Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Andrea J Oestreich"'
Autor:
Andrew P Norgan, Jacqueline R E Lee, Andrea J Oestreich, Johanna A Payne, Eugene W Krueger, David J Katzmann
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e52603 (2012)
Heterologous expression of HIV-1 Gag in a variety of host cells results in its packaging into virus-like particles (VLPs) that are subsequently released into the extracellular milieu. This phenomenon represents a useful tool for probing cellular fact
Externí odkaz:
https://doaj.org/article/393def816cef4623a6aa2a2dd65a3de3
Autor:
Johanna A. Payne, Jacqueline R. E. Lee, Andrew P. Norgan, David J. Katzmann, Andrea J. Oestreich, Mia S. Gunawan
Publikováno v:
Journal of Biological Chemistry. 284:32126-32137
Ubiquitin modification of endosomal membrane proteins is a signal for active inclusion into the Multivesicular Body (MVB) pathway, resulting in lysosomal degradation. However, the endosome represents a dynamic site of protein sorting with a majority
Autor:
Doris Nguyen, Robert C. Piper, S. Brookhart Shields, Stanley C. Winistorfer, Johanna A. Payne, Andrea J. Oestreich, David J. Katzmann
Publikováno v:
The Journal of Cell Biology
Ubiquitin (Ub) sorting receptors facilitate the targeting of ubiquitinated membrane proteins into multivesicular bodies (MVBs). Ub-binding domains (UBDs) have been described in several endosomal sorting complexes required for transport (ESCRT). Using
Publikováno v:
Chemical Reviews. 109:1575-1586
Cells sense and respond to their environment largely through the function of receptors, transporters, and channels within the plasma membrane. For cells to appropriately respond to environmental cues, they must maintain the proper protein complement
Autor:
Ishara F. Azmi, Andrea J. Oestreich, Jacqueline R. E. Lee, Mariam Aboian, David J. Katzmann, Rachel B. Issaka, Johanna A. Payne, Brian A. Davies
Publikováno v:
Molecular Biology of the Cell. 18:707-720
A subset of proteins that transit the endosomal system are directed into the intralumenal vesicles of multivesicular bodies (MVBs). MVB formation is critical for a variety of cellular functions including receptor down-regulation, viral budding, antig
Autor:
Lee Jre, Eugene W. Krueger, Andrea J. Oestreich, Johanna A. Payne, David J. Katzmann, Andrew P. Norgan
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 11 (2013)
PLoS ONE, Vol 8, Iss 11 (2013)
Autor:
Andrew P. Norgan, Jacqueline R. E. Lee, Andrea J. Oestreich, Johanna A. Payne, Eugene W. Krueger, David J. Katzmann
Publikováno v:
PLoS ONE, Vol 8, Iss 11 (2013)
Autor:
Jacqueline R. E. Lee, Eugene W. Krueger, Andrew P. Norgan, Andrea J. Oestreich, David J. Katzmann, Johanna A. Payne
Publikováno v:
PLoS ONE
PLoS ONE, Vol 7, Iss 12, p e52603 (2012)
PLoS ONE, Vol 7, Iss 12, p e52603 (2012)
Heterologous expression of HIV-1 Gag in a variety of host cells results in its packaging into virus-like particles (VLPs) that are subsequently released into the extracellular milieu. This phenomenon represents a useful tool for probing cellular fact
Publikováno v:
ChemInform. 40
Cells sense and respond to their environment largely through the function of receptors, transporters, and channels within the plasma membrane. For cells to appropriately respond to environmental cues, they must maintain the proper protein complement
Publikováno v:
Molecular biology of the cell. 18(2)
The multivesicular body (MVB) sorting pathway impacts a variety of cellular functions in eukaryotic cells. Perhaps the best understood role for the MVB pathway is the degradation of transmembrane proteins within the lysosome. Regulation of cargo sele