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Disappearance of induced endoplasmic reticulum after cessation of phenobarbital treatment

1976; Wiley; Volume: 68; Issue: 2 Linguagem: Inglês

10.1016/0014-5793(76)80440-1

1873-3468

Joseph W. DePierre, Lars Ernster,

Receptor Mechanisms and Signaling

FEBS LettersVolume 68, Issue 2 p. 219-224 Full-length articleFree Access Disappearance of induced endoplasmic reticulum after cessation of phenobarbital treatment Joseph W. Depierre, Joseph W. Depierre Arrhenius Laboratory, Department of Biochemistry, University of Stockholm, Fack, 104 05 Stockholm, SwedenSearch for more papers by this authorLars Ernster, Lars Ernster Arrhenius Laboratory, Department of Biochemistry, University of Stockholm, Fack, 104 05 Stockholm, SwedenSearch for more papers by this author Joseph W. Depierre, Joseph W. Depierre Arrhenius Laboratory, Department of Biochemistry, University of Stockholm, Fack, 104 05 Stockholm, SwedenSearch for more papers by this authorLars Ernster, Lars Ernster Arrhenius Laboratory, Department of Biochemistry, University of Stockholm, Fack, 104 05 Stockholm, SwedenSearch for more papers by this author First published: October 01, 1976 https://doi.org/10.1016/0014-5793(76)80440-1Citations: 13AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 A.H. Conney, A.G. Gilman, J. Biol. Chem., 238, (1963), 3682– 3690. 10.1016/S0021-9258(19)75326-5 CASPubMedWeb of Science®Google Scholar 2 H. Remmer, H.J. Merker, Science, 142, (1963), 1657– 1659. 10.1126/science.142.3600.1657 CASPubMedWeb of Science®Google Scholar 3 S. Orrenius, J.L.E. Ericsson, L. Ernster, J. Cell Biol., 25, (1965), 627– 639. 10.1083/jcb.25.3.627 CASPubMedWeb of Science®Google Scholar 4 L. Ernster, S. Orrenius, Fed. Proc., 24, (1965), 1190– 1199. CASPubMedGoogle Scholar 5 J. Meldolesi, Biochem. Pharmacol., 16, (1967), 125– 129. 10.1016/0006-2952(67)90193-1 CASWeb of Science®Google Scholar 6 W. Stäubli, R. Hess, E.R. Weibel, J. Cell Biol., 42, (1969), 92– 112. 10.1083/jcb.42.1.92 CASPubMedWeb of Science®Google Scholar 7 S. Orrenius, J.L.E. Ericsson, J. Cell Biol., 28, (1966), 181– 198. 10.1083/jcb.28.2.181 CASPubMedWeb of Science®Google Scholar 8 J.L. Holtzman, J.R. Gilette, J. Biol. Chem., 243, (1968), 3020– 3028. 10.1016/S0021-9258(18)93373-9 CASPubMedWeb of Science®Google Scholar 9 L.C. Eriksson, G. Dallner, FEBS Lett., 29, (1973), 351– 354. 10.1016/0014-5793(73)80057-2 CASPubMedWeb of Science®Google Scholar 10 Y. Kuriyama, T. Omura, P. Siekevitz, G.E. Palade, J. Biol. Chem., 244, (1969), 2017– 2026. 10.1016/S0021-9258(18)94361-9 CASPubMedWeb of Science®Google Scholar 11 R.P. Bolender, E.R. Weibel, J. Cell Biol., 56, (1973), 746– 761. 10.1083/jcb.56.3.746 CASPubMedWeb of Science®Google Scholar 12 L. Ernster, P. Siekevitz, G.E. Palade, J. Cell Biol., 15, (1962), 541– 562. 10.1083/jcb.15.3.541 CASPubMedWeb of Science®Google Scholar 13 G. Dallner, Acta Pathol. Microbiol. Scand., (1963), 166– Suppl. Google Scholar 14 J. Folch, M. Lees, G.H.S. Stanley, J. Biol. Chem., 226, (1957), 497– 509. 10.1016/S0021-9258(18)64849-5 CASPubMedWeb of Science®Google Scholar 15 G.R. Bartlett, J. Biol. Chem., 234, (1959), 466– 468. 10.1016/S0021-9258(18)70226-3 CASPubMedWeb of Science®Google Scholar 16 O.H. Lowry, N.J. Rosebrough, A.L. Farr, R.J. Randall, J. Biol. Chem., 193, (1951), 265– 275. 10.1016/S0021-9258(19)52451-6 CASPubMedWeb of Science®Google Scholar 17 L.C. Eriksson, Acta Pathol. Microbiol. Scand., (1973), 239– Suppl. Google Scholar 18 C.S. Song, O. Bodansky, J. Biol. Chem., 242, (1967), 694– 699. 10.1016/S0021-9258(18)96260-5 CASPubMedWeb of Science®Google Scholar 19 G. Sottocasa, B. Kuylenstierna, L. Ernster, A. Bergstrand, J. Cell Biol., 32, (1967), 415– 438. 10.1083/jcb.32.2.415 CASPubMedWeb of Science®Google Scholar 20 F. Appelmans, R. Wattiaux, Duve C. de, Biochem. J., 59, (1955), 438– 445. 10.1042/bj0590438 CASPubMedWeb of Science®Google Scholar 21 G. Dallner, P. Siekevitz, G.E. Palade, J. Cell Biol., 30, (1966), 97– 117. 10.1083/jcb.30.1.97 CASPubMedWeb of Science®Google Scholar 22 Y. Gnosspelius, H. Thor, S. Orrenius, Chem.-Biol. Interactions, 1, (1969), 125– 137. 10.1016/0009-2797(69)90001-5 CASPubMedGoogle Scholar 23 J.W. DePierre, G. Dallner, A.H. Maddy Biochemical Methods in Membrane Studies (1976), Chapman and Hall London in press Google Scholar 24 P. Strittmatter, P.D. Boyer H. Lardy K. Myrbäck The Enzymes 8, (1963), Academic Press New York 113– 145. Google Scholar Citing Literature Volume68, Issue2October 01, 1976Pages 219-224 ReferencesRelatedInformation