Zobrazeno 1 - 10
of 158
pro vyhledávání: '"B. C. Paton"'
Publikováno v:
British Journal of Surgery; May 1958, Vol. 45 Issue: 194 p662-663, 2p
Autor:
Alf Poulos, Maria Schröder, Doris Schnabel, W Fürst, K Harzer, Robert Hurwitz, Thomas S. Zenk, A Klein, B C Paton, J Weber
Publikováno v:
Journal of Biological Chemistry. 267:3312-3315
Sphingolipid activator proteins (SAPs) are small, nonenzymic glycoproteins that stimulate lysosomal degradation of various sphingolipids. SAP-1, SAP-2, and two additional potential activator proteins are derived from a common precursor by proteolytic
Autor:
B C, Paton
Publikováno v:
International journal of circumpolar health. 59(2)
Autor:
Z, Zhang, Y, Suzuki, N, Shimozawa, S, Fukuda, A, Imamura, T, Tsukamoto, T, Osumi, Y, Fujiki, T, Orii, R J, Wanders, P G, Barth, H W, Moser, B C, Paton, G T, Besley, N, Kondo
Publikováno v:
Human mutation. 13(6)
The PEX6 (peroxisome assembly factor-2, PAF-2) gene encodes a member of the AAA protein (ATPases associated with diverse cellular activities) family and restores peroxisome assembly in fibroblasts from peroxisome biogenesis disorder patients belongin
Autor:
D, Schnabel, M, Schröder, W, Fürst, A, Klein, R, Hurwitz, T, Zenk, J, Weber, K, Harzer, B C, Paton, A, Poulos
Publikováno v:
The Journal of biological chemistry. 267(5)
Sphingolipid activator proteins (SAPs) are small, nonenzymic glycoproteins that stimulate lysosomal degradation of various sphingolipids. SAP-1, SAP-2, and two additional potential activator proteins are derived from a common precursor by proteolytic
Publikováno v:
Advances in experimental medicine and biology. 318
Fatty acids with from 24 to 28 carbon atoms (very long-chain fatty acids, VLCFA) are present in small amounts in all mammalian tissues. Even longer chain fatty acids with from 30 to 38 carbon atoms (ultra-long-chain fatty acids, ULCFA) are found in c
Publikováno v:
European journal of cell biology. 51(1)
The intracellular localization of sphingolipid activator protein 2 (SAP-2) was determined immunocytochemically using an antiserum raised against a SAP-2 preparation from Gaucher spleen. The immunolabeling indicated that SAP-2 was largely localized in
Publikováno v:
Journal of Inherited Metabolic Disease. 9:163-168
We measured the activity of dihydroxyacetone phosphate acyltransferase (DHAP-AT) in fibroblasts of controls and patients with classical Refsum's disease (RD), infantile Refsum's disease (IRD) and Zellweger's syndrome (ZS). We confirmed that DHAP-AT a