Zobrazeno 1 - 10
of 39
pro vyhledávání: '"sterol carrier protein-x"'
Autor:
Yusuke Inoue, Ai-Ming Yu, Sun Hee Yim, Xiaochao Ma, Kristopher W. Krausz, Junko Inoue, Charlie C. Xiang, Michael J. Brownstein, Gösta Eggertsen, Ingemar Björkhem, Frank J. Gonzalez
Publikováno v:
Journal of Lipid Research, Vol 47, Iss 1, Pp 215-227 (2006)
Hepatocyte nuclear factor 4α (HNF4α) regulates many genes that are preferentially expressed in liver. Mice lacking hepatic expression of HNF4α (HNF4αΔL) exhibited markedly increased levels of serum bile acids (BAs) compared with HNF4α-floxed (H
Externí odkaz:
https://doaj.org/article/2e0d84da66da4c6894602d2415ebe533
Autor:
Barbara P. Atshaves, H. Ross Payne, Avery L. McIntosh, Shane E. Tichy, David Russell, Ann B. Kier, Friedhelm Schroeder
Publikováno v:
Journal of Lipid Research, Vol 45, Iss 5, Pp 812-830 (2004)
Despite the importance of branched chain lipid oxidation in detoxification, almost nothing is known regarding factors regulating peroxisomal uptake, targeting, and metabolism. One peroxisomal protein, sterol carrier protein-x (SCP-x), is thought to c
Externí odkaz:
https://doaj.org/article/bd3737ff3cd241f6a358352cdaa29e6b
Autor:
Christian Wolfrum, Peter Ellinghaus, Manfred Fobker, Udo Seedorf, Gerd Assmann, Torsten Börchers, Friedrich Spener
Publikováno v:
Journal of Lipid Research, Vol 40, Iss 4, Pp 708-714 (1999)
Branched-chain phytanic acid is metabolized in liver peroxisomes. Sterol carrier protein 2/sterol carrier protein x (SCP2/SCPx) knockout mice, which develop a phenotype with a deficiency in phytanic acid degradation, accumulate dramatically high conc
Externí odkaz:
https://doaj.org/article/dd763c00f6b8461c946a50f450971cf6
Akademický článek
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Publikováno v:
Prostaglandins, Leukotrienes and Essential Fatty Acids. 78:131-135
Sterol carrier protein X (SCPx) is a peroxisomal protein with both lipid transfer and thiolase activity. Treating with the fatty acid, lauric acid, induced SCPx mRNA levels in rat liver and in rat hepatoma H4IIE cells but enhanced protein levels of S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8363280809daa26406def3588ccfc392
https://doi.org/10.1016/j.plefa.2007.11.003
https://doi.org/10.1016/j.plefa.2007.11.003
Autor:
Junko Inoue, Ingemar Björkhem, Frank J. Gonzalez, Yusuke Inoue, Michael J. Brownstein, Kristopher W. Krausz, Xiaochao Ma, Sun Hee Yim, Gösta Eggertsen, Aiming Yu, Charlie C. Xiang
Publikováno v:
Journal of Lipid Research, Vol 47, Iss 1, Pp 215-227 (2006)
Hepatocyte nuclear factor 4alpha (HNF4alpha) regulates many genes that are preferentially expressed in liver. Mice lacking hepatic expression of HNF4alpha (HNF4alphaDeltaL) exhibited markedly increased levels of serum bile acids (BAs) compared with H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d28449651a2b97a947a8010758a8b1d5
https://doi.org/10.1194/jlr.m500430-jlr200
https://doi.org/10.1194/jlr.m500430-jlr200
Autor:
David H. Russell, Shane E. Tichy, Barbara P. Atshaves, H. Ross Payne, Friedhelm Schroeder, Ann B. Kier, Avery L. McIntosh
Publikováno v:
Journal of Lipid Research, Vol 45, Iss 5, Pp 812-830 (2004)
Despite the importance of branched chain lipid oxidation in detoxification, almost nothing is known regarding factors regulating peroxisomal uptake, targeting, and metabolism. One peroxisomal protein, sterol carrier protein-x (SCP-x), is thought to c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dac86fd78c86062d3babe6d811510289
http://www.sciencedirect.com/science/article/pii/S0022227520318216
http://www.sciencedirect.com/science/article/pii/S0022227520318216
Publikováno v:
Archives of Biochemistry and Biophysics. 334:251-260
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dris___00893::f3a279e771955b0f1ad4bf226b3ad303
We cloned a full-length cDNA of the nematode Caenorhabditis elegans that encodes a 44-kDa protein (P-44, 412 residues) similar to sterol carrier protein x (SCPx). Mammalian SCPx is a bipartite protein: its 404-residue N-terminal and 143-residue C-ter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3182ca9bb20c53c68a97b0becb97b81
http://ir.lib.hiroshima-u.ac.jp/00014887
http://ir.lib.hiroshima-u.ac.jp/00014887
Autor:
Ossendorp, B.C., Voorhout, W.F., van Amerongen, A., Brunink, F., Batenburg, J.J., Wirtz, K.W.A.
Publikováno v:
Archives of Biochemistry and Biophysics 334 (1996)
Archives of Biochemistry and Biophysics, 334, 251-260
Archives of Biochemistry and Biophysics, 334, 251-260
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::610ee1354596e8b775b104ae8c97b05b
https://research.wur.nl/en/publications/tissue-specific-distribution-of-a-peroxisomal-46-kda-protein-rela
https://research.wur.nl/en/publications/tissue-specific-distribution-of-a-peroxisomal-46-kda-protein-rela