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  1. Article ; Online: Renal Dysfunction due to Tenofovir-Diphosphate Inhibition of Mitochondrial Complex V (ATP Synthase).

    Sluis-Cremer, Nicolas

    Function (Oxford, England)

    2023  Volume 4, Issue 3, Page(s) zqad010

    MeSH term(s) Humans ; Tenofovir/adverse effects ; Diphosphates ; Adenosine Triphosphate/metabolism ; Kidney Diseases/chemically induced
    Chemical Substances oligomycin sensitivity-conferring protein (EC 7.1.2.2) ; Tenofovir (99YXE507IL) ; Diphosphates ; tenofovir diphosphate ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2023-02-24
    Publishing country England
    Document type Journal Article ; Comment
    ISSN 2633-8823
    ISSN (online) 2633-8823
    DOI 10.1093/function/zqad010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Retroviral reverse transcriptase: Structure, function and inhibition.

    Sluis-Cremer, Nicolas

    The Enzymes

    2021  Volume 50, Page(s) 179–194

    Abstract: Reverse transcriptase (RT) is a multifunctional enzyme that has RNA- and DNA-dependent DNA polymerase activity and ribonuclease H (RNase H) activity, and is responsible for the reverse transcription of retroviral single-stranded RNA into double-stranded ... ...

    Abstract Reverse transcriptase (RT) is a multifunctional enzyme that has RNA- and DNA-dependent DNA polymerase activity and ribonuclease H (RNase H) activity, and is responsible for the reverse transcription of retroviral single-stranded RNA into double-stranded DNA. The essential role that RT plays in the human immunodeficiency virus (HIV) life cycle is highlighted by the fact that multiple antiviral drugs-which can be classified into two distinct therapeutic classes-are routinely used to treat and/or prevent HIV infection. This book chapter provides detailed insights into the three-dimensional structure of HIV RT, the biochemical mechanisms of DNA polymerization and RNase H activity, and the mechanisms by which nucleoside/nucleotide and nonnucleoside RT inhibitors block reverse transcription.
    MeSH term(s) DNA Replication ; HIV Infections/drug therapy ; HIV Reverse Transcriptase/metabolism ; HIV Reverse Transcriptase/therapeutic use ; Humans ; RNA ; Reverse Transcriptase Inhibitors/pharmacology ; Reverse Transcriptase Inhibitors/therapeutic use
    Chemical Substances Reverse Transcriptase Inhibitors ; RNA (63231-63-0) ; HIV Reverse Transcriptase (EC 2.7.7.49)
    Language English
    Publishing date 2021-07-24
    Publishing country United States
    Document type Journal Article
    ISSN 0423-2607
    ISSN 0423-2607
    DOI 10.1016/bs.enz.2021.06.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mutations in the HIV-1 3'-Polypurine Tract and Integrase Strand Transfer Inhibitor Resistance.

    Wei, Yuliang / Sluis-Cremer, Nicolas

    Antimicrobial agents and chemotherapy

    2021  Volume 65, Issue 6

    MeSH term(s) Drug Resistance, Viral/genetics ; HIV Infections/drug therapy ; HIV Integrase/genetics ; HIV Integrase Inhibitors/pharmacology ; HIV Integrase Inhibitors/therapeutic use ; HIV-1/genetics ; Humans ; Mutation
    Chemical Substances HIV Integrase Inhibitors ; HIV Integrase (EC 2.7.7.-)
    Language English
    Publishing date 2021-05-18
    Publishing country United States
    Document type Letter ; Research Support, N.I.H., Extramural
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/AAC.02432-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 809: 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)
    Einzelsignatur: Show issues

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  4. Article ; Online: Cholesterol Metabolism in Antigen-Presenting Cells and HIV-1 Trans-Infection of CD4

    Okpaise, Daniel / Sluis-Cremer, Nicolas / Rappocciolo, Giovanna / Rinaldo, Charles R

    Viruses

    2023  Volume 15, Issue 12

    Abstract: Antiretroviral therapy (ART) provides an effective method for managing HIV-1 infection and preventing the onset of AIDS; however, it is ineffective against the reservoir of latent HIV-1 that persists predominantly in resting ... ...

    Abstract Antiretroviral therapy (ART) provides an effective method for managing HIV-1 infection and preventing the onset of AIDS; however, it is ineffective against the reservoir of latent HIV-1 that persists predominantly in resting CD4
    MeSH term(s) Humans ; HIV Infections/metabolism ; HIV-1/metabolism ; CD4-Positive T-Lymphocytes/metabolism ; Virus Latency ; Dendritic Cells/metabolism ; Cholesterol/metabolism ; Virus Replication
    Chemical Substances Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2023-11-29
    Publishing country Switzerland
    Document type Review ; Journal Article
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v15122347
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Mechanism by Which PF-3758309, a Pan Isoform Inhibitor of p21-Activated Kinases, Blocks Reactivation of HIV-1 Latency.

    Vargas, Benni / Boslett, James / Yates, Nathan / Sluis-Cremer, Nicolas

    Biomolecules

    2023  Volume 13, Issue 1

    Abstract: The "block and lock" strategy is one approach that might elicit a sterilizing cure for HIV-1 infection. The "block" refers to a compound's ability to inhibit latent HIV-1 proviral transcription, while the "lock" refers to its capacity to induce permanent ...

    Abstract The "block and lock" strategy is one approach that might elicit a sterilizing cure for HIV-1 infection. The "block" refers to a compound's ability to inhibit latent HIV-1 proviral transcription, while the "lock" refers to its capacity to induce permanent proviral silencing. We previously identified PF-3758309, a pan-isoform inhibitor of p21-activated kinases (PAKs), as a potent inhibitor of HIV-1 latency reversal. The goal of this study was to define the mechanism(s) involved. We found that both 24ST1NLESG cells (a cell line model of HIV-1 latency) and purified CD4+ naïve and central memory T cells express high levels of PAK2 and lower levels of PAK1 and PAK4. Knockdown of PAK1 or PAK2, but not PAK4, in 24ST1NLESG cells resulted in a modest, but statistically significant, decrease in the magnitude of HIV-1 latency reversal. Overexpression of PAK1 significantly increased the magnitude of latency reversal. A phospho-protein array analysis revealed that PF-3758309 down-regulates the NF-κB signaling pathway, which provides the most likely mechanism by which PF-3758309 inhibits latency reversal. Finally, we used cellular thermal shift assays combined with liquid chromatography and mass spectrometry to ascertain whether PF-3758309 off-target binding contributed to its activity. In 24ST1NLESG cells and in peripheral blood mononuclear cells, PF-3758309 bound to mitogen-activated protein kinase 1 and protein kinase A; however, knockdown of either of these kinases did not impact HIV-1 latency reversal. Collectively, our study suggests that PAK1 and PAK2 play a key role in the maintenance of HIV-1 latency.
    MeSH term(s) Humans ; HIV Infections ; HIV-1/metabolism ; p21-Activated Kinases/metabolism ; Virus Latency ; Leukocytes, Mononuclear/metabolism
    Chemical Substances p21-Activated Kinases (EC 2.7.11.1) ; PF 3758309 ; PAK4 protein, human (EC 2.7.1.11)
    Language English
    Publishing date 2023-01-04
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13010100
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Future of nonnucleoside reverse transcriptase inhibitors.

    Sluis-Cremer, Nicolas

    Proceedings of the National Academy of Sciences of the United States of America

    2018  Volume 115, Issue 4, Page(s) 637–638

    MeSH term(s) Anti-HIV Agents ; Drug Resistance, Viral/drug effects ; HIV Infections ; HIV Reverse Transcriptase ; Reverse Transcriptase Inhibitors
    Chemical Substances Anti-HIV Agents ; Reverse Transcriptase Inhibitors ; HIV Reverse Transcriptase (EC 2.7.7.49)
    Language English
    Publishing date 2018--23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1720975115
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: 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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  7. Article: Structures of kinetic intermediate states of HIV-1 reverse transcriptase DNA synthesis.

    Vergara, Sandra / Zhou, Xiahong / Santiago, Ulises / Conway, James F / Sluis-Cremer, Nicolas / Calero, Guillermo

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Reverse transcription of the retroviral single-stranded RNA into double-stranded DNA is an integral step during HIV-1 replication, and reverse transcriptase (RT) is a primary target for antiviral therapy. Despite a wealth of structural information on RT, ...

    Abstract Reverse transcription of the retroviral single-stranded RNA into double-stranded DNA is an integral step during HIV-1 replication, and reverse transcriptase (RT) is a primary target for antiviral therapy. Despite a wealth of structural information on RT, we lack critical insight into the intermediate kinetic states of DNA synthesis. Using catalytically active substrates, and a novel blot/diffusion cryo-electron microscopy approach, we captured 11 structures that define the substrate binding, reactant, transition and product states of dATP addition by RT at 1.9 to 2.4 Å resolution in the active site. Initial dATP binding to RT-template/primer complex involves a single Mg
    Language English
    Publishing date 2023-12-18
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.12.18.572243
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Retroviral RNase H: Structure, mechanism, and inhibition.

    Ilina, Tatiana V / Brosenitsch, Teresa / Sluis-Cremer, Nicolas / Ishima, Rieko

    The Enzymes

    2021  Volume 50, Page(s) 227–247

    Abstract: All retroviruses encode the enzyme, reverse transcriptase (RT), which is involved in the conversion of the single-stranded viral RNA genome into double-stranded DNA. RT is a multifunctional enzyme and exhibits DNA polymerase and ribonuclease H (RNH) ... ...

    Abstract All retroviruses encode the enzyme, reverse transcriptase (RT), which is involved in the conversion of the single-stranded viral RNA genome into double-stranded DNA. RT is a multifunctional enzyme and exhibits DNA polymerase and ribonuclease H (RNH) activities, both of which are essential to the reverse-transcription process. Despite the successful development of polymerase-targeting antiviral drugs over the last three decades, no bona fide inhibitor against the RNH activity of HIV-1 RT has progressed to clinical evaluation. In this review article, we describe the retroviral RNH function and inhibition, with primary consideration of the structural aspects of inhibition.
    MeSH term(s) DNA-Directed DNA Polymerase ; HIV-1/genetics ; HIV-1/metabolism ; Reverse Transcription ; Ribonuclease H/genetics ; Ribonuclease H/metabolism
    Chemical Substances DNA-Directed DNA Polymerase (EC 2.7.7.7) ; Ribonuclease H (EC 3.1.26.4)
    Language English
    Publishing date 2021-09-24
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0423-2607
    ISSN 0423-2607
    DOI 10.1016/bs.enz.2021.07.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Therapeutic Approaches to Eradicate Latent HIV-1 in Resting CD4+ T Cells.

    Sluis-Cremer, Nicolas

    Current topics in medicinal chemistry

    2015  Volume 16, Issue 10, Page(s) 1191–1197

    Abstract: While combination antiretroviral therapy (cART) can drive HIV-1 RNA levels to < 50 copies/mL in patient plasma, most infected individuals continue to harbor low-level persistent viremia. Latently infected resting CD4+ T cells are thought to constitute ... ...

    Abstract While combination antiretroviral therapy (cART) can drive HIV-1 RNA levels to < 50 copies/mL in patient plasma, most infected individuals continue to harbor low-level persistent viremia. Latently infected resting CD4+ T cells are thought to constitute the major reservoir of HIV-1 persistence. In this reservoir, the integrated provirus remains transcriptionally silent as long as the host cell is in a resting state. On discontinuation of cART, these viruses can reactivate and lead to waves of de novo infection events. The prevailing hypothesis in the field is that molecules that reactivate latent HIV-1 infection will purge this reservoir by inducing transcription of the latent provirus, thereby causing cells to undergo apoptosis. This review article summarizes the results of all therapeutic approaches that have been clinically evaluated for their potential to reverse HIV latency.
    MeSH term(s) Anti-HIV Agents/pharmacology ; Anti-HIV Agents/therapeutic use ; CD4-Positive T-Lymphocytes/cytology ; CD4-Positive T-Lymphocytes/drug effects ; CD4-Positive T-Lymphocytes/virology ; HIV Infections/drug therapy ; HIV Infections/virology ; HIV-1/drug effects ; HIV-1/physiology ; Humans ; Virus Latency/drug effects
    Chemical Substances Anti-HIV Agents
    Language English
    Publishing date 2015-09-01
    Publishing country United Arab Emirates
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2064823-6
    ISSN 1873-4294 ; 1568-0266
    ISSN (online) 1873-4294
    ISSN 1568-0266
    DOI 10.2174/1568026615666150901114138
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5572: 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)

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  10. Article: The HIV-1 capsid serves as a nanoscale reaction vessel for reverse transcription.

    Jennings, Jordan / Bracey, Harrison / Nguyen, Danny T / Dasgupta, Rishav / Rivera, Alondra Vázquez / Sluis-Cremer, Nicolas / Shi, Jiong / Aiken, Christopher

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The viral capsid performs critical functions during HIV-1 infection and is a validated target for antiviral therapy. Previous studies have established that the proper structure and stability of the capsid are required for efficient HIV-1 reverse ... ...

    Abstract The viral capsid performs critical functions during HIV-1 infection and is a validated target for antiviral therapy. Previous studies have established that the proper structure and stability of the capsid are required for efficient HIV-1 reverse transcription in target cells. Moreover, it has recently been demonstrated that permeabilized virions and purified HIV-1 cores undergo efficient reverse transcription in vitro when the capsid is stabilized by addition of the host cell metabolite inositol hexakisphosphate (IP6). However, the molecular mechanism by which the capsid promotes reverse transcription is undefined. Here we show that wild type HIV-1 particles can undergo efficient reverse transcription
    Language English
    Publishing date 2023-11-09
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.11.08.566350
    Database MEDical Literature Analysis and Retrieval System OnLINE

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