Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Gseping Liu"'
Asymmetric Binding Between SecA and SecB Two Symmetric Proteins: Implications for Function in Export
Autor:
Chunfeng Mao, Jennine M. Crane, Angela A. Lilly, Gseping Liu, Patel Chetankumar Natvarlal, Linda L. Randall, Simon J. S. Hardy
Publikováno v:
Journal of Molecular Biology. 348:479-489
SecB, a small tetrameric chaperone in Escherichia coli, facilitates export of precursor polypeptides from the cytoplasm to the periplasmic space. During this process, SecB displays two modes of binding. As a chaperone, it binds promiscuously to precu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddd97996347167e4984e3897193d0bbb
https://doi.org/10.1016/j.jmb.2005.02.036
https://doi.org/10.1016/j.jmb.2005.02.036
Autor:
Yang Kevin Xiang, Kori Stella, Laurel Thomas, Gseping Liu, François Jean, Andrew J. Reason, Gary Thomas
Publikováno v:
Proceedings of the National Academy of Sciences. 95:7293-7298
The important role of furin in the proteolytic activation of many pathogenic molecules has made this endoprotease a target for the development of potent and selective antiproteolytic agents. Here, we demonstrate the utility of the protein-based inhib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c02db89424433fce0a7c4f2b48518cf
https://doi.org/10.1073/pnas.95.13.7293
https://doi.org/10.1073/pnas.95.13.7293
Autor:
Robin A. Warren, Caroline A. Enns, Gseping Liu, Gary Thomas, John H. Hartwig, C. Casey Cunningham, Laurel Thomas
Publikováno v:
The Journal of Cell Biology
Furin catalyzes the proteolytic maturation of many proproteins within the trans-Golgi network (TGN)/endosomal system. Furin's cytosolic domain (cd) directs both the compartmentalization to and transit between its manifold processing compartments (i.e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25ed222c862cb5ec3ea55a68da559068
http://europepmc.org/articles/PMC1424222
http://europepmc.org/articles/PMC1424222
Autor:
Michael A. Jarvis, Gary Thomas, François Jean, Sean S. Molloy, Gseping Liu, Laurel Thomas, Jay A. Nelson
Current antiviral strategies target viral gene products. Although initially successful, their severe toxicity and susceptibility to circumvention by the generation of drug-resistant variants limit their usefulness. By contrast, the central role of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b61f53124a8693bc07ba0de0f680965e
https://europepmc.org/articles/PMC16021/
https://europepmc.org/articles/PMC16021/
Autor:
Sheree Lynn Rybak, Laurel Thomas, Yang Kevin Xiang, Lei Wan, Sean S. Molloy, Gary Thomas, Gseping Liu
Publikováno v:
Cell. 94(2)
We report the role of one member of a novel gene family, PACS-1, in the localization of trans-Golgi network (TGN) membrane proteins. PACS-1 directs the TGN localization of furin by binding to the protease’s phosphorylated cytosolic domain. Antisens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7d517184f1f956508fb27f8f1d963d1
https://pubmed.ncbi.nlm.nih.gov/9695949
https://pubmed.ncbi.nlm.nih.gov/9695949
Publikováno v:
Journal of Biological Chemistry. 263:14790-14793
We have proposed (Randall, L. L., and Hardy, S. J. S. (1986) Cell 46, 921-928) that during export of protein from Escherichia coli, there is a kinetic partitioning between the pathway that leads to productive translocation and the pathway that leads
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::084e6976412020661c657e4b24208d11
https://doi.org/10.1016/s0021-9258(18)68107-4
https://doi.org/10.1016/s0021-9258(18)68107-4
Publikováno v:
Science (New York, N.Y.). 239(4843)
Leader peptides that function to direct export of proteins through membranes have some common features but exhibit a remarkable sequence diversity. Thus there is some question whether leader peptides exert their function through conventional stereosp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::500f7e582c592c9100b2a65164a81c9e
https://pubmed.ncbi.nlm.nih.gov/3278378
https://pubmed.ncbi.nlm.nih.gov/3278378
It has been shown that folding of precursor maltose-binding protein of Escherichia coli in vitro is retarded by the leader peptide. We now present evidence that this modulation of folding plays a role during the export of maltose-binding protein in v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16bad09498e6dda84ef781ccf566529e
https://europepmc.org/articles/PMC298464/
https://europepmc.org/articles/PMC298464/
Autor:
Wan, Lei, Molloy, Sean S., Thomas, Laurel, Gseping Liu, Yang Xiang, Rybak, Sheree Lynn, Thomas, Gary
Publikováno v:
Cell. 07/24/98, Vol. 94 Issue 2, p205. 12p. 1 Color Photograph, 3 Black and White Photographs, 1 Diagram, 9 Graphs.