Artigos de revistas: "Transfrauen"

1

Wortmann, Martin. "Barthaarentfernung von Transfrauen: Privatabrechnung möglich". ästhetische dermatologie & kosmetologie 15, n.º 1 (fevereiro de 2023): 7. http://dx.doi.org/10.1007/s12634-022-2272-3.

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Pfeiffer, Jan. "LG Frankfurt a. M.: Persönlichkeitsrechte von Transfrauen im Internet". Computer und Recht 39, n.º 8 (1 de agosto de 2023): r90. http://dx.doi.org/10.9785/cr-2023-390806.

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Proufas, Nina, Karlsson Olberg e Jonas Simon Schöck. "Transpersonen im Sport – im Zweifel für die Inklusion?" TUP - Theorie und Praxis der Sozialen Arbeit, n.º 4 (1 de dezembro de 2022): 333–39. http://dx.doi.org/10.3262/tup2204333.

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Die Autor*innen haben sich im Rahmen eines Hochschul-Moduls zu den kulturwissenschaftlichen Grundlagen der Sozialen Arbeit mit dem Thema "Transfrauen im Sport" befasst. Ihre Überlegungen und Schlussfolgerungen präsentieren sie in Heft 4-2022 und Heft 1-2023 der TUP. Exklusion von Transpersonen im Sport wird sichtbar durch mannigfaltige Ausprägungen. Diese können in der Gesellschaft, dem Sport und dem Individuum selbst zum Ausdruck kommen. Barrieren wie vor allem die generelle binäre Geschlechterunterteilung erschweren den Zugang zu verschiedenen Sport- und Bewegungsbereichen. Daraus resultierend ergibt sich die mögliche Gefahr, dass die soziale Geschlechteridentität keine Beachtung findet, was am Beispiel eines binär verteilten Umkleideraumes als vormals geschützter Raum deutlich wird. Die Vernachlässigung des sozialen Geschlechts im Sport spiegelt sich in der rigiden binären biologischen Geschlechterunterteilung wider.

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G. Mildenberger, Florian. "Wolfert, Raimund, Charlotte Charlaque. Transfrau, Laienschauspielerin, „Königin der Brooklyn Heights Promenade“". Sexuologie. Zeitschrift für Sexualmedizin, Sexualtherapie und Sexualwissenschaft 29, n.º 3-4 (dezembro de 2022): 207–8. http://dx.doi.org/10.61387/hwbr1851.

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G. Mildenberger, Florian. "Wolfert, Raimund, Charlotte Charlaque. Transfrau, Laienschauspielerin, „Königin der Brooklyn Heights Promenade“". Sexuologie. Zeitschrift für Sexualmedizin, Sexualtherapie und Sexualwissenschaft 29, n.º 3-4 (dezembro de 2022): 207–8. http://dx.doi.org/10.61387/s.2022.34.53.

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6

Bleiber, Gabriela, Solange Peters, Raquel Martinez, Dusan Cmarko, Pascal Meylan e Amalio Telenti. "The central region of human immunodeficiency virus type 1 p6 protein (Gag residues S14–I31) is dispensable for the virus in vitro". Journal of General Virology 85, n.º 4 (1 de abril de 2004): 921–27. http://dx.doi.org/10.1099/vir.0.19576-0.

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The human immunodeficiency virus type 1 p6 region encodes p6Gag and the transframe p6Pol protein. The Gag frame encodes an N-terminal late assembly L domain and a C-terminal Vpr binding domain. In the Pol frame, substitution at a C-terminal motif decreases protease autocleavage. The role of the highly polymorphic central region of p6, comprising amino acids S14–I31 (p6Gag) and R20–D39 (p6Pol), is unclear. Analysis of this central region demonstrated that 35 % of p6Gag appears to be dispensable for virus propagation in vitro and smaller deletion and insertion polymorphisms can be tolerated in vivo. Extensive Pol deletion (ΔR20–D39, 42 % of p6Pol) did not alter protease autocleavage.

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7

Yu, Fu-Hsien, Kuo-Jung Huang e Chin-Tien Wang. "Amino acid substitutions at the HIV-1 transframe region significantly impair virus infectivity". PLOS ONE 17, n.º 1 (27 de janeiro de 2022): e0262477. http://dx.doi.org/10.1371/journal.pone.0262477.

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A transframe region within HIV-1 Gag-Pol (referred to as p6* or p6pol), directly linked to the protease (PR) N-terminus, plays a pivotal role in modulating PR activation. To identify specific p6* residues involved in PR activation, we created a series of p6* mutants by making substitutions for conserved p6* residues. Our results indicate that some p6* mutants were defective in terms of virus infectivity, despite displaying a wild-type virus particle processing pattern. Mutations at p6* F8 reduced virus infectivity associated with insufficient virus processing, due in part to impaired PR maturation and RT packaging. Our data strongly suggest that conserved Phe (F) residues at position 8 of p6* are involved in the PR maturation process.

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Huang, Liangqun, Jane M. Sayer, Marie Swinford, John M. Louis e Chaoping Chen. "Modulation of Human Immunodeficiency Virus Type 1 Protease Autoprocessing by Charge Properties of Surface Residue 69". Journal of Virology 83, n.º 15 (20 de maio de 2009): 7789–93. http://dx.doi.org/10.1128/jvi.00473-09.

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ABSTRACT Mature, fully active human immunodeficiency virus protease (PR) is liberated from the Gag-Pol precursor via regulated autoprocessing. A chimeric protease precursor, glutathione S-transferase-transframe region (TFR)-PR-FLAG, also undergoes N-terminal autocatalytic maturation when it is expressed in Escherichia coli. Mutation of the surface residue H69 to glutamic acid, but not to several neutral or basic amino acids, impedes protease autoprocessing in bacteria and mammalian cells. Only a fraction of mature PR with an H69E mutation (PRH69E) folds into active enzymes, and it does so with an apparent Kd (dissociation constant) significantly higher than that of the wild-type protease, corroborating the marked retardation of the in vitro N-terminal autocatalytic processing of TFR-PRH69E and suggesting a folding defect in the precursor.

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9

Yu, Fu-Hsien, Ting-An Chou, Wei-Hao Liao, Kuo-Jung Huang e Chin-Tien Wang. "Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation". PLOS ONE 10, n.º 6 (1 de junho de 2015): e0127974. http://dx.doi.org/10.1371/journal.pone.0127974.

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10

Chiu, Hsu-Chen, Fu-Der Wang, Yi-Ming Arthur Chen e Chin-Tien Wang. "Effects of human immunodeficiency virus type 1 transframe protein p6* mutations on viral protease-mediated Gag processing". Journal of General Virology 87, n.º 7 (1 de julho de 2006): 2041–46. http://dx.doi.org/10.1099/vir.0.81601-0.

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The proteolytic processing of human immunodeficiency virus (HIV) particles mediated by the viral pol-encoded protease (PR) is essential for viral infectivity. The pol coding sequence partially overlaps with the gag coding sequence and is translated as a Gag–Pol polyprotein precursor. Within Gag–Pol, the C-terminal p6 gag domain is replaced by a transframe peptide referred to as p6*, which separates the Gag nucleocapsid domain from PR. Several previous in vitro studies have ascribed a PR-suppression regulatory function to p6*. Here, it was demonstrated that an HIV-1 Gag–Pol lacking p6* is efficiently incorporated into virions when coexpressed with HIV-1 Gag precursor. However, the released virions are not processed appropriately and show a greatly reduced viral infectivity. This suggests that the p6* is indispensable during the process of PR-mediated virus particle maturation.

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11

Paulus, Christina, Susanne Hellebrand, Uwe Tessmer, Hans Wolf, Hans-Georg Kräusslich e Ralf Wagner. "Competitive Inhibition of Human Immunodeficiency Virus Type-1 Protease by the Gag-Pol Transframe Protein". Journal of Biological Chemistry 274, n.º 31 (30 de julho de 1999): 21539–43. http://dx.doi.org/10.1074/jbc.274.31.21539.

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12

Louis, John M., Fred Dyda, Nashaat T. Nashed, Alan R. Kimmel e David R. Davies. "Hydrophilic Peptides Derived from the Transframe Region of Gag-Pol Inhibit the HIV-1 Protease†". Biochemistry 37, n.º 8 (fevereiro de 1998): 2105–10. http://dx.doi.org/10.1021/bi972059x.

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13

J. Dinsmore, Christopher. "Preface by Christopher J. Dinsmore (Hot Topic: Farnesyl-Protein Transfrase Inhibitors Guest Editor: Christopher J. Dinsmore". Current Topics in Medicinal Chemistry 3, n.º 10 (1 de maio de 2003): i. http://dx.doi.org/10.2174/1568026033452041.

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J. Dinsmore, C. "Preface by Christopher J. Dinsmore (Hot Topic: Farnesyl-Protein Transfrase Inhibitors Guest Editor: Christopher J. Dinsmore". Current Topics in Medicinal Chemistry 3, n.º 10 (1 de junho de 2003): 1. http://dx.doi.org/10.2174/1568026033452069.

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15

Dautin, Nathalie, Gouzel Karimova e Daniel Ladant. "Human Immunodeficiency Virus (HIV) Type 1 Transframe Protein Can Restore Activity to a Dimerization-Deficient HIV Protease Variant". Journal of Virology 77, n.º 15 (1 de agosto de 2003): 8216–26. http://dx.doi.org/10.1128/jvi.77.15.8216-8226.2003.

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ABSTRACT The protease (PR) from human immunodeficiency virus (HIV) is essential for viral replication: this aspartyl protease, active only as a dimer, is responsible for cleavage of the viral polyprotein precursors (Gag and Gag-Pol), to release the functional mature proteins. In this work, we have studied the structure-function relationships of the HIV PR by combining a genetic test to detect proteolytic activity in Escherichia coli and a bacterial two-hybrid assay to analyze PR dimerization. We showed that a drug-resistant PR variant isolated from a patient receiving highly active antiretroviral therapy is impaired in its dimerization capability and, as a consequence, is proteolytically inactive. We further showed that the polypeptide regions adjacent to the PR coding sequence in the Gag-Pol polyprotein precursor, and in particular, the transframe polypeptide (TF), located at the N terminus of PR, can facilitate the dimerization of this variant PR and restore its enzymatic activity. We propose that the TF protein could help to compensate for folding and/or dimerization defects in PR arising from certain mutations within the PR coding sequence and might therefore function to buffer genetic variations in PR.

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Al- Taee, Nihal E., Sajida A. Abood e Mozahim K. Al-Mallah. "Specific activity of thymidine nucleotide biosynthetic enzymes in hairy roots extracts of Sesamum indicum L. transformed by two strains of Agrobacteruim rhizogenes". Journal of Biotechnology Research Center 8, n.º 2 (1 de junho de 2014): 64–72. http://dx.doi.org/10.24126/jobrc.2014.8.2.334.

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The study concluded induction of transformed hairy roots from leaves and decapitated seedlings of Sesamum indicum L. using two strains of Agrobacterium rhizogenes considered as natural vector of transformation. The strain R1601 stimulated roots on leaves and seedlings during 20 days of inoculation placed on solidified Arnon and Hoagland medium. Whereas they involved 12 days when inoculated with the strain R15834. Generally strain R15834 was efficient in inducing these roots and their numbers than strain R1601 which approached 54.4% and 41.6% respectively. The results indicated an increase in the specific activity of enzymes Thymidlate synthase (TS), Dihydrofolate reductase (DHFR), Serine hydroxy methyl transfrase (SHMT) in extract of transformed hairy roots producing agropine by stain R15834 and approach 4.610, 1.057, 0.480 µmolmin mg of protein respectively compared with the activity of 1.256, 0.097, 0.125µ molmin mg in the control samples. This was coupled with an increase in amount of DNA and RNA that approached 105, 1020 µg per gram respectively compared to 44, 462 µg per gram in control samples. The transformation of these hairy roots was pointed out through the separation of agropine spots from their extracts when electrophoreted in the presence of standared agropine.

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17

Saulquin, Xavier, Emmanuel Scotet, Lydie Trautmann, Marie-Alix Peyrat, Franck Halary, Marc Bonneville e Elisabeth Houssaint. "+1 Frameshifting as a Novel Mechanism to Generate a Cryptic Cytotoxic T Lymphocyte Epitope Derived from Human Interleukin 10". Journal of Experimental Medicine 195, n.º 3 (4 de fevereiro de 2002): 353–58. http://dx.doi.org/10.1084/jem.20011399.

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Recent data indicate that some cytotoxic T cells (CTLs) recognize so-called cryptic epitopes, encoded by nonprimary open reading frame (ORF) sequences or other nonclassical expression pathways. We describe here a novel mechanism leading to generation of a cryptic CTL epitope. We isolated from the synovial fluid of a patient suffering from a Reiter's syndrome an autoreactive T cell clone that recognized cellular IL-10 in the HLA-B*2705 context. The minimal IL-10 sequence corresponding to nucleotides 379–408 was shown to activate this clone, upon cotransfection into COS cells with the DNA encoding HLA-B*2705, but the synthetic peptide deduced from this sequence did not stimulate the clone. Using a site-directed mutagenesis approach, we found that this clone recognized a transframe epitope generated by an internal +1 frameshifting in the IL-10 sequence and so derived partly from ORF1, partly from ORF2. We defined that +1 frameshifting was induced by a specific heptamer sequence. These observations illustrate the variety of mechanisms leading to generation of cryptic epitopes and suggest that frameshifting in normal cellular genes may be more common than expected.

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18

Sei, Shizuko, Quan-en Yang, Dennis O'Neill, Kazuhisa Yoshimura, Kunio Nagashima e Hiroaki Mitsuya. "Identification of a Key Target Sequence To Block Human Immunodeficiency Virus Type 1 Replication within thegag-pol Transframe Domain". Journal of Virology 74, n.º 10 (2000): 4621–33. http://dx.doi.org/10.1128/.74.10.4621-4633.2000.

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Sei, Shizuko, Quan-en Yang, Dennis O'Neill, Kazuhisa Yoshimura, Kunio Nagashima e Hiroaki Mitsuya. "Identification of a Key Target Sequence To Block Human Immunodeficiency Virus Type 1 Replication within thegag-pol Transframe Domain". Journal of Virology 74, n.º 10 (15 de maio de 2000): 4621–33. http://dx.doi.org/10.1128/jvi.74.10.4621-4633.2000.

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ABSTRACT Although the full sequence of the human immunodeficiency virus type 1 (HIV-1) genome has been known for more than a decade, effective genetic antivirals have yet to be developed. Here we show that, of 22 regions examined, one highly conserved sequence (ACTCTTTGGCAACGA) near the 3′ end of the HIV-1 gag-poltransframe region, encoding viral protease residues 4 to 8 and a C-terminal Vpr-binding motif of p6Gag protein in two different reading frames, can be successfully targeted by an antisense peptide nucleic acid oligomer named PNAPR2. A disrupted translation of gag-pol mRNA induced at the PNAPR2-annealing site resulted in a decreased synthesis of Pr160Gag-Pol polyprotein, hence the viral protease, a predominant expression of Pr55Gag devoid of a fully functional p6Gag protein, and the excessive intracellular cleavage of Gag precursor proteins, hindering the processes of virion assembly. Treatment with PNAPR2abolished virion production by up to 99% in chronically HIV-1-infected H9 cells and in peripheral blood mononuclear cells infected with clinical HIV-1 isolates with the multidrug-resistant phenotype. This particular segment of the gag-pol transframe gene appears to offer a distinctive advantage over other regions in invading viral structural genes and restraining HIV-1 replication in infected cells and may potentially be exploited as a novel antiviral genetic target.

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SEKINO, N. "IS1-encoded proteins, InsA and the InsA-B?-InsB transframe protein (transposase): Functions deduced from their DNA-binding ability". Advances in Biophysics 31 (1995): 209–22. http://dx.doi.org/10.1016/0065-227x(95)99393-4.

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21

Cao, Jianhong, John McNevin, Matthew McSweyn, Yi Liu, James I. Mullins e M. Juliana McElrath. "Novel Cytotoxic T-Lymphocyte Escape Mutation by a Three-Amino-Acid Insertion in the Human Immunodeficiency Virus Type 1 p6Pol and p6Gag Late Domain Associated with Drug Resistance". Journal of Virology 82, n.º 1 (17 de outubro de 2007): 495–502. http://dx.doi.org/10.1128/jvi.01096-07.

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ABSTRACT Cytolytic T lymphocytes (CTL) play a major role in controlling human immunodeficiency virus type 1 (HIV-1) infection. To evade immune pressure, HIV-1 is selected at targeted CTL epitopes, which may consequentially alter viral replication fitness. In our longitudinal investigations of the interplay between T-cell immunity and viral evolution following acute HIV-1 infection, we observed in a treatment-naïve patient the emergence of highly avid, gamma interferon-secreting, CD8+ CTL recognizing an HLA-Cw*0102-restricted epitope, NSPTRREL (NL8). This epitope lies in the p6Pol protein, located in the transframe region of the Gag-Pol polyprotein. Over the course of infection, an unusual viral escape mutation arose within the p6Pol epitope through insertion of a 3-amino-acid repeat, NSPT(SPT)RREL, with a concomitant insertion in the p6Gag late domain, PTAPP(APP). Interestingly, this p6Pol insertion mutation is often selected in viruses with the emergence of antiretroviral drug resistance, while the p6Gag late-domain PTAPP motif binds Tsg101 to permit viral budding. These results are the first to demonstrate viral evasion of immune pressure by amino acid insertions. Moreover, this escape mutation represents a novel mechanism whereby HIV-1 can alter its sequence within both the Gag and Pol proteins with potential functional consequences for viral replication and budding.

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Köppe, B., L. Menéndez-Arias e S. Oroszlan. "Expression and purification of the mouse mammary tumor virus gag-pro transframe protein p30 and characterization of its dUTPase activity." Journal of Virology 68, n.º 4 (1994): 2313–19. http://dx.doi.org/10.1128/jvi.68.4.2313-2319.1994.

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23

Leiherer, Andreas, Christine Ludwig e Ralf Wagner. "Influence of extended mutations of the HIV-1 transframe protein p6⁎ on Nef-dependent viral replication and infectivity in vitro". Virology 387, n.º 1 (abril de 2009): 200–210. http://dx.doi.org/10.1016/j.virol.2009.01.042.

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Leiherer, Andreas, Christine Ludwig e Ralf Wagner. "Uncoupling Human Immunodeficiency Virus Type 1 gag and pol Reading Frames: Role of the Transframe Protein p6* in Viral Replication". Journal of Virology 83, n.º 14 (29 de abril de 2009): 7210–20. http://dx.doi.org/10.1128/jvi.02603-08.

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ABSTRACT Apart from its regulatory role in protease (PR) activation, little is known about the function of the human immunodeficiency virus type 1 transframe protein p6* in the virus life cycle. p6* is located between the nucleocapsid and PR domains in the Gag-Pol polyprotein precursor and is cleaved by PR during viral maturation. We have recently reported that the central region of p6* can be extensively mutated without abolishing viral infectivity and replication in vitro. However, mutagenesis of the entire p6*-coding sequence in the proviral context is not feasible without affecting the superimposed frameshift signal or the overlapping p1-p6gag sequences. To overcome these limitations, we created a novel NL4-3-derived provirus by displacing the original frameshift signal to the 3′ end of the gag gene, thereby uncoupling the p6* gene sequence from the p1-p6gag reading frame. The resulting virus (AL) proved to be replication competent in different cell cultures and thus represents an elegant tool for detailed analysis of p6* function. Hence, extensive deletions or substitutions were introduced into the p6* gene sequence of the AL provirus, and effects on particle release, protein processing, and viral infectivity were evaluated. Interestingly, neither the deletion of 63% of all p6* residues nor the partial substitution by a heterologous sequence affected virus growth and infectivity, suggesting that p6* is widely dispensable for viral in vitro replication. However, the insertion of a larger reporter sequence interfered with virus production and maturation, implying that the length or conformation of this spacer region might be critical for p6* function.

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Trentin, Bernadette, Nicole Rebeyrotte e Robert Z. Mamoun. "Human T-Cell Leukemia Virus Type 1 Reverse Transcriptase (RT) Originates from the pro andpol Open Reading Frames and Requires the Presence of RT-RNase H (RH) and RT-RH-Integrase Proteins for Its Activity". Journal of Virology 72, n.º 8 (1 de agosto de 1998): 6504–10. http://dx.doi.org/10.1128/jvi.72.8.6504-6510.1998.

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ABSTRACT The first description of an active form of a recombinant human T-cell leukemia virus type 1 (HTLV-1) reverse transcriptase (RT) and subsequent predictions of its amino acid sequence and quaternary structure are reported here. By using amino acid alignment methods, the NH2 and COOH termini of the RT, RNase H (RH), and integrase (IN) domains of the Pol polyprotein were determined. The HTLV-1 RT seems to be unique since its NH2 terminus is probably encoded by the pro open reading frame (ORF) fused downstream, via a transframe peptide, to the polypeptide encoded by the pol ORF. The HTLV-1 Pol amino acid sequence was revealed to be highly similar to that of Rous sarcoma virus (RSV), particularly at the RT-RH hinge region. These two domains remain linked for RSV; this may also be the case for HTLV-1. In light of these results, RT, RT-RH, and RT-RH-IN genes were constructed and introduced into His-tagged protein expression vectors. The corresponding proteins were synthesized in vitro, and the DNA polymerase activities of different protein combinations were tested. Solely the RT-RH–RT-RH-IN combination was found to have a significant activity level. Velocity sedimentation analysis suggested that the HTLV-1 RT-RH and RT-RH-IN monomers are likely associated in an oligomeric structure, probably of the α3/β type.

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Pettit, Steven C., Sergei Gulnik, Lori Everitt e Andrew H. Kaplan. "The Dimer Interfaces of Protease and Extra-Protease Domains Influence the Activation of Protease and the Specificity of GagPol Cleavage". Journal of Virology 77, n.º 1 (1 de janeiro de 2003): 366–74. http://dx.doi.org/10.1128/jvi.77.1.366-374.2003.

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ABSTRACT Activation of the human immunodeficiency virus type 1 (HIV-1) protease is an essential step in viral replication. As is the case for all retroviral proteases, enzyme activation requires the formation of protease homodimers. However, little is known about the mechanisms by which retroviral proteases become active within their precursors. Using an in vitro expression system, we have examined the determinants of activation efficiency and the order of cleavage site processing for the protease of HIV-1 within the full-length GagPol precursor. Following activation, initial cleavage occurs between the viral p2 and nucleocapsid proteins. This is followed by cleavage of a novel site located in the transframe domain. Mutational analysis of the dimer interface of the protease produced differential effects on activation and specificity. A subset of mutations produced enhanced cleavage at the amino terminus of the protease, suggesting that, in the wild-type precursor, cleavages that liberate the protease are a relatively late event. Replacement of the proline residue at position 1 of the protease dimer interface resulted in altered cleavage of distal sites and suggests that this residue functions as a cis-directed specificity determinant. In summary, our studies indicate that interactions within the protease dimer interface help determine the order of precursor cleavage and contribute to the formation of extended-protease intermediates. Assembly domains within GagPol outside the protease domain also influence enzyme activation.

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Beissinger, Martina, Christina Paulus, Peter Bayer, Hans Wolf, Paul Rosch e Ralf Wagner. "Sequence-Specific Resonance Assignments of the 1H-NMR Spectra and Structural Characterization in Solution of the HIV-1 Transframe Protein p6*". European Journal of Biochemistry 237, n.º 2 (15 de abril de 1996): 383–92. http://dx.doi.org/10.1111/j.1432-1033.1996.0383k.x.

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Paulus, Christina, Christine Ludwig e Ralf Wagner. "Contribution of the Gag-Pol transframe domain p6* and its coding sequence to morphogenesis and replication of human immunodeficiency virus type 1". Virology 330, n.º 1 (dezembro de 2004): 271–83. http://dx.doi.org/10.1016/j.virol.2004.09.013.

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Ludwig, Christine, Andreas Leiherer e Ralf Wagner. "Importance of Protease Cleavage Sites within and Flanking Human Immunodeficiency Virus Type 1 Transframe Protein p6* for Spatiotemporal Regulation of Protease Activation". Journal of Virology 82, n.º 9 (5 de março de 2008): 4573–84. http://dx.doi.org/10.1128/jvi.02353-07.

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ABSTRACT The human immunodeficiency virus type 1 (HIV-1) protease (PR) has recently been shown to be inhibited by its propeptide p6* in vitro. As p6* itself is a PR substrate, the primary goal of this study was to determine the importance of p6* cleavage for HIV-1 maturation and infectivity. For that purpose, short peptide variants mimicking proposed cleavage sites within and flanking p6* were designed and analyzed for qualitative and quantitative hydrolysis in vitro. Proviral clones comprising the selected cleavage site mutations were established and analyzed for Gag and Pol processing, virus maturation, and infectivity in cultured cells. Amino-terminal cleavage site mutation caused aberrant processing of nucleocapsid proteins and delayed replication kinetics. Blocking the internal cleavage site resulted in the utilization of a flanking site at a significantly decreased hydrolysis rate in vitro, which however did not affect Gag-Pol processing and viral replication. Although mutations blocking cleavage at the p6* carboxyl terminus yielded noninfectious virions exhibiting severe Gag processing defects, mutations retarding hydrolysis of this cleavage site neither seemed to impact viral infectivity and propagation in cultured cells nor seemed to interfere with overall maturation of released viruses. Interestingly, these mutants were shown to be clearly disadvantaged when challenged with wild-type virus in a dual competition assay. In sum, we conclude that p6* cleavage is absolutely essential to allow complete activation of the PR and subsequent processing of the viral precursors.

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Bartosik, Dariusz, Michal Szymanik e Jadwiga Baj. "Identification and Distribution of Insertion Sequences of Paracoccus solventivorans". Applied and Environmental Microbiology 69, n.º 12 (dezembro de 2003): 7002–8. http://dx.doi.org/10.1128/aem.69.12.7002-7008.2003.

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ABSTRACT Three novel insertion sequences (ISs) (ISPso1, ISPso2, and ISPso3) of the soil bacterium Paracoccus solventivorans DSM 11592 were identified by transposition into entrapment vector pMEC1. ISPso1 (1,400 bp) carries one large open reading frame (ORF) encoding a putative basic protein (with a DDE motif conserved among transposases [Tnps] of elements belonging to the IS256 family) with the highest levels of similarity with the hypothetical Tnps of Rhodospirillum rubrum and Sphingopyxis macrogoltabida. ISPso2 (832 bp) appeared to be closely related to ISPpa2 of Paracoccus pantotrophus DSM 11072 and IS1248 of Paracoccus denitrificans PdX22, both of which belong to the IS427 group (IS5 family). These elements contain two overlapping ORFs and a putative frameshift motif (AAAAG) responsible for production of a putative transframe Tnp. ISPso3 (1,286 bp) contains a single ORF, whose putative product showed homology with Tnps of ISs classified as members of a distinct subgroup of the IS5 group of the IS5 family. The highest levels of similarity were observed with ISSsp126 of Sphingomonas sp. and IS1169 of Bacteroides fragilis. Analysis of the distribution of ISs of P. solventivorans revealed that ISPso2-like elements are the most widely spread of the elements in nine species of the genus Paracoccus. ISPso1 and ISPso3 are present in only a few paracoccal strains, which suggests that they were acquired by lateral transfer. Phylogenetic analysis of Tnps of the novel ISs and their closest relatives showed their evolutionary relationships and possible directions of lateral transfer between various bacterial hosts.

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Costa, Luciana J., Yong-Hui Zheng, Jerica Sabotic, Johnson Mak, Oliver T. Fackler e B. Matija Peterlin. "Nef Binds p6* in GagPol during Replication of Human Immunodeficiency Virus Type 1". Journal of Virology 78, n.º 10 (15 de maio de 2004): 5311–23. http://dx.doi.org/10.1128/jvi.78.10.5311-5323.2004.

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ABSTRACT The atypical Nef protein (NefF12) from human immunodeficiency virus type 1 strain F12 (HIV-1F12) interferes with virion production and infectivity via a mysterious mechanism. The correlation of these effects with the unusual perinuclear subcellular localization of NefF12 suggested that the wild-type Nef protein could bind to assembly intermediates in late stages of viral replication. To test this hypothesis, Nef from HIV-1NL4-3 was fused to an endoplasmic reticulum (ER) retention signal (NefKKXX). This mutant NefKKXX protein recapitulated fully the effects of NefF12 on Gag processing and virion production, either alone or as a CD8 fusion protein. Importantly, the mutant NefKKXX protein also localized to the intermediate compartment, between the ER and the trans-Golgi network. Furthermore, Nef bound the GagPol polyprotein in vitro and in vivo. This binding mapped to the C-terminal flexible loop in Nef and the transframe p6* protein in GagPol. The significance of this interaction was demonstrated by a genetic assay in which the release of a mutant HIV-1 provirus lacking the PTAP motif in the late domain that no longer binds Tsg101 was rescued by a Nef.Tsg101 chimera. Importantly, this rescue as well as incorporation of Nef into HIV-1 virions correlated with the ability of Nef to interact with GagPol. Our data demonstrate that the retention of Nef in the intermediate compartment interferes with viral replication and suggest a new role for Nef in the production of HIV-1.

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Heidecker, Gisela, Shawn Hill, Patricia A. Lloyd e David Derse. "A Novel Protease Processing Site in the Transframe Protein of Human T-Cell Leukemia Virus Type 1 PR76gag-pro Defines the N Terminus of RT". Journal of Virology 76, n.º 24 (15 de dezembro de 2002): 13101–5. http://dx.doi.org/10.1128/jvi.76.24.13101-13105.2002.

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ABSTRACT The genomic RNA of human T-cell leukemia virus type 1 encodes three polyproteins, Gag, Gag-Pro, and Gag-Pro-Pol, which are translated as a result of no, one, and two frameshifts, respectively. In this report we demonstrate that the 77 residues encoded at the C terminus of the Gag-Pro precursor can be collectively detected as an 8-kDa transframe protein (TFP) in virions. Mutant viruses with a C-terminally truncated TFP (19, 32, or 50 residues) had essentially a wild-type phenotype in vitro. However, a virus mutant that encoded only the Gag and Gag-Pro-Pol polyproteins due to a mutation in the second frameshift site, and hence did not produce TFP, was noninfectious. Mutation analysis of the proteolytic cleavage site between PR and TFP revealed the presence of an additional site and the existence of a p1 peptide separating protease and TFP. While removal of the cleavage site at the PR-p1 junction had a modest effect on virus replication, mutation of the p1-TFP cleavage site led to noninfectious virus and the loss of reverse transcriptase activity. Determination of the amino-terminal sequence of a hemagglutinin-tagged RT demonstrated that the same site is used in processing the Gag-Pro-Pol precursor and thus defines the start of mature RT. Neither mutation alone or in combination caused changes in the amounts or processing patterns of the Gag polyprotein, indicating that protease is active independent of its C terminus.

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Kobbi, L., J. Dias, G. Octobre, M. Comisso, M. Kaminska, V. F. Shalak e M. Mirande. "Association of mitochondrial lysyl-tRNA synthetase with HIV-1 GagPol involves catalytic domain of the synthetase and transframe and integrase domains of Pol". Biopolymers and Cell 27, n.º 5 (20 de setembro de 2011): 381–82. http://dx.doi.org/10.7124/bc.000128.

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Kobbi, Lydia, Guillaume Octobre, José Dias, Martine Comisso e Marc Mirande. "Association of Mitochondrial Lysyl-tRNA Synthetase with HIV-1 GagPol Involves Catalytic Domain of the Synthetase and Transframe and Integrase Domains of Pol". Journal of Molecular Biology 410, n.º 5 (julho de 2011): 875–86. http://dx.doi.org/10.1016/j.jmb.2011.03.005.

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Peters, Solange, Miguel Muñoz, Sabine Yerly, Victor Sanchez-Merino, Cecilio Lopez-Galindez, Luc Perrin, Brendan Larder et al. "Resistance to Nucleoside Analog Reverse Transcriptase Inhibitors Mediated by Human Immunodeficiency Virus Type 1 p6 Protein". Journal of Virology 75, n.º 20 (15 de outubro de 2001): 9644–53. http://dx.doi.org/10.1128/jvi.75.20.9644-9653.2001.

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ABSTRACT Resistance of human immunodeficiency virus type 1 (HIV-1) to antiretroviral agents results from target gene mutation within thepol gene, which encodes the viral protease, reverse transcriptase (RT), and integrase. We speculated that mutations in genes other that the drug target could lead to drug resistance. For this purpose, the p1-p6 gag -p6 pol region of HIV-1, placed immediately upstream ofpol, was analyzed. This region has the potential to alter Pol through frameshift regulation (p1), through improved packaging of viral enzymes (p6Gag), or by changes in activation of the viral protease (p6Pol). Duplication of the proline-rich p6Gag PTAP motif, necessary for late viral cycle activities, was identified in plasma virus from 47 of 222 (21.2%) patients treated with nucleoside analog RT inhibitor (NRTI) antiretroviral therapy but was identified very rarely from drug-naı̈ve individuals. Molecular clones carrying a 3-amino-acid duplication, APPAPP (transframe duplication SPTSPT in p6Pol), displayed a delay in protein maturation; however, they packaged a 34% excess of RT and exhibited a marked competitive growth advantage in the presence of NRTIs. This phenotype is reminiscent of the inoculum effect described in bacteriology, where a larger input, or a greater infectivity of an organism with a wild-type antimicrobial target, leads to escape from drug pressure and a higher MIC in vitro. Though the mechanism by which the PTAP region participates in viral maturation is not known, duplication of this proline-rich motif could improve assembly and packaging at membrane locations, resulting in the observed phenotype of increased infectivity and drug resistance.

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Hill, Melissa K., Miranda Shehu-Xhilaga, Suzanne M. Crowe e Johnson Mak. "Proline Residues within Spacer Peptide p1 Are Important for Human Immunodeficiency Virus Type 1 Infectivity, Protein Processing, and Genomic RNA Dimer Stability". Journal of Virology 76, n.º 22 (15 de novembro de 2002): 11245–53. http://dx.doi.org/10.1128/jvi.76.22.11245-11253.2002.

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ABSTRACT The full-length human immunodeficiency virus type 1 (HIV-1) mRNA encodes two precursor polyproteins, Gag and GagProPol. An infrequent ribosomal frameshifting event allows these proteins to be synthesized from the same mRNA in a predetermined ratio of 20 Gag proteins for each GagProPol. The RNA frameshift signal consists of a slippery sequence and a hairpin stem-loop whose thermodynamic stability has been shown in in vitro translation systems to be critical to frameshifting efficiency. In this study we examined the frameshift region of HIV-1, investigating the effects of altering stem-loop stability in the context of the complete viral genome and assessing the role of the Gag spacer peptide p1 and the GagProPol transframe (TF) protein that are encoded in this region. By creating a series of frameshift region mutants that systematically altered the stability of the frameshift stem-loop and the protein sequences of the p1 spacer peptide and TF protein, we have demonstrated the importance of stem-loop thermodynamic stability in frameshifting efficiency and viral infectivity. Multiple changes to the amino acid sequence of p1 resulted in altered protein processing, reduced genomic RNA dimer stability, and abolished viral infectivity. The role of the two highly conserved proline residues in p1 (position 7 and 13) was also investigated. Replacement of the two proline residues by leucines resulted in mutants with altered protein processing and reduced genomic RNA dimer stability that were also noninfectious. The unique ability of proline to confer conformational constraints on a peptide suggests that the correct folding of p1 may be important for viral function.

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de Oliveira, Tulio, Susan Engelbrecht, Estrelita Janse van Rensburg, Michelle Gordon, Karen Bishop, Jan zur Megede, Susan W. Barnett e Sharon Cassol. "Variability at Human Immunodeficiency Virus Type 1 Subtype C Protease Cleavage Sites: an Indication of Viral Fitness?" Journal of Virology 77, n.º 17 (1 de setembro de 2003): 9422–30. http://dx.doi.org/10.1128/jvi.77.17.9422-9430.2003.

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ABSTRACT Naturally occurring polymorphisms in the protease of human immunodeficiency virus type 1 (HIV-1) subtype C would be expected to lead to adaptive (compensatory) changes in protease cleavage sites. To test this hypothesis, we examined the prevalences and patterns of cleavage site polymorphisms in the Gag, Gag-Pol, and Nef cleavage sites of C compared to those in non-C subtypes. Codon-based maximum-likelihood methods were used to assess the natural selection and evolutionary history of individual cleavage sites. Seven cleavage sites (p17/p24, p24/p2, NC/p1, NC/TFP, PR/RT, RT/p66, and p66/IN) were well conserved over time and in all HIV-1 subtypes. One site (p1/p6 gag ) exhibited moderate variation, and four sites (p2/NC, TFP/p6 pol , p6 pol /PR, and Nef) were highly variable, both within and between subtypes. Three of the variable sites are known to be major determinants of polyprotein processing and virion production. P2/NC controls the rate and order of cleavage, p6 gag is an important phosphoprotein required for virion release, and TFP/p6 pol , a novel cleavage site in the transframe domain, influences the specificity of Gag-Pol processing and the activation of protease. Overall, 58.3% of the 12 HIV-1 cleavage sites were significantly more diverse in C than in B viruses. When analyzed as a single concatenated fragment of 360 bp, 96.0% of group M cleavage site sequences fell into subtype-specific phylogenetic clusters, suggesting that they coevolved with the virus. Natural variation at C cleavage sites may play an important role, not only in regulation of the viral cycle but also in disease progression and response to therapy.

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Nadimpalli, R. G., W. Zhang, J. Kececioglu e E. W. Taylor. "The HIV-1 nef transframe protein has significant sequence and structural similarity to chemokines, as assessed by threading (inverse folding), sequence analysis, and molecular modeling". Antiviral Research 34, n.º 2 (abril de 1997): A57. http://dx.doi.org/10.1016/s0166-3542(97)83193-2.

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Cheng, Ting-Jen, Ashraf Brik, Chi-Huey Wong e Chen-Chen Kan. "Model System for High-Throughput Screening of Novel Human Immunodeficiency Virus Protease Inhibitors in Escherichia coli". Antimicrobial Agents and Chemotherapy 48, n.º 7 (julho de 2004): 2437–47. http://dx.doi.org/10.1128/aac.48.7.2437-2447.2004.

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ABSTRACT Novel human immunodeficiency virus (HIV) protease inhibitors are urgently needed for combating the drug-resistance problem in the fight against AIDS. To facilitate lead discovery of HIV protease inhibitors, we have developed a safe, convenient, and cost-effective Escherichia coli-based assay system. This E. coli-based system involves coexpression of an engineered β-galactosidase as an HIV protease substrate and the HIV protease precursor comprising the transframe region and the protease domain. Autoprocessing of the HIV protease precursor releases the mature HIV protease. Subsequently, the HIV protease cleaves β-galactosidase, resulting in a loss of the β-galactosidase activity, which can be detected in high-throughput screens. Using Food and Drug Administration-approved HIV protease inhibitors, this E. coli-based system is validated as a surrogate screening system for identifying inhibitors that not only possess inhibitory activity against HIV protease but also have solubility and permeability for in vivo activity. The usefulness of the E. coli-based system was demonstrated with the identification of a novel HIV protease inhibitor from a library of compounds that were prepared by an amide-forming reaction with transition-state analog cores. A novel inhibitor with a sulfonamide core of amprenavir, E2, has shown good correlation with the in vitro enzymatic assay and in vivo E. coli-based system. This system can also be used to generate drug resistance profiles that could be used to suggest therapeutic uses of HIV protease inhibitors to treat the drug-resistant HIV strains. This simple yet efficient E. coli system not only represents a screening platform for high-throughput identification of leads targeting the HIV proteases but also can be adapted to all other classes of proteases.

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Ziaei, Mahboobeh, Jaleh Tahsili, Mozafar Sharifi, Mehrdad Behmanesh e Khadijeh Razavi. "Gene expression of phenyl alanine ammonia-lyase (PAL), chavicol O-methyle transfrase (CVOMT) and eugenol O-methyle transferase (EOMT) in Ocimume basilicum at different stages of growth". Journal of Biotechnology 136 (outubro de 2008): S55—S56. http://dx.doi.org/10.1016/j.jbiotec.2008.07.118.

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Taylor, Adam, Julian V. Melton, Lara J. Herrero, Bastian Thaa, Liis Karo-Astover, Peter W. Gage, Michelle A. Nelson et al. "Effects of an In-Frame Deletion of the6kGene Locus from the Genome of Ross River Virus". Journal of Virology 90, n.º 8 (10 de fevereiro de 2016): 4150–59. http://dx.doi.org/10.1128/jvi.03192-15.

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ABSTRACTThe alphaviral6kgene region encodes the two structural proteins 6K protein and, due to a ribosomal frameshift event, the transframe protein (TF). Here, we characterized the role of the6kproteins in the arthritogenic alphavirus Ross River virus (RRV) in infected cells and in mice, using a novel6kin-frame deletion mutant. Comprehensive microscopic analysis revealed that the6kproteins were predominantly localized at the endoplasmic reticulum of RRV-infected cells. RRV virions that lack the6kproteins 6K and TF [RRV-(Δ6K)] were more vulnerable to changes in pH, and the corresponding virus had increased sensitivity to a higher temperature. While the6kdeletion did not reduce RRV particle production in BHK-21 cells, it affected virion release from the host cell. Subsequentin vivostudies demonstrated that RRV-(Δ6K) caused a milder disease than wild-type virus, with viral titers being reduced in infected mice. Immunization of mice with RRV-(Δ6K) resulted in a reduced viral load and accelerated viral elimination upon secondary infection with wild-type RRV or another alphavirus, chikungunya virus (CHIKV). Our results show that the6kproteins may contribute to alphaviral disease manifestations and suggest that manipulation of the6kgene may be a potential strategy to facilitate viral vaccine development.IMPORTANCEArthritogenic alphaviruses, such as chikungunya virus (CHIKV) and Ross River virus (RRV), cause epidemics of debilitating rheumatic disease in areas where they are endemic and can emerge in new regions worldwide. RRV is of considerable medical significance in Australia, where it is the leading cause of arboviral disease. The mechanisms by which alphaviruses persist and cause disease in the host are ill defined. This paper describes the phenotypic properties of an RRV6kdeletion mutant. The absence of the6kgene reduced virion release from infected cells and also reduced the severity of disease and viral titers in infected mice. Immunization with the mutant virus protected mice against viremia not only upon exposure to RRV but also upon challenge with CHIKV. These findings could lead to the development of safer and more immunogenic alphavirus vectors for vaccine delivery.

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"Stimmtherapie mit Transfrauen". Sprache · Stimme · Gehör 43, n.º 03 (setembro de 2019): 126–27. http://dx.doi.org/10.1055/a-0887-9669.

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Meier, Anna Cäcilia, e Nikolaos Papadopulos. "Lebensqualität nach geschlechtsangleichenden Operationen – eine Übersicht". Handchirurgie · Mikrochirurgie · Plastische Chirurgie, 16 de junho de 2021. http://dx.doi.org/10.1055/a-1487-6415.

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Zusammenfassung Hintergrund Bei Personen mit Geschlechtsinkongruenz wird eine Verminderung der Lebensqualität durch zahlreiche Studien belegt. Die hohe psychische Belastung führt zu depressiven Erkrankungen, Angststörungen und gegenüber der Normbevölkerung erhöhter Suizidalität. Auch soziale Limitationen führen zu verminderter Lebensqualität. Die Möglichkeit geschlechtsangleichender Operationen wird zunehmend wahrgenommen, stellt jedoch einen radikalen Eingriff in das Leben dieser Patienten dar.Ob die chirurgischen Maßnahmen die Lebensqualität und Lebenszufriedenheit von Transfrauen und Transmännern nachhaltig verbessern, soll in dieser Übersichtsarbeit untersucht werden. Methoden Es erfolgte eine Literaturrecherche in den Datenbanken PubMed, Embase und Cochrane Library. Berücksichtigt wurden Originalarbeiten, welche retro- und prospektiv die Lebensqualität nach geschlechtsangleichenden Operationen untersuchten. Ergebnisse 27 Studien, davon 20 retrospektive und 7 prospektive Studien, wurden berücksichtigt, wobei bei 4 Studien ausschließlich Transmänner, bei 11 Studien ausschließlich Transfrauen und bei 12 Studien beide Geschlechter analysiert wurden. In der Gesamtheit der Arbeiten wurden 1849 Transfrauen und 869 Transmänner untersucht. Die Veränderungen der Lebensqualität wurden in diesen durch verschiedene validierte Fragebögen erfasst. Hierbei zeigte sich eine signifikante Verbesserung der Lebensqualität in physischen, psychischen und sozialen Bereichen. Die gesteigerte Zufriedenheit mit dem eigenen Körper und Geschlecht sowie der Lebensqualität generell konnten ebenfalls nachgewiesen werden. Vermehrte psychische Störungen und erhöhte Sterblichkeit gegenüber der Norm wurden auch nach geschlechtsangleichenden Operationen festgestellt. Im Vergleich zur Normbevölkerung blieb die Lebensqualität transsexueller Personen vermindert. Schlussfolgerung Durch zahlreiche Studien kann belegt werden, dass geschlechtsangleichende Operationen helfen, den Leidensdruck unter Transfrauen und Transmännern zu lindern. Lebenszufriedenheit, Gesundheit und soziale Kontakte werden durch chirurgische Eingriffe in Kombination mit endokrinologischer und psychologischer Therapie verbessert. Die Lebensqualität bleibt dennoch hinter der der Normbevölkerung zurück.

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Meyenburg, Bernd, Karin Renter-Schmidt e Gunter Schmidt. "Transidentität in Jugend und Adoleszenz: Zur Veränderung der Sexratio und der Prävalenz in den letzten eineinhalb Jahrzehnten". Zeitschrift für Kinder- und Jugendpsychiatrie und Psychotherapie, 10 de dezembro de 2020, 1–8. http://dx.doi.org/10.1024/1422-4917/a000763.

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Zusammenfassung. Die Auswertung von 1434 Gutachten (darunter 420 unter 20-jährige Begutachtete) zur Vornamens- und Personenstandsänderung nach dem Transsexuellengesetz (TSG) aus den Jahren 2005 bis 2019 zeigt im Untersuchungszeitraum (1) bei Jugendlichen und Adoleszenten eine erhebliche Veränderung der Sexratio zugunsten transidenter Jungen/junger Männer (geburtsgeschlechtlicher Mädchen/Frauen) von 2:1 auf 10:1; (2) bezogen auf die Population aller Begutachteten eine deutliche Zunahme der Prävalenz jugendlicher/adoleszenter Transmänner (geburtsgeschlechtlicher Frauen), wohingegen die Prävalenz der Transfrauen (geburtsgeschlechtlicher Männer), die den juristischen Geschlechtswechsel noch als „Teenager“ vollziehen, im Untersuchungszeitraum praktisch unverändert bleibt. Transidentität im Jugendalter kommt nach unseren Daten heute vor allem bei den als Mädchen Geborenen vor, sie ist ein extrem geschlechtsabhängiges Merkmal. Klinische und soziokulturelle Aspekte dieser Veränderungen werden diskutiert.

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Yu, Fu-Hsien, Kuo-Jung Huang e Chin-Tien Wang. "C-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain". Journal of Virology 91, n.º 10 (1 de março de 2017). http://dx.doi.org/10.1128/jvi.00103-17.

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ABSTRACT HIV-1 protease (PR) functions as a homodimer mediating virus maturation following virus budding. Gag-Pol dimerization is believed to trigger embedded PR activation by promoting PR dimer formation. Early PR activation can lead to markedly reduced virus yields due to premature Gag cleavage. The p6* peptide, located between Gag and PR, is believed to ensure virus production by preventing early PR maturation. Studies aimed at finding supporting evidence for this proposal are limited due to a reading frame overlap between p6* and the p6gag budding domain. To determine if p6* affects virus production via the modulation of PR activation, we engineered multiple constructs derived from Dp6*PR (an assembly- and processing-competent construct with Pol fused at the inactivated PR C terminus). The data indicated that a p6* deletion adjacent to active PR significantly impaired virus processing. We also observed that the insertion of a leucine zipper (LZ) dimerization motif in the deleted region eliminated virus production in a PR activity-dependent manner, suggesting that the LZ insertion triggered premature PR activation by facilitating PR dimer formation. As few as four C-terminal p6* residues remaining at the p6*/PR junction were sufficient to restore virus yields, with a Gag processing profile similar to that of the wild type. Our study provides supporting evidence in a virus assembly context that the C-terminal p6* tetrapeptide plays a role in preventing premature PR maturation. IMPORTANCE Supporting evidence for the assumption that p6* retards PR maturation in the context of virus assembly is lacking. We found that replacing p6* with a leucine zipper peptide abolished virus assembly due to the significant enhancement of Gag cleavage. However, as few as four C-terminal p6* residues remaining in the deleted region were sufficient for significant PR release, as well as for counteracting leucine zipper-incurred premature Gag cleavage. Our data provide evidence that (i) p6* ensures virus assembly by preventing early PR activation and (ii) four C-terminal p6* residues are critical for modulating PR activation. Current PR inhibitor development efforts are aimed largely at mature PR, but there is a tendency for HIV-1 variants that are resistant to multiple protease inhibitors to emerge. Our data support the idea of modulating PR activation by targeting PR precursors as an alternative approach to controlling HIV-1/AIDS.

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Yu, Fu-Hsien, Kuo-Jung Huang e Chin-Tien Wang. "Correction for Yu et al., “C-Terminal HIV-1 Transframe p6* Tetrapeptide Blocks Enhanced Gag Cleavage Incurred by Leucine Zipper Replacement of a Deleted p6* Domain”". Journal of Virology 91, n.º 14 (26 de junho de 2017). http://dx.doi.org/10.1128/jvi.00727-17.

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