Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding.

By J. Garrus, U. V. Schwedler, O. Pornillos, S. Morham, K. Zavitz, H. Wang, D. Wettstein, Kirsten M. Stray, M. Côté, R. Rich and 2 more. Cell, 2001

1,468 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Virology

View Paper: https://www.semanticscholar.org/paper/92ba849ffe1ba448491b7e6b3d76ac1e94d3b9c3

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In Cell Biology

1. G. Raposo
2. David J. Katzmann
3. S. Emr
4. C. Théry
5. W. Henne
6. Nicholas J. Buchkovich
7. W. Stoorvogel
8. S. Amigorena

In Molecular Biology

1. G. Raposo
2. C. Théry
3. W. Stoorvogel
4. David J. Katzmann
5. S. Amigorena
6. W. Henne
7. Wesley I. Sundquist
8. J. Ernst

In Virology

1. C. K. Kwan
2. J. Ernst
3. C. Seeger
4. W. Mason

Citations in the corpus

• Formation and release of arrestin domain-containing protein 1-mediated microvesicles (ARMMs) at plasma membrane by recruitment of TSG101 protein (2012, background): “TSG101 is essential for MVB formation (33) and HIV budding (19).”
• The protein network of HIV budding. (2003, methodology): “PTAP late domains recruit the cellular protein TSG101 to facilitateHyo-Young Chung,1 Eiji Morita,1 Hubert E. Wang,4 Thaylon Davis,4 virus budding (Demirov et al., 2002a; Garrus et al., 2001; Martin-Serrano et al., 2001; VerPlank et al., 2001).”
• Genome-scale RNAi screen for host factors required for HIV replication. (2008, methodology): “The screen was optimized using siRNAs targeting cyclin T1 and Tsg101, factors associated with HIV Tat-mediated transcription and HIV particle release, respectively (Bieniasz et al., 1999; Garrus et al., 2001).”
• Ubiquitin and ubiquitin-like proteins as multifunctional signals (2005, background): “It is now well known that retroviruses subvert the multivesicular-body system for their exit from the cel”
• Receptor downregulation and multivesicular-body sorting (2002, background): “pl?Q99816">Tsg101 (see below), has been shown to bind ubiquitin directly in vitro”
• Lassa Virus Z Protein Is a Matrix Protein Sufficient for the Release of Virus-Like Particles (2003, background): “Late domains were originally identified in the Gag proteins of a number of retroviruses and in the matrix proteins of rhabdo- and filoviruses and interact with cellular target proteins to promote virus particle release by membrane fission (11, 12, 15, 17, 18, 26, 27, 37, 38).”
• The Biogenesis and Functions of Exosomes (2002, background): “HIV-1 assembly is driven by Gag, a viral protein that associates with Tsg101.”