Zobrazeno 1 - 10
of 86
pro vyhledávání: '"K H Weisgraber"'
Autor:
V Meiner, C Tam, M D Gunn, L M Dong, K H Weisgraber, S Novak, H M Myers, S K Erickson, R V Farese, Jr
Publikováno v:
Journal of Lipid Research, Vol 38, Iss 9, Pp 1928-1933 (1997)
Cholesterol esterification is involved in the regulation of cellular cholesterol content and has been hypothesized to play a role in important physiologic processes including intestinal cholesterol absorption, hepatic lipoprotein production, and macr
Externí odkaz:
https://doaj.org/article/5b71597d2a2a4450a5b664b3bddd1cb4
Publikováno v:
Journal of Lipid Research, Vol 36, Iss 1, Pp 57-66 (1995)
Apolipoprotein (apo) E mediates the removal of chylomicron and VLDL remnants from plasma. In a proband with mild hyperlipidemia and a family history of premature coronary artery disease, we have identified a new mutant of apoE with an isoelectric poi
Externí odkaz:
https://doaj.org/article/ae5791b71d6f417496fb4ca4a98fbecd
Autor:
J B Swaney, K H Weisgraber
Publikováno v:
Journal of Lipid Research, Vol 35, Iss 1, Pp 134-142 (1994)
To evaluate the role of apolipoprotein (apo) C-I in inhibiting lipoprotein binding to the low density lipoprotein receptor-related protein (LRP), a putative lipoprotein remnant receptor, apoC-peptide fragments were prepared by chemical synthesis or b
Externí odkaz:
https://doaj.org/article/243960f9eecc469ab3054639652bbdfe
Autor:
K H Weisgraber
Publikováno v:
Journal of Lipid Research, Vol 31, Iss 8, Pp 1503-1511 (1990)
Human apolipoprotein (apo) E occurs as three common isoforms (apoE4, E3, and E2), all of which influence plasma cholesterol levels. Although both apoE4 and E3 bind with equal effectiveness to the low density lipoprotein receptor, they associate prefe
Externí odkaz:
https://doaj.org/article/43a3280cdc254afb8d6c8144585baa9f
Autor:
V I Zannis, J L Breslow, G Utermann, R W Mahley, K H Weisgraber, R J Havel, J L Goldstein, M S Brown, G Schonfeld, W R Hazzard, C Blum
Publikováno v:
Journal of Lipid Research, Vol 23, Iss 6, Pp 911-914 (1982)
Externí odkaz:
https://doaj.org/article/9bdebe3f4f444ec2bdc5fb95691a1aa0
Autor:
K H Weisgraber, R W Mahley
Publikováno v:
Journal of Lipid Research, Vol 21, Iss 3, Pp 316-325 (1980)
A reproducible and quantitative subfractionation of human high density lipoproteins (HDL) by heparin-Sepharose affinity chromatography has been developed. Two elution methods (A and B) were used to subfractionate HDL(2) (d 1.063-1.125 g/ml) or total
Externí odkaz:
https://doaj.org/article/a6e4c7876dce4aedb4be2b8ad56acd44
Publikováno v:
Journal of Lipid Research, Vol 25, Iss 12, Pp 1277-1294 (1984)
Plasma lipoprotein metabolism is regulated and controlled by the specific apolipoprotein (apo-) constituents of the various lipoprotein classes. The major apolipoproteins include apoE, apoB, apoA-I, apoA-II, apoA-IV, apoC-I, apoC-II, and apoC-III. Sp
Externí odkaz:
https://doaj.org/article/6315e32536c04f099b26da86afa923fb
Publikováno v:
Journal of Lipid Research, Vol 25, Iss 4, Pp 378-382 (1984)
The apolipoprotein E2 ( apoE2 ) variant that possesses a cysteine substituted for an arginine at residue 158 in the amino acid sequence E2( Arg158 ----Cys) can be distinguished by sodium dodecyl sulfate-polyacrylamide gel electrophoresis from other f
Externí odkaz:
https://doaj.org/article/9665d4baf0f7405f9705b4053f735613
Autor:
S C Rall, Jr, K H Weisgraber, R W Mahley, C Ehnholm, O Schamaun, B Olaisen, J P Blomhoff, P Teisberg
Publikováno v:
Journal of Lipid Research, Vol 27, Iss 4, Pp 436-441 (1988)
An apolipoprotein (apo) A-I variant, previously described in two Norwegian families (Schamaun et al. 1983. Hum. Genet. 64: 380-383), represents a mutation in apoA-I in which a single amino acid substitution of lysine for glutamic acid has taken place
Externí odkaz:
https://doaj.org/article/ddb0da5146c84575a04b9408a135404e
Publikováno v:
Journal of Biological Chemistry. 268:23008-23015
Lysine (Lys) residues in apolipoprotein (apo) E are known to be involved in binding of apoE-containing lipoproteins to the low density lipoprotein (LDL) receptor. To examine the microenvironments of the Lys residues of apoE-3 in a variety of lipid-as