pseglen

• Klionsky, Daniel J.; Abdel-Aziz, Amal Kamal; Abdelfatah, Sara; Abdellatif, Mahmoud Khaled; Abdoli, Asghar & Abudu, Yakubu Princely [Vis alle 50 forfattere av denne artikkelen] (2021). Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) . Autophagy. ISSN 1554-8627. 17(1), s. 1–382. doi: 10.1080/15548627.2020.1797280.
• Engedal, Nikolai; Luhr, Morten; Szalai, Paula & Seglen, Per O. (2019). Measurement of Bulk Autophagy by a Cargo Sequestration Assay. Methods in molecular biology. ISSN 1064-3745. 1880, s. 307–313. doi: 10.1007/978-1-4939-8873-0_20.
• Luhr, Morten; Szalai, Paula; Sætre, Frank; Gerner, Lisa; Seglen, Per O. & Engedal, Nikolai (2017). A simple cargo sequestration assay for quantitative measurement of non-selective autophagy in cultured cells. Methods in Enzymology. ISSN 0076-6879. 587, s. 351–364. doi: 10.1016/bs.mie.2016.09.064.
• Engedal, Kim Nikolai & Seglen, Per O. (2016). Autophagy of cytoplasmic bulk cargo does not require LC3. Autophagy. ISSN 1554-8627. 12(2), s. 439–441. doi: 10.1080/15548627.2015.1076606.
• Sætre, Frank; Hagen, Linda K Korsberg; Engedal, Kim Nikolai & Seglen, Per O. (2015). Novel steps in the autophagic-lysosomal pathway. The FEBS Journal. ISSN 1742-464X. 282(11), s. 2202–2214. doi: 10.1111/febs.13268. Fulltekst i vitenarkiv
• Szalai, Paula; Hagen, Linda K Korsberg; Sætre, Frank; Luhr, Morten; Sponheim, Marianne & Øverbye, Anders [Vis alle 9 forfattere av denne artikkelen] (2015). Autophagic bulk sequestration of cytosolic cargo is independent of LC3, but requires GABARAPs. Experimental Cell Research. ISSN 0014-4827. 333(1), s. 21–38. doi: 10.1016/j.yexcr.2015.02.003.
• Seglen, Per O.; Luhr, Morten; Mills, Ian Geoffrey; Sætre, Frank; Szalai, Paula & Engedal, Kim Nikolai (2015). Macroautophagic cargo sequestration assays. Methods. ISSN 1046-2023. 75, s. 25–36. doi: 10.1016/j.ymeth.2014.12.021.
• Patel, Khushbu K; Miyoshi, Hiroyuki; Beatty, Wandy L; Head, Richard D; Malvin, Nicole P & Cadwell, Ken [Vis alle 13 forfattere av denne artikkelen] (2013). Autophagy proteins control goblet cell function by potentiating reactive oxygen species production. EMBO Journal. ISSN 0261-4189. 32(24), s. 3130–3144. doi: 10.1038/emboj.2013.233.
• Engedal, Kim Nikolai; Torgersen, Maria Lyngaas; Guldvik, Ingrid Jenny; Barfeld, Stefan; Bakula, D & Sætre, Frank Ove [Vis alle 12 forfattere av denne artikkelen] (2013). Modulation of intracellular calcium homeostasis blocks autophagosome formation. Autophagy. ISSN 1554-8627. 9(10), s. 1475–1490. doi: 10.4161/auto.25900.
• Klionsky, Daniel J.; Abdalla, FC; Abeliovich, H; Abraham, RT; Acevedo-Arozena, A & Adeli, K [Vis alle 1 261 forfattere av denne artikkelen] (2012). Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy. ISSN 1554-8627. 8(4), s. 445–544. doi: 10.4161/auto.19496.
• Eskelinen, Eeva-Liisa; Reggiori, Fulvio; Baba, Misuzu; Kovács, Attila L. & Seglen, Per O. (2011). Seeing is believing The impact of electron microscopy on autophagy research. Autophagy. ISSN 1554-8627. 7(9), s. 935–956. doi: 10.4161/auto.7.9.15760.
• Øverbye, Anders; Sætre, Frank Ove; Hagen, Linda K Korsberg; Johansen, Harald Thidemann & Seglen, Per O. (2011). Autophagic activity measured in whole rat hepatocytes as the accumulation of a novel BHMT fragment (p10), generated in amphisomes by the asparaginyl proteinase, legumain. Autophagy. ISSN 1554-8627. 7(9), s. 1011–1027. doi: 10.4161/auto.7.9.16436.
• Seglen, Per Ottar & Brinchmann, Monica Fengsrud (2010). Purification of autophagosomes from rat hepatocytes. Autophagy. ISSN 1554-8627. 6(4), s. 542–547. doi: 10.4161/auto.6.4.11272. Vis sammendrag

  To facilitate the purification of rat liver autophagosomes, isolated rat hepatocytes are first incubated for 2 h at 37 C with vinblastine, which induces autophagosome accumulation by blocking the fusion of these organelles with endosomes and lysosomes. The hepatocytes are then electrodisrupted and homogenized, and the various cellular organelles sequentially removed by subcellular fractionation. A brief incubation of the homogenate with the cathepsin C substrate, glycyl-phenylalanine-naphthylamide (GPN), causes rapid osmotic disruption of the lysosomes due to intralysosomal accumulation of GPN cleavage products. Nuclei are removed by differential centrifugation, and the post-nuclear supernatant subsequently fractionated on a two-step Nycodenz density gradient. Autophagosomes are recovered in an intermediate density fraction, free from cytosol and mitochondria. The autophagosomes are finally separated from the membranes and vesicles of the endoplasmic reticulum, Golgi, endosomes, etc., by sieving through a density gradient of colloidal silica particles (Percoll). The final preparation contains about 95% autophagosomes and 5% amphisomes according to morphological and biochemical criteria.

• Klionsky, Daniel J. & Seglen, Per O. (2010). The Norse god of autophagy. Autophagy. ISSN 1554-8627. 6(8), s. 1017–1031. doi: 10.4161/auto.6.8.13092.
• Øverbye, Anders & Seglen, Per O. (2009). Phosphorylated and non-phosphorylated forms of catechol O-methyltransferase in rat liver, brain and other tissues. Biochemical Journal. ISSN 0264-6021. 417, s. 535–545. doi: 10.1042/BJ20081284.
• Seglen, Per O.; Øverbye, Anders & Sætre, Frank (2009). Sequestration assays for mammalian autophagy. Methods in Enzymology. ISSN 0076-6879. 452, s. 63–83. doi: 10.1016/S0076-6879(08)03605-7.
• Klionsky, DJ; Abeliovich, H; Agostinis, P; Agrawal, DK; Aliev, G & Askew, DS [Vis alle 235 forfattere av denne artikkelen] (2008). Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy. ISSN 1554-8627. 4(2), s. 151–175.
• Øverbye, Anders; Fengsrud, Monica & Seglen, Per Ottar (2007). Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy. ISSN 1554-8627. 3(4), s. 300–322. Vis sammendrag

  Proteins associated with membranes from purified rat liver autophagosomes were separated by two-dimensional (2D) gel electrophoresis (zoom gels, pl 4-7 and 6-9), silver-stained and identified by MALDI-TOF mass spectrometry. Among >1,500 detectable protein spots, 58 (derived from 39 different known proteins) were at least twofold (and significantly) enriched in autophagosomal membranes relative to cytoplasmic membranes. All of these membrane-associated proteins were also present in the cytosol, many of them being truncated enzyme variants that would be expected to serve a binding rather than an enzymatic function. Eleven proteins were highly enriched (consistent with the theoretical maximum of 25x), corresponding to an exclusive membrane localization in the delimiting membrane of the autophagosome. Three of these were methyltransferases: betaine:homocysteine methyltransferase (five variants); catechol O-methyltransferase (one phosphorylated and one unphosphorylated variant) and methionine adenosyltransferase, perhaps indicating that methylation/demethylation of membrane components could play a role in autophagy. A fourth highly enriched autophagosomal protein, phosphatidylethanolamine binding protein, is particularly interesting considering that the autophagic marker protein, LC3/ Atg8, is linked to autophagosomal membranes through its covalent conjugation with phosphatidylethanolamine (as the form LC3-II). LC3-II was not detectable on silver-stained 2D-gels, but could be shown by immunoblotting to be highly enriched in autophagosomal membranes. Other highly enriched proteins were heat shock cognate protein Hsc70 (one short and one long variant), peroxiredoxin 2, peroxiredoxin 6 (two variants), fructose 1,6-bisphosphatase (one phosphorylated and one unphosphorylated variant), adenosine kinase, inorganic pyrophosphatase and selenium-binding protein 2. Hsc70, a chaperonin that plays an important role in the recognition and proteasomal degradation of aggregated proteins as well as in the lysosomal membrane uptake and degradation of certain cytosolic proteins (chaperone-mediated autophagy), could conceivably also serve a recognition function in the autophagic scavenging of denatured or aggregated proteins (aggrephagy). The moderately enriched (2-14x) autophagosomal membrane-associated proteins included a remarkably high proportion of drug-metabolizing enzymes, such as several glutathione S-transferases, sulfotransferases and aromatic hydrocarbon/steroid oxidoreductases. If the autophagic function of these proteins is to recognize protein-drug adducts, they may, along with the peroxiredoxins, chaperonins and methyl metabolic enzymes, make the phagophores (the sequestering precursors of the autophagosomal delimiting membrane) well equipped for the detection and scavenging of proteins denatured by oxidation, hypermethylation, drug adduction or other mechanisms.

• Samari, Hamid R.; Møller, Michael T.N.; Holden, Lise; Asmyhr, Tonje & Seglen, Per O. (2005). Stimulation of hepatocytic AMP-activated protein kinase by okadaic acid and other autophagy-suppressive toxins. Biochemical Journal. ISSN 0264-6021. 386, s. 237–244.
• Asmyhr, Tonje; Samari, Hamid R.; Hildonen, Siri; Helgerud, Marit; Dahl, Mai B. & Seglen, Per O. (2005). Multiphosphorylation of hepatocellular AMPK: implications for ageing. Giornale di Gerontologia. ISSN 0017-0305. 53, s. 40–41.
• Lindstad, Rune I.; Sylte, Ingebrigt; Mikalsen, Svein O.; Seglen, Per O.; Berg, Eli & Winberg, Jan O. (2005). Pancreatic trypsin activates human promatrix metalloproteinase-2. Journal of Molecular Biology (JMB). ISSN 0022-2836. 350, s. 682–698.
• Lunde Sneve, Marianne; Øverbye, Anders; Fengsrud, Monica & Seglen, Per O. (2005). Comigration of two autophagosome-associated dehydrogenases on two-dimensional polyacrylamide gels. Autophagy. ISSN 1554-8627. 1, s. 157–162.
• Samari, Hamid Reza; Møller, Michael T. N; Holden, Lise; Asmyhr, Tonje & Seglen, Per O. (2005). Biochem. J. (2005) 386, 237–244 (Printed in Great Britain) 237 Stimulation of hepatocytic AMP-activated protein kinase by okadaic acid and other autophagy-suppressive toxins. Biochemical Journal. ISSN 0264-6021. 386, s. 237–244. doi: 10.1042/BJ20040609. Vis sammendrag

  Autophagic activity in isolated rat hepatocytes is strongly suppressed by OA (okadaic acid) and other PP (protein phosphatase)-inhibitory toxins as well as by AICAR (5-aminoimidazole-4-carboxamide riboside), a direct activator of AMPK (AMP-activated protein kinase). To investigate whether AMPK is a mediator of the effects of the toxin, a phosphospecific antibody directed against the activation of phosphorylation of the AMPK α (catalytic)-subunit at Thr172 was used to assess the activation status of this enzyme. AICAR as well as all the toxins tested (OA, microcystin-LR, calyculin A, cantharidin and tautomycin) induced strong, dose-dependent AMPKα phosphorylation, correlating with AMPK activity in situ (in intact hepatocytes) as measured by the AMPK-dependent phosphorylation of acetyl-CoA carboxylase at Ser79. All treatments induced the appearance of multiple, phosphatase-sensitive, low-mobility forms of the AMPK α-subunit, consistent with phosphorylation at several sites other than Thr172. The flavonoid naringin, an effective antagonist of OA-induced autophagy suppression, inhibited the AMPK phosphorylation and mobility shifting induced by AICAR, OA or microcystin, but not the changes induced by calyculin A or cantharidin. AMPK may thus be activated both by a naringin-sensitive and a naringin-resistant mechanism, probably involving the PPs PP2A and PP1 respectively. Neither the Thr172-phosphorylating protein kinase LKB1 nor the Thr172-dephosphorylating PP, PP2C, were mobility-shifted after treatment with toxins or AICAR, whereas a slight mobility shifting of the regulatory AMPK β-subunit was indicated. Immunoblotting with a phosphospecific antibody against pSer108 at the β-subunit revealed a naringin-sensitive phosphorylation induced by OA, microcystin and AICAR and a naringin-resistant phosphorylation induced by calyculin A and cantharidin, suggesting that β-subunit phosphorylation could play a role in AMPK activation. Naringin antagonized the autophagy-suppressive effects of AICAR and OA, but not the autophagy suppression caused by cantharidin, consistent with AMPK-mediated inhibition of autophagy by toxins as well as by AICAR.

• Fengsrud, Monica ; Lunde Sneve, Marianne; Øverbye, Anders & Seglen, Per O. (2004). Structural aspects of mammalian autophagy, Autophagy (Klionsky, D.J., ed.). Landes Bioscience. ISSN 1-58706-203-8. s. 11–25.
• Møller, Michael T.N.; Samari, Hamid R.; Holden, Lise & Seglen, Per O. (2004). Regulation of mammalian autophagy by protein phosphorylation, Autophagy (Klionsky, D.J., ed.). Landes Bioscience. ISSN 1-58706-203-8. s. 48–59.
• Rusten, Tor E.; Lindmo, Karine; Juhász, Gábor; Sass, Miklós; Seglen, Per O. & Brech, Andreas [Vis alle 7 forfattere av denne artikkelen] (2004). Programmed autophagy in the Drosophila fat body is induced by ecdysone through regulation of the PI3K pathway. Developmental Cell. ISSN 1534-5807. 7, s. 179–192.
• Møller, Michael T. N; Samari, Hamid R. & Seglen, Per O. (2004). Toxin-induced tail phosphorylation of hepatocellular S6 kinase: Evidence for a dual involvement of the AMP-activated protein kinase in S6 kinase regulation. Toxicological Sciences. ISSN 1096-6080. s. 628–637. doi: 10.1093/toxsci/kfh273. Vis sammendrag

  Several protein phosphatase-inhibitory toxins (okadaic acid, microcystin, calyculin A, cantharidin, tautomycin) administered to isolated rat hepatocytes were found to induce phosphorylation in the tail region of S6 kinase (S6K; p70S6K1) as detected with a phosphospecific antibody against doubly phosphorylated Thr-421/Ser424. 5-Aminoimidazole-4-carboxamide riboside (AICAR), an adenosine analogue that elicits activation of the hepatocellular AMP-activated protein kinase (AMPK), similarly stimulated S6K tail phosphorylation. The flavonoid naringin prevented the effects of AICAR, okadaic acid, and microcystin on AMPK activation as well as on S6K tail phosphorylation, suggesting AMPK as a mediator of the latter. The effects of AICAR and the toxins were rapamycin resistant; in contrast, amino acids induced an S6K tail phosphorylation that was rapamycin sensitive, suggesting mediation by the protein kinase mammalian target of rapamycin (mTOR). Amino acids activated S6K by phosphorylation at Thr-389, but the toxins did not, and AICAR in fact suppressed the activating phosphorylation induced by the amino acids. The possibility thus must be considered that the phosphorylated S6K tail may transmit a toxin-induced signal independently of S6K enzymatic activity. Despite their inability to activate S6K, the toxins (but not AICAR) stimulated phosphorylation of the ribosomal protein S6, presumably by activating some other S6-phosphorylating protein kinase.

• Seglen, Per O. (2003). Bibliometric analysis - what can it tell us? Proceedings / Max Planck Forum. 6, s. 139–151.
• Møller, Michael T. N; Samari, Hamid R.; Fengsrud, Monica ; Strømhaug, Per E.; Østvold, Anne C. & Seglen, Per O. (2003). Okadaic acid-induced, naringin-sensitive phosphorylation of glycine N-methyltransferase in isolated rat hepatocytes. Biochemical Journal. ISSN 0264-6021. 373, s. 505–513. doi: 10.1042/BJ20030502. Vis sammendrag

  Glycine N-methyltransferase (GNMT) is an abundant cytosolic enzyme that catalyses the methylation of glycine into sarcosine, coupled with conversion of the methyl donor, S -adenosylmethionine (AdoMet), into S -adenosylhomocysteine (AdoHcy). GNMT is believed to play a role in monitoring the AdoMet/AdoHcy ratio, and hence the cellular methylation capacity, but regulation of the enzyme itself is not well understood. In the present study, treatment of isolated rat hepatocytes with the protein phosphatase inhibitor okadaic acid, was found to induce an overphosphorylation of GNMT, as shown by proteomic analysis. The analysis comprised two-dimensional gel electrophoretic separation of (32)P-labelled phosphoproteins and identification of individual protein spots by matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry. The identity of GNMT was verified by N-terminal Edman sequencing of tryptic peptides. Chromatographic separation of proteolytic peptides and (32)P-labelled amino acids suggested that GNMT was phosphorylated within a limited region, and only at serine residues. GNMT phosphorylation could be suppressed by naringin, an okadaic acid-antagonistic flavonoid. To assess the possible functional role of GNMT phosphorylation, the effect of okadaic acid on hepatocytic AdoMet and AdoHcy levels was examined, using HPLC separation for metabolite analysis. Surprisingly, okadaic acid was found to have no effect on the basal levels of AdoMet or AdoHcy. An accelerated AdoMet-AdoHcy flux, induced by the addition of methionine (1 mM), was likewise unaffected by okadaic acid. 5-Aminoimidazole-4-carboxamide riboside, an activator of the hepatocytic AMP-activated protein kinase, similarly induced GNMT phosphorylation without affecting AdoMet and AdoHcy levels. Activation of cAMP-dependent protein kinase by dibutyryl-cAMP, reported to cause GNMT phosphorylation under cell-free conditions, also had little effect on hepatocytic AdoMet and AdoHcy levels. Phosphorylation of GNMT would thus seem to play no role in regulation of the intracellular AdoMet/AdoHcy ratio, but could be involved in other GNMT functions, such as the binding of folates or aromatic hydrocarbons.

• Ruud Larsen, Ann K.; Møller, Michael T. N; Blankson, Henrietta; Samari, Hamid R.; Holden, Lise & Seglen, Per O. (2002). Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes. Journal of Biological Chemistry. ISSN 0021-9258. 277, s. 34826–34835. doi: 10.1074/jbc.M205028200. Fulltekst i vitenarkiv Vis sammendrag

  To identify phosphoproteins that might play a role in naringin-sensitive hepatocellular cytoskeletal disruption and apoptosis induced by algal toxins, hepatocyte extracts were separated by gel electrophoresis and immunostained with a phosphothreonine-directed antibody. Use of dilute (5%) polyacrylamide gels containing 6 m urea allowed the resolution of one very large (approximately 500-kDa) okadaic acid- and naringin-sensitive phosphoprotein, identified by tryptic fingerprinting, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, and immunostaining as the cytolinker protein, plectin. The naringin-sensitive phosphorylation induced by okadaic acid and microcystin-LR probably reflected inhibition of a type 2A protein phosphatase, whereas the naringin-resistant phosphorylation induced by calyculin A, tautomycin, and cantharidin probably involved a type 1 phosphatase. Okadaic acid caused a collapse of the plectin-immunostaining bile canalicular sheaths and the general cytoskeletal plectin network into numerous medium-sized plectin aggregates. Inhibitors of protein kinase C, cAMP-dependent protein kinase, or Ca(2+)/calmodulin-dependent kinase II had moderate or no protective effects on plectin network disruption, whereas naringin offered 86% protection. Okadaic acid induced a naringin-sensitive phosphorylation of AMP-activated protein kinase (AMPK), the stress-activated protein kinases SEK1 and JNK, and S6 kinase. The AMPK-activating kinase (AMPKK) is likely to be the target of inhibition by naringin, the other kinases serving as downstream components of an AMPKK-initiated signaling pathway.

• Berven, Grethe; Sætre, Frank; Halvorsen, Kathrine & Seglen, Per O. (2001). Effects of the diarrhetic shellfish toxin, okadaic acid, on cytoskeletal elements, viability and functionality of rat liver and intestinal cells. Toxicon. ISSN 0041-0101. 39, s. 349–362.
• Mousavi, Seyed A.; Kjeken, Rune; Berg, Trond O.; Seglen, Per O.; Berg, Trond & Brech, Andreas (2001). Effects of inhibitors of the vacuolar proton pump on hepatic heterophagy and autophagy. Biochimica et Biophysica Acta. ISSN 0006-3002. 1510, s. 243–257.
• Seglen, Per O. (2001). Evaluating biology: A scientometric study of a university biology department. NIFU skriftserie. ISSN 0808-4572. s. 1–70.
• Aksnes, Dag W.; Olsen, Terje B. & Seglen, Per O. (2000). Validation of bibliometric indicators in the field of microbiology: A Norwegian case study. Scientometrics. ISSN 0138-9130. 49, s. 7–22.
• Seglen, Per O. & Aksnes, Dag W. (2000). Scientific productivity and group size: A bibliometric analysis of Norwegian microbiological research. Scientometrics. ISSN 0138-9130. 49, s. 125–143.
• Fengsrud, Monica ; Raiborg, Camilla; Berg, Trond O.; Strømhaug, Per E.; Ueno, Takashi & Erichsen, Egil S. [Vis alle 7 forfattere av denne artikkelen] (2000). Autophagosome-associated variant isoforms of cytosolic enzymes. Biochemical Journal. ISSN 0264-6021. 352, s. 773–781.
• Fengsrud, Monica ; Erichsen, Egil S.; Berg, Trond O.; Raiborg, Camilla & Seglen, Per O. (2000). Ultrastructural characterization of the delimiting membranes of isolated autophagosomes and amphisomes by freeze-fracture electron microscopy. European Journal of Cell Biology. ISSN 0171-9335. 79, s. 871–882.
• Blankson, Henrietta; Grotterød, Else M. & Seglen, Per O. (2000). Prevention of toxin-induced cytoskeletal disruption and apoptotic liver cell death by the grapefruit flavonoid, naringin. Cell Death and Differentiation. ISSN 1350-9047. 7, s. 739–746.
• Aksnes, Dag W.; Olsen, Terje B. & Seglen, Per O. (1999). Inadequacy of a journal-based research field delineation. Incomplete recovery of Norwegian microbiology articles in ISI's Microbiology field. I Macías-Chapula, César A. (Red.), Proceedings of the Seventh Conference of the International Society for Scientometrics and Informetrics. Universidad de Colima. ISSN 968-6190-91-0. s. 1–10.
• Rundén, Elise; Seglen, Per O.; Haug, Finn M.; Ottersen, Ole P.; Wieloch, Tadeusz & Shamloo, Mehrdad [Vis alle 7 forfattere av denne artikkelen] (1998). Regional selective neuronal degeneration after protein phosphatase inhibition in hippocampal slice cultures: Evidence for a MAP kinase-dependent mechanism. Journal of Neuroscience. ISSN 0270-6474. 18, s. 7296–7305.
• Samari, Hamid R. & Seglen, Per O. (1998). Inhibition of hepatocytic autophagy by adenosine, AICAR and N6-mercaptopurine riboside: Evidence for involvement of AMP-activated protein kinase. Journal of Biological Chemistry. ISSN 0021-9258. 273, s. 23758–23763.
• Strømhaug, Per E.; Berg, Trond O.; Fengsrud, Monica & Seglen, Per O. (1998). Purification and characterization of autophagosomes from rat hepatocytes. Biochemical Journal. ISSN 0264-6021. 335, s. 217–224.
• Kovács, Attila L.; Gordon, Paul B.; Grotterød, Else M. & Seglen, Per O. (1998). Inhibition of hepatocytic autophagy by adenosine, adenosine analogues and AMP. Biological chemistry. ISSN 1431-6730. 379, s. 1341–1347.
• Berg, Trond O.; Fengsrud, Monica ; Strømhaug, Per E.; Berg, Trond & Seglen, Per O. (1998). Isolation and characterization of rat liver amphisomes: Evidence for fusion of autophagosomes with both early and late endosomes. Journal of Biological Chemistry. ISSN 0021-9258. 273, s. 21883–21892.
• Seglen, Per O. (1998). Citation rates and journal impact factors are not suitable for evaluation of research. Acta Orthopaedica Scandinavica. ISSN 0001-6470. 69, s. 224–229.
• Strømhaug, Per E.; Fengsrud, Monica ; Berg, Trond Olav; Møller, Michael T. N; Grotterød, Else M. & Samari, Hamid Reza [Vis alle 12 forfattere av denne artikkelen] (1997). Regulation of autophagy by protein phosphorylation, Proteolysis in cell function. IOS Press. s. 357–366.
• Strømhaug, Per E.; Berg, Trond O.; Gjøen, Tor & Seglen, Per O. (1997). Differences between fluid-phase endocytosis (pinocytosis) and receptor-mediated endocytosis in isolated rat hepatocytes. European Journal of Cell Biology. ISSN 0171-9335. 73, s. 28–39.
• Seglen, Per O.; Berg, Trond Olav; Blankson, Henrietta; Fengsrud, Monica ; Holen, Ingunn & Strømhaug, Per E. (1996). Structural aspects of autophagy. I Suzuki, Koichi & Bond, Judith S. (Red.), Intracellular Protein Catabolism. Springer. ISSN 978-1-4613-8003-0. s. 103–11.
• Holen, Ingunn; Strømhaug, Per E.; Gordon, Paul B.; Fengsrud, Monica ; Berg, Trond Olav & Seglen, Per O. (1995). Inhibition of autophagy and multiple steps in asialoglycoprotein endocytosis by inhibitors of tyrosine protein kinases (tyrphostins). Journal of Biological Chemistry. ISSN 0021-9258. 270(21), s. 12823–31.
• Fengsrud, Monica ; Roos, Norbert; Berg, Trond; Liou, Willisa; Slot, Jan W & Seglen, Per O. (1995). Ultrastructural and immunocytochemical characterization of autophagic vacoules in isolated hepatocytes: Effects of vinblastine and asparagine on vacoule distributions. Experimental Cell Research. ISSN 0014-4827. 221, s. 504–519.
• Holen, Ingunn; Gordon, Paul B.; Strømhaug, Per E.; Berg, Trond Olav; Fengsrud, Monica & Brech, Andreas [Vis alle 9 forfattere av denne artikkelen] (1995). Inhibition of asialoglycoprotein endocytosis and degradation in rat hepatocytes by protein phosphatase inhibitors. Biochemical Journal. ISSN 0264-6021. 311, s. 317–326.

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• Klionsky, DJ; Elazar, Z; Seglen, Per O. & Rubinsztein, DC (2008). Does bafilomycin A(1) block the fusion of autophagosomes with lysosomes? Autophagy. ISSN 1554-8627. 4(7), s. 849–850.
• Klionsky, DJ; Cuervo, AM; Dunn, WA; Levine, B; van der Klei, I & Seglen, Per O. (2007). How shall I eat thee? Autophagy. ISSN 1554-8627. 3.
• Seglen, Per O. (1998). Isolation of hepatocytes. I Celis, Julio E. (Red.), Cell Biology: A Laboratory Handbook. Academic Press. ISSN 0-12-164726-9. s. 119–124.
• Laake, Jon H.; Rundén, Elise; Seglen, Per O. & Ottersen, Ole P. (1996). In vitro ischemia and phosphatase 1/2a inhibition cause selective neuronal damage in hippocampal slice cultures. Neuropharmacology. ISSN 0028-3908. 35.
• Seglen, Per O. (2004). Økologisk samspill i Bærum: Vegetasjon og insektliv på Isi. Naturvernforbundet i Bærum.
• Seglen, Per O. (2003). Biologisk mangfold i Bærum: Sommerfuglfaunaen på Isi. Naturvernforbundet i Bærum.

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