Relevant bibliographies by topics / Transfrauen

Academic literature on the topic 'Transfrauen'

Author: Grafiati
Published: 25 July 2024
Last updated: 31 July 2024

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Journal articles on the topic "Transfrauen"

1

Wortmann, Martin. "Barthaarentfernung von Transfrauen: Privatabrechnung möglich." ästhetische dermatologie & kosmetologie 15, no. 1 (February 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, no. 8 (August 1, 2023): r90. http://dx.doi.org/10.9785/cr-2023-390806.

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Proufas, Nina, Karlsson Olberg, and Jonas Simon Schöck. "Transpersonen im Sport – im Zweifel für die Inklusion?" TUP - Theorie und Praxis der Sozialen Arbeit, no. 4 (December 1, 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, no. 3-4 (December 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, no. 3-4 (December 2022): 207–8. http://dx.doi.org/10.61387/s.2022.34.53.

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Bleiber, Gabriela, Solange Peters, Raquel Martinez, Dusan Cmarko, Pascal Meylan, and 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, no. 4 (April 1, 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, and Chin-Tien Wang. "Amino acid substitutions at the HIV-1 transframe region significantly impair virus infectivity." PLOS ONE 17, no. 1 (January 27, 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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8

Huang, Liangqun, Jane M. Sayer, Marie Swinford, John M. Louis, and Chaoping Chen. "Modulation of Human Immunodeficiency Virus Type 1 Protease Autoprocessing by Charge Properties of Surface Residue 69." Journal of Virology 83, no. 15 (May 20, 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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Yu, Fu-Hsien, Ting-An Chou, Wei-Hao Liao, Kuo-Jung Huang, and Chin-Tien Wang. "Gag-Pol Transframe Domain p6* Is Essential for HIV-1 Protease-Mediated Virus Maturation." PLOS ONE 10, no. 6 (June 1, 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, and 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, no. 7 (July 1, 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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Dissertations / Theses on the topic "Transfrauen"

1

Dautin, Nathalie. "L'adénylcyclase de Bordetella pertussis comme outil génétique chez Escherichia coli : élaboration d'un système génétique de criblage d'activités protéolytiques et application à l'étude de la protéase du virus de l'immunodéficience humaine." Paris 7, 2003. http://www.theses.fr/2003PA077032.

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Yu, Fu-Hsien, and 于福賢. "The Role of HIV-1 p6pol Transframe Region in Modulating Protease Activation." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/gr95s8.

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博士
國立陽明大學
臨床醫學研究所
106
Abstract HIV-1 protease (PR) is encoded by pol, which is initially translated as a Pr160gag-pol polyprotein by a ribosomal frameshift event. 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. Within Gag-Pol, truncated p6gag is replaced by a transframe region (referred to as p6pol or p6*) located directly upstream of PR. The p6* peptide is believed to ensure virus production by preventing early PR maturation. Overlapping reading frames between p6* and p6gag present a challenge to researchers using genetic approaches to studying p6* biological functions. To determine the role of p6* in PR activation without affecting the gag reading frame, we constructed a series of Gag/Gag-Pol expression vectors by duplicating PR with or without p6* between PR pairs, and observed that PR duplication eliminated virus production due to significant Gag cleavage enhancement. This effect was mitigated when p6* was placed between the two PRs. Further, Gag cleavage enhancement was markedly reduced when either one of the two PRs was mutationally inactivated. Additional reduction in Gag cleavage efficiency was noted following the removal of p6* from between the two PRs. Next, 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 8 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. To clarify the involvement of C terminal p6* residues in mitigating enhanced LZ-incurred Gag processing, we engineered constructs containing C-terminal p6* residue substitutions with and without a mutation blocking the p6*/PR cleavage site. The p6*-PR cleavage blocking did not significantly reduce the LZ enhancement effect on Gag cleavage when only four amino acid residues were present between the p6* and PR. This suggests that the potent LZ dimerization motif may enhance PR activation by facilitating PR dimer formation, and that PR precursors may trigger sufficient enzymatic activity without breaking off from the PR N-terminus. We also observed that a proline substitution at the P3 position eliminated the ability of p6*-deleted Gag-Pol to mediate virus maturation, thus emphasizing the importance of C-terminal p6* residues to modulating PR activation. 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, C-terminal p6* tetra-peptides 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. Key words: HIV-1 , virus maturation, protease, ribosomal frameshift, transframe region (p6pol or p6*), leucine zipper (LZ), tetra-peptide
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3

Chiu, Hsu-Chen, and 邱旭真. "Effects of the human immunodeficiency virus type 1 transframe protein p6* mutations on the viral protease-mediated Gag processing." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/42997903377765764828.

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碩士
國立陽明大學
公共衛生研究所
93
The maturation of human immunodeficiency virus particles mediated by viral protease (PR) is not required for virus assembly but is essential for viral infectivity. The PR is encoded by the pol gene, which partially overlaps with the gag open reading frame and is translated as a Gag-Pol polyprotein precursor. Within the Gag-Pol, the C-terminal Gag cleavage product p6gag is truncated and replaced by a transframe peptide referred to as p6* or p6pol. The p6* separates the Gag nucleocapsid (NC) domain from PR. Removal of the p6* can improve HIV Gag processing in vitro, suggesting that the p6* is involved in the regulation of protease activation. To investigate the contribution of p6* to virus particle maturation, a series of Gag-Pol constructs with various mutations in the p6* was engineered. Effects of the p6* mutations on virus particle assembly and processing were analyzed by coexpressing each of the p6* mutants with an HIV-1 Gag precursor expression plasmid in 293T cells. Analysis indicated that the deletion mutations in p6* markedly affect virus infectivity although Western blot analyses suggested that the deletion mutations have no significant effects on the PR-mediated Gag processing. However, negative effects of the p6*-deletion mutations on PR-mediated virus particle processing were readily observed when the upstream gag coding sequence had been deleted or an intact C-terminal p6gag was present. Consistent with the previous reports, mutations blocking p6*/PR cleavage significantly affected PR activity. These results suggest that the presence of p6* is required during the process of PR activation; however, the p6* needs to be removed eventually in order to obtain a fully functional PR.
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4

Ludwig, Christine [Verfasser]. "Funktionelle Untersuchungen zur Rolle des "transframe"-Proteins p6* bei der Replikation von HIV-1 : Bedeutung der Proteasespaltstellen von p6* für die virale Maturation und Infektiosität / vorgelegt von Christine Ludwig." 2003. http://d-nb.info/968950787/34.

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Books on the topic "Transfrauen"

1

Elsner, Constanze, ed. Ich war ein Mann: Die Lebensgeschichte einer Transsexuellen. Rastatt, Germany: Hestia, 1992.

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2

Antonelli, Federico J., ed. Charlotte Charlaque: Transfrau, Laienschauspielerin, "Königin der Brooklyn Heights Promenade". Berlin, Germany: Hentrich & Hentrich, 2021.

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Appleby, Steven. Dragman. London, UK: Jonathan Cape, 2020.

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4

Das verbotene Ich: Lebenswege eines Transsexuellen. Salzgitter, Germany: Bonz Verlag, 2000.

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Steininger, Patti-Saoirse. Mein Weg Zu Mir: Aus Dem Leben Einer Transfrau. Independently Published, 2019.

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Dragman: Een graphic novel. Podium b.v. Uitgeverij, 2020.

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Dragman. Denoël Graphic, 2020.

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Molines, Núria, and Steven Appleby. Dragman. FINESTRES, 2022.

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Appleby, Steven. Dragman. Denoël Graphic, 2020.

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Appleby, Steven. Dragman: A Novel. Metropolitan Books, 2020.

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