Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Kirilee A. Wilson"'
Publikováno v:
Traffic (Copenhagen, Denmark). 8(11)
Sec9p and Spo20p are two SNAP25 family SNARE proteins specialized for different developmental stages in yeast. Sec9p interacts with Sso1/2p and Snc1/2p to mediate intracellular trafficking between post-Golgi vesicles and the plasma membrane during ve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04725d81de8db2f6c1324275a7e8ccf6
https://pubmed.ncbi.nlm.nih.gov/17714435
https://pubmed.ncbi.nlm.nih.gov/17714435
Retroviral transmembrane proteins (TMs) contain an N-terminal fusion peptide that initiates virus-cell membrane fusion. The fusion peptide is linked to the coiled-coil core through a conserved sequence that is often rich in glycines. We investigated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f18f834f461836231add5ae6e5810ae
https://europepmc.org/articles/PMC1061562/
https://europepmc.org/articles/PMC1061562/
Publikováno v:
Biochemical and biophysical research communications. 328(1)
The tetraspanin CD81 plays an essential role in diverse cellular processes. CD81 also acts as an entry receptor for HCV through an interaction between the large extracellular loop (LEL) of CD81 and HCV glycoprotein E2. The E2-CD81 interaction also re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1b82ede445e49b22940b9d8a0ceaa0b
https://pubmed.ncbi.nlm.nih.gov/15670777
https://pubmed.ncbi.nlm.nih.gov/15670777
Autor:
Brenton L. Scott, Kirilee A. Wilson, Song Liu, James A. McNew, Hassan Irshad, Jeffrey S. Van Komen
Publikováno v:
The Journal of Cell Biology
Sec1 proteins are critical players in membrane trafficking, yet their precise role remains unknown. We have examined the role of Sec1p in the regulation of post-Golgi secretion in Saccharomyces cerevisiae. Indirect immunofluorescence shows that endog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83e2f4dab93195859a2b3e0acd0367d9
https://pubmed.ncbi.nlm.nih.gov/15466482
https://pubmed.ncbi.nlm.nih.gov/15466482
Autor:
Chan-Sien Lay, Bruce E. Kemp, Kirilee A. Wilson, Bostjan Kobe, Heidi E. Drummer, Pantelis Poumbourios
Publikováno v:
FEBS letters. 567(2-3)
The folding of HIV gp41 into a 6-helix bundle drives virus-cell membrane fusion. To examine the structural relationship between the 6-helix bundle core domain and other regions of gp41, we expressed in Escherichia coli, the entire ectodomain of HIV-2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12876b127114959947d3b98edffcdac4
https://pubmed.ncbi.nlm.nih.gov/15178320
https://pubmed.ncbi.nlm.nih.gov/15178320
Publikováno v:
Journal of virology. 76(21)
The binding of hepatitis C virus glycoprotein E2 to the large extracellular loop (LEL) of CD81 has been shown to modulate human T-cell and NK cell activity in vitro. Using random mutagenesis of a chimera of maltose-binding protein and LEL residues 11
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf33a5bbb5c57bb5ee0e492eee64f4b7
https://pubmed.ncbi.nlm.nih.gov/12368358
https://pubmed.ncbi.nlm.nih.gov/12368358
Publikováno v:
The Journal of biological chemistry. 276(52)
To investigate the structural context of the fusion peptide region in human T-cell leukemia virus type 1 gp21, maltose-binding protein (MBP) was used as an N-terminal solubilization partner for the entire gp21 ectodomain (residues 313-445) and C-term
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c529b1fcd345da238313b363eb54a77
https://pubmed.ncbi.nlm.nih.gov/11595747
https://pubmed.ncbi.nlm.nih.gov/11595747
Publikováno v:
Journal of virology. 75(14)
Human immunodeficiency virus type 1 (HIV-1) entry into cells is mediated by the surface-exposed envelope protein (SU) gp120, which binds to cellular CD4 and chemokine receptors, triggering the membrane fusion activity of the transmembrane (TM) protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e286ee401b0ad99244025bebd5da158b
https://pubmed.ncbi.nlm.nih.gov/11413331
https://pubmed.ncbi.nlm.nih.gov/11413331
Autor:
Rob J. Center, Bostjan Kobe, Kirilee A. Wilson, Trazel Teh, Bruce E. Kemp, Pantelis Poumbourios, Geoffrey J. Howlett
We present a novel protein crystallization strategy, applied to the crystallization of human T cell leukemia virus type 1 (HTLV-1) transmembrane protein gp21 lacking the fusion peptide and the transmembrane domain, as a chimera with the Escherichia c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d99e954b3247146c4c6becdabf27ee1d
https://europepmc.org/articles/PMC2144054/
https://europepmc.org/articles/PMC2144054/