Zobrazeno 1 - 10
of 23
pro vyhledávání: '"G S, Shelness"'
Autor:
M F Ingram, G S Shelness
Publikováno v:
Journal of Lipid Research, Vol 37, Iss 10, Pp 2202-2214 (1996)
It has been proposed that inefficient translocation across the endoplasmic reticulum (ER) membrane gives rise to transmembrane forms of apolipoprotein B-100 (apoB). However, we previously demonstrated that the amino-terminal 50% of apoB (apoB-50) was
Externí odkaz:
https://doaj.org/article/91710b29c4c84188ac9f6431742be0c4
Autor:
G S Shelness, J T Thornburg
Publikováno v:
Journal of Lipid Research, Vol 37, Iss 2, Pp 408-419 (1996)
Apolipoprotein B-100 (apoB) is essential for the hepatic assembly and secretion of triglyceride-rich very low density lipoprotein (VLDL). The mechanism of VLDL assembly was explored by perturbing apoB folding in HepG2 cells with the thiol reducing ag
Externí odkaz:
https://doaj.org/article/f667bebaa24341ce9ece89aeae247fbf
Autor:
G Blobel, G S Shelness
Publikováno v:
Journal of Biological Chemistry. 265:9512-9519
Canine microsomal signal peptidase activity was previously isolated as a complex of five subunits (25, 22/23, 21, 18, and 12 kDa). Two of the signal peptidase complex (SPC) subunits (23/23 and 21 kDa) have been cloned and sequenced. One of these, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d41d0b2459c57ac4ded0c60e6bffa3d
https://doi.org/10.1016/s0021-9258(19)38879-9
https://doi.org/10.1016/s0021-9258(19)38879-9
Autor:
J A, Sellers, G S, Shelness
Publikováno v:
Journal of lipid research. 42(11)
C127, a murine mammary tumor-derived cell line, is capable of lipidating and secreting apolipoprotein B-41 (apoB-41) in the apparent absence of microsomal triglyceride transfer protein (MTP). Using a semiquantitative reverse transcriptase-coupled pol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::78c88b075115f1baa2ce78131ea5b7c5
https://pubmed.ncbi.nlm.nih.gov/11714859
https://pubmed.ncbi.nlm.nih.gov/11714859
Publikováno v:
Journal of lipid research. 42(3)
Previous studies demonstrated that structural perturbation of the alpha(1) domain of apolipoprotein B (apoB) blocked the initiation of lipoprotein assembly. We explored the hypothesis that this domain may interact with the inner leaflet of the endopl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b89eb67c0c351062250ce46f3fc3c063
https://pubmed.ncbi.nlm.nih.gov/11254752
https://pubmed.ncbi.nlm.nih.gov/11254752
Publikováno v:
Journal of lipid research. 41(9)
Viscoelastic behavior of proteins at interfaces is a critical determinant of their ability to stabilize emulsions. We therefore used air bubble surfactometry and drop volume tensiometry to examine the dynamic interfacial properties of two plasma apol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::15d0614313e23b7ce5cbf3ce472bf7d1
https://pubmed.ncbi.nlm.nih.gov/10974049
https://pubmed.ncbi.nlm.nih.gov/10974049
Autor:
X F, Huang, G S, Shelness
Publikováno v:
Journal of lipid research. 40(12)
The balance between the hepatic assembly of apolipoprotein B (apoB) and its presecretory degradation at the level of the endoplasmic reticulum (ER) may control the secretion of apoB-containing lipoproteins. In one model, apoB that fails to assemble w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::122b342a64ec00c686452830c9adfe7d
https://pubmed.ncbi.nlm.nih.gov/10588947
https://pubmed.ncbi.nlm.nih.gov/10588947
Publikováno v:
The Journal of nutrition. 129(2S)
Apolipoprotein (apo) B and the microsomal triglyceride transfer protein are essential for the hepatic assembly and secretion of triglyceride-rich VLDL. To understand how apoB initiates the process of lipoprotein formation, interest has focused on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::188fd07a61e622bab3c00b3409c0249b
https://pubmed.ncbi.nlm.nih.gov/10064309
https://pubmed.ncbi.nlm.nih.gov/10064309
Publikováno v:
The Journal of biological chemistry. 268(7)
The signal peptidase complex (SPC) is a hetero-oligomeric membrane protein containing subunits of 12, 18, 21, 22/23, and 25 kDa. The 18- and 21-kDa subunits are mammalian homologs of SEC11 protein, which is necessary for signal peptide processing and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3eb649f05f3ceef89cb972b4ed06c520
https://pubmed.ncbi.nlm.nih.gov/8444896
https://pubmed.ncbi.nlm.nih.gov/8444896
Publikováno v:
Journal of Biological Chemistry. 263:17063-17070
Canine microsomal signal peptidase activity has been shown previously to co-migrate as an apparent complex of six polypeptides with molecular masses of 25, 23, 22, 21, 18, and 12 kDa. The 22- and 23-kDa species are differentially glycosylated forms o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b2f7aabe3a3dd22551d7489882be363
https://doi.org/10.1016/s0021-9258(18)37498-2
https://doi.org/10.1016/s0021-9258(18)37498-2