Article
    ZDB-ID 756157-x
    ISSN 0973-7138 ; 0250-5991
    ISSN (online) 0973-7138
    ISSN 0250-5991
    DOI 10.1007/BF02970151
    Database NAL-Catalogue (AGRICOLA)

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    Z 5290: Show issues

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  5. Article: Apoptosis induced in synchronized human immunodeficiency virus type 1-infected primary peripheral blood mononuclear cells is detected after the peak of CD4+ T-lymphocyte loss and is dependent on the tropism of the gp120 envelope glycoprotein.

    Lawson, Victoria A / Silburn, Katherine A / Gorry, Paul R / Paukovic, Geza / Purcell, Damian F J / Greenway, Alison L / McPhee, Dale A

    Virology

    2004  Volume 327, Issue 1, Page(s) 70–82

    Abstract: Disease progression in human immunodeficiency virus type-1 (HIV-1)-infected individuals is frequently accompanied by declining CD4 cell numbers and the acquisition of a T-tropic (X4) or dual tropic (R5X4) phenotype. Understanding the mechanism of CD4 ... ...

    Abstract Disease progression in human immunodeficiency virus type-1 (HIV-1)-infected individuals is frequently accompanied by declining CD4 cell numbers and the acquisition of a T-tropic (X4) or dual tropic (R5X4) phenotype. Understanding the mechanism of CD4 cell loss in HIV-1 infection is essential for the development of effective therapeutic strategies. In this study, donor populations of peripheral blood mononuclear cells (PBMCs) were selected for their ability to support an equivalent acute infection by both R5 and X4 virus phenotypes. This demonstrated that CD4+ T-lymphocyte loss was due to the gp120 region of Env and was replication independent. Furthermore, apoptosis was only detected in cells infected with an X4 virus after the majority of CD4+ T-lymphocyte loss had occurred. These observations indicate that the CD4+ T-lymphocyte loss in an X4 HIV-1 infection is not directly mediated by apoptosis, although apoptosis may be induced in the remaining cell population as a consequence of this CD4+ T-lymphocyte loss.
    MeSH term(s) Apoptosis ; CD4-Positive T-Lymphocytes/pathology ; CD4-Positive T-Lymphocytes/virology ; Cells, Cultured ; HIV Envelope Protein gp120/metabolism ; HIV-1/pathogenicity ; HIV-1/physiology ; Humans ; Leukocytes, Mononuclear/physiology ; Leukocytes, Mononuclear/virology ; Lymphocyte Activation ; Receptors, CXCR4/metabolism ; Virus Replication
    Chemical Substances HIV Envelope Protein gp120 ; Receptors, CXCR4
    Language English
    Publishing date 2004-09-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 200425-2
    ISSN 1096-0341 ; 0042-6822
    ISSN (online) 1096-0341
    ISSN 0042-6822
    DOI 10.1016/j.virol.2004.06.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.172: Show issues Location:
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  6. Article: Human immunodeficiency virus type 1 Nef binds to tumor suppressor p53 and protects cells against p53-mediated apoptosis.

    Greenway, Alison L / McPhee, Dale A / Allen, Kelly / Johnstone, Ricky / Holloway, Gavan / Mills, John / Azad, Ahmed / Sankovich, Sonia / Lambert, Paul

    Journal of virology

    2001  Volume 76, Issue 6, Page(s) 2692–2702

    Abstract: The nef gene product of human immunodeficiency virus type 1 (HIV-1) is important for the induction of AIDS, and key to its function is its ability to manipulate T-cell function by targeting cellular signal transduction proteins. We reported that Nef ... ...

    Abstract The nef gene product of human immunodeficiency virus type 1 (HIV-1) is important for the induction of AIDS, and key to its function is its ability to manipulate T-cell function by targeting cellular signal transduction proteins. We reported that Nef coprecipitates a multiprotein complex from cells which contains tumor suppressor protein p53. We now show that Nef interacts directly with p53. Binding assays showed that an N-terminal, 57-residue fragment of Nef (Nef 1-57) contains the p53-binding domain. Nef also interacted with p53 during HIV-1 infection in vitro. As p53 plays a critical role in the regulation of apoptosis, we hypothesized that Nef may alter this process. Nef inhibited UV light-induced, p53-dependent apoptosis in MOLT-4 cells, with Nef 1-57 being as effective as its full-length counterpart. The inhibition by Nef of p53 apoptotic function is most likely due its observed ability to decrease p53 protein half-life and, consequently, p53 DNA binding activity and transcriptional activation. These data show that HIV-1 Nef may augment HIV replication by prolonging the viability of infected cells by blocking p53-mediated apoptosis.
    MeSH term(s) Apoptosis/physiology ; CD4-Positive T-Lymphocytes/virology ; Gene Products, nef/genetics ; Gene Products, nef/metabolism ; HIV-1/genetics ; HIV-1/pathogenicity ; HIV-1/physiology ; Humans ; Transcriptional Activation ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Ultraviolet Rays ; nef Gene Products, Human Immunodeficiency Virus
    Chemical Substances Gene Products, nef ; Tumor Suppressor Protein p53 ; nef Gene Products, Human Immunodeficiency Virus
    Language English
    Publishing date 2001-05-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.76.6.2692-2702.2002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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