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Leshets M, Ramamurthy D, Lisby M, Lehming N, Pines O. Fumarase is involved in DNA double-strand break resection through a functional interaction with Sae2. Current Genetics [Internet]. 2018;64(3):697–712. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85036591606&doi=10.1007%252fs00294-017-0786-4&partnerID=40&md5=975b06291793dde4f34560aafc7c86e7

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Singer E, Silas YBH, Ben-Yehuda S, Pines O. Bacterial fumarase and L-malic acid are evolutionary ancient components of the DNA damage response. eLife [Internet]. 2017;6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85041024652&doi=10.7554%252feLife.30927&partnerID=40&md5=d98747e31a1dd8ac3fde51200e67789c

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Dik E, Naamati A, Asraf H, Lehming N, Pines O. Human Fumarate Hydratase Is Dual Localized by an Alternative Transcription Initiation Mechanism. Traffic [Internet]. 2016;17(7):720–32. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84974685711&doi=10.1111%252ftra.12397&partnerID=40&md5=bc4718d540ca26c7fe90bd5bb12556ba

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Kalderon B, Kogan G, Bubis E, Pines O. Cytosolic Hsp60 can modulate proteasome activity in yeast. Journal of Biological Chemistry [Internet]. 2015;290(6):3542–51. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84922422474&doi=10.1074%252fjbc.M114.626622&partnerID=40&md5=2b42fa00150156922c932523d0c256b9

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Kalderon B, Pines O. Protein folding as a driving force for dual protein targeting in eukaryotes. Frontiers in Molecular Biosciences [Internet]. 2014;1(NOV). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84974687278&doi=10.3389%252ffmolb.2014.00023&partnerID=40&md5=c07cf8487256b306ec2493f70070feeb

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Kisslov I, Naamati A, Shakarchy N, Pines O. Dual-targeted proteins tend to be more evolutionarily conserved. Molecular Biology and Evolution [Internet]. 2014;31(10):2770–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84930342555&doi=10.1093%252fmolbev%252fmsu221&partnerID=40&md5=77de75e149d3608ed8110ee961dce693

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Burak E, Yogev O, Sheffer S, Schueler-Furman O, Pines O. Evolving dual targeting of a prokaryotic protein in yeast. Molecular Biology and Evolution [Internet]. 2013;30(7):1563–73. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84879406272&doi=10.1093%252fmolbev%252fmst039&partnerID=40&md5=8780715a05ecd3095043dc139d02828f

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Michot C, Hubert L, Romero NB, Gouda A, Mamoune A, Mathew S, et al. Study of LPIN1, LPIN2 and LPIN3 in rhabdomyolysis and exercise-induced myalgia. Journal of Inherited Metabolic Disease [Internet]. 2012;35(6):1119–28. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84867887549&doi=10.1007%252fs10545-012-9461-6&partnerID=40&md5=fd69d82e50e7d81d183da1f01d554a24

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Spiegel R, Pines O, Ta-Shma A, Burak E, Shaag A, Halvardson J, et al. Infantile cerebellar-retinal degeneration associated with a mutation in mitochondrial aconitase, ACO2. American Journal of Human Genetics [Internet]. 2012;90(3):518–23. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84858040979&doi=10.1016%252fj.ajhg.2012.01.009&partnerID=40&md5=16bf64f5d44f2465d39c4070f527a5ae

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Mühlenhoff U, Richter N, Pines O, Pierik AJ, Lill R. Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins. Journal of Biological Chemistry [Internet]. 2011;286(48):41205–16. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-80955125480&doi=10.1074%252fjbc.M111.296152&partnerID=40&md5=ddc0c6fb51bb42aa9aa63d19a8b93109

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Ben-Menachem R, Tal M, Shadur T, Pines O. A third of the yeast mitochondrial proteome is dual localized: A question of evolution. Proteomics [Internet]. 2011;11(23):4468–76. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-81855185408&doi=10.1002%252fpmic.201100199&partnerID=40&md5=fce442a5b5b5030813749ce5a2a1b789

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Yogev O, Naamati A, Pines O. Fumarase: A paradigm of dual targeting and dual localized functions. FEBS Journal [Internet]. 2011;278(22):4230–42. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-80255122737&doi=10.1111%252fj.1742-4658.2011.08359.x&partnerID=40&md5=4e4508522eaf607bd6d2406abf4bcf3d

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Ben-Menachem R, Regev-Rudzki N, Pines O. The aconitase C-terminal domain is an independent dual targeting element. Journal of Molecular Biology [Internet]. 2011;409(2):113–23. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-79955904604&doi=10.1016%252fj.jmb.2011.03.045&partnerID=40&md5=d6c3edadc8602bed60731c1061c4b869

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Matthews GD, Gur N, Koopman WJH, Pines O, Vardimon L. Weak mitochondrial targeting sequence determines tissue-specific subcellular localization of glutamine synthetase in liver and brain cells. Journal of Cell Science [Internet]. 2010;123(3):351–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-76649117422&doi=10.1242%252fjcs.060749&partnerID=40&md5=b132541394bd8c397db08a058a2d90bb

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Eliyahu E, Pnueli L, Melamed D, Scherrer T, Gerber AP, Pines O, et al. Tom20 mediates localization of mRNAs to mitochondria in a translation-dependent manner. Molecular and Cellular Biology [Internet]. 2010;30(1):284–94. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-73549098882&doi=10.1128%252fMCB.00651-09&partnerID=40&md5=e67165b37419ce1c37b456e2e5f4c8dd

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Naamati A, Regev-Rudzki N, Galperin S, Lill R, Pines O. Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. Journal of Biological Chemistry [Internet]. 2009;284(44):30200–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-71049136017&doi=10.1074%252fjbc.M109.034694&partnerID=40&md5=ebc2ea4f83b3e4730f3991546b8ef373

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Regev-Rudzki N, Yogev O, Pines O. The mitochondrial targeting sequence tilts the balance between mitochondrial and cytosolic dual localization. Journal of Cell Science [Internet]. 2008;121(14):2423–31. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-49649109965&doi=10.1242%252fjcs.029207&partnerID=40&md5=e96dd580f997140c0987684ccf00d075

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Dinur-Mills M, Tal M, Pines O. Dual targeted mitochondrial proteins are characterized by lower MTS parameters and total net charge. PLoS ONE [Internet]. 2008;3(5). Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-47749097978&doi=10.1371%252fjournal.pone.0002161&partnerID=40&md5=3bf3b355895f314af7116bcfe9129734

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Yogev O, Karniely S, Pines O. Translation-coupled translocation of yeast fumarase into mitochondria in vivo. Journal of Biological Chemistry [Internet]. 2007;282(40):29222–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-35748984947&doi=10.1074%252fjbc.M704201200&partnerID=40&md5=6478384377fdd5de050a29245903425b

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Hadas Y, Goldberg I, Pines O, Prusky D. Involvement of gluconic acid and glucose oxidase in the pathogenicity of Penicillium expansum in apples. Phytopathology [Internet]. 2007;97(3):384–90. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33847371123&doi=10.1094%252fPHYTO-97-3-0384&partnerID=40&md5=b56c9750b26e4012088265268b34ea33

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Shlevin L, Regev-Rudzki N, Karniely S, Pines O. Location-specific depletion of a dual-localized protein. Traffic [Internet]. 2007;8(2):169–76. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33846251261&doi=10.1111%252fj.1600-0854.2006.00518.x&partnerID=40&md5=ee00144bd0b424985f66d98c39304663

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Karniely S, Rayzner A, Sass E, Pines O. α-Complementation as a probe for dual localization of mitochondrial proteins. Experimental Cell Research [Internet]. 2006;312(19):3835–46. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33750375536&doi=10.1016%252fj.yexcr.2006.08.021&partnerID=40&md5=4646058c1327f9ffa2895d5b9a586a39

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Goldberg I, Rokem JS, Pines O. Organic acids: Old metabolites, new themes. Journal of Chemical Technology and Biotechnology [Internet]. 2006;81(10):1601–11. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33749333439&doi=10.1002%252fjctb.1590&partnerID=40&md5=75316bcb74e7702d4d450bdb5ca305be

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Karniely S, Regev-Rudzki N, Pines O. The Presequence of Fumarase is Exposed to the Cytosol during Import into Mitochondria. Journal of Molecular Biology [Internet]. 2006;358(2):396–405. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-33646109080&doi=10.1016%252fj.jmb.2006.02.023&partnerID=40&md5=a02eb8a073fd3d12e10e2bd0029e2a62

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Regev-Rudzki N, Karniely S, Ben-Haim NN, Pines O. Yeast aconitase in two locations and two metabolic pathways: Seeing small amounts is believing. Molecular Biology of the Cell [Internet]. 2005;16(9):4163–71. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-24344441532&doi=10.1091%252fmbc.E04-11-1028&partnerID=40&md5=f2179012e8f40bff857621cea22a7e0a

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Karniely S, Pines O. Single translation-dual destination: Mechanisms of dual protein targeting in eukaryotes. EMBO Reports [Internet]. 2005;6(5):420–5. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-20044387943&doi=10.1038%252fsj.embor.7400394&partnerID=40&md5=0059c891b11ec2f2e1e4dee3e9ee52c0

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Sass E, Karniely S, Pines O. Folding of Fumarase during Mitochondrial Import Determines its Dual Targeting in Yeast. Journal of Biological Chemistry [Internet]. 2003;278(46):45109–16. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0242413667&doi=10.1074%252fjbc.M302344200&partnerID=40&md5=16f0cd3af68614c79b02dfb5a07d5951

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Drori N, Kramer-Haimovich H, Rollins J, Dinoor A, Okon Y, Pines O, et al. External pH and nitrogen source affect secretion of pectate lyase by Colletotrichum gloeosporioides. Applied and Environmental Microbiology [Internet]. 2003;69(6):3258–62. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0037641220&doi=10.1128%252fAEM.69.6.3258-3262.2003&partnerID=40&md5=8eb99685baa629bc16fab589f060783d

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Bressler E, Pines O, Goldberg I, Braun S. Conversion of fumaric acid to L-malic by sol-gel immobilized Saccharomyces cerevisiae in a supported liquid membrane bioreactor. Biotechnology Progress [Internet]. 2002;18(3):445–50. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035988002&doi=10.1021%252fbp010139t&partnerID=40&md5=c8de93b5cdbcf7c36e44ed81fc3f938d

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Sass E, Blachinsky E, Karniely S, Pines O. Mitochondrial and Cytosolic Isoforms of Yeast Fumarase Are Derivatives of a Single Translation Product and Have Identical Amino Termini. Journal of Biological Chemistry [Internet]. 2001;276(49):46111–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0035824654&doi=10.1074%252fjbc.M106061200&partnerID=40&md5=f20050c1ec490703ce3582f524fe192c

56.

Yakoby N, Beno-Moualem D, Keen NT, Dinoor A, Pines O, Prusky D. Colletotrichum gloeosporioides pelB is an important virulence factor in avocado fruit-fungus interaction. Molecular Plant-Microbe Interactions [Internet]. 2001;14(8):988–95. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034921938&doi=10.1094%252fMPMI.2001.14.8.988&partnerID=40&md5=2b42a69c2ba3bf58c936f279aef34db1

57.

Pines O, Inouye M. Expression and secretion of proteins in E. coli. Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology [Internet]. 1999;12(1):25–34. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032707339&doi=10.1385%252fMB%253a12%253a1%253a25&partnerID=40&md5=c63235a4fd0535a22bbaee0e58b1af0b

58.

Knox C, Sass E, Neupert W, Pines O. Import into mitochondria, folding and retrograde movement of fumarase in yeast. Journal of Biological Chemistry [Internet]. 1998;273(40):25587–93. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032475958&doi=10.1074%252fjbc.273.40.25587&partnerID=40&md5=c8da65fb4051e0e040a457f9df5e2940

59.

Pines O, Shemesh S, Battat E, Goldberg I. Overexpression of cytosolic malate dehydrogenase (MDH2) causes overproduction of specific organic acids in Saccharomyces cerevisiae. Applied Microbiology and Biotechnology [Internet]. 1997;48(2):248–55. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030858003&doi=10.1007%252fs002530051046&partnerID=40&md5=e69e0adb787c54990a3df63c4bcf2a88

60.

Pines O, Inouye M. Expression and secretion of proteins in E. coli. Methods in molecular biology (Clifton, NJ) [Internet]. 1997;62:73–87. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030642164&partnerID=40&md5=a421b47d781c8537493733045756486b

61.

Pines O, Even-Ram S, Elnathan N, Battat E, Aharonov O, Gibson D, et al. The cytosolic pathway of L-malic acid synthesis in Saccharomyces cerevisiae: The role of fumarase. Applied Microbiology and Biotechnology [Internet]. 1996;46(4):393–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029801279&doi=10.1007%252fs002530050835&partnerID=40&md5=7c15bc1580a205052e5d30afa4fa6f56

62.

Schonberger O, Knox C, Bibi E, Pines O. Split invertase polypeptides form functional complexes in the yeast periplasm in vivo. Proceedings of the National Academy of Sciences of the United States of America [Internet]. 1996;93(18):9612–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029835280&doi=10.1073%252fpnas.93.18.9612&partnerID=40&md5=3a7e3d446dd52039df5ca0a1ed65ac25

63.

Geller D, Taglicht D, Edgar R, Tam A, Pines O, Michaelis S, et al. Comparative topology studies in Saccharomyces cerevisiae and in Escherichia coli: The N-terminal half of the yeast ABC protein Ste6. Journal of Biological Chemistry [Internet]. 1996;271(23):13746–53. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0030011712&doi=10.1074%252fjbc.271.23.13746&partnerID=40&md5=0ebef18f9326e28ddeff63076c7b210f

64.

Stein I, Peleg Y, Even-Ram S, Pines O. The single translation product of the FUM1 gene (fumarase) is processed in mitochondria before being distributed between the cytosol and mitochondria in Saccharomyces cerevisiae. Molecular and Cellular Biology [Internet]. 1994;14(7):4770–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028233427&doi=10.1128%252fMCB.14.7.4770&partnerID=40&md5=45dfce7cd802b74e6f674e51343fa07b

65.

Davidov Y, Rahat A, Flechner I, Pines O. Characterization of the rnc-97 mutation of RNAaseIII: A glycine to glutamate substitution increases the requirement for magnesium ions. Journal of General Microbiology [Internet]. 1993;139(4):717–24. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0027278089&doi=10.1099%252f00221287-139-4-717&partnerID=40&md5=df7b0527ffc5bca9ad4a74f713d73acc

66.

Pines O, Shani O. Elimination of the disulphide bond alters the conformation of mature lipo-β-lactamase in yeast. Applied Microbiology and Biotechnology [Internet]. 1992;38(1):67–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026452483&doi=10.1007%252fBF00169421&partnerID=40&md5=7f701f8d5157d3cc817bf00b48bbbd12

67.

Davidov Y, Zivion G, Pines O. Ribonuclease III reduces the efficiency of bacteriophage gy1 propagation in E. coli. Current Microbiology [Internet]. 1992;24(2):63–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026710695&doi=10.1007%252fBF01570899&partnerID=40&md5=c4cc91233de5a27d88bdd00c12da769a

68.

Shani O, Pines O. The relationship between disulphide bond formation, processing and secretion of lipo‐β‐lactamase in yeast. Molecular Microbiology [Internet]. 1992;6(2):189–95. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026584618&doi=10.1111%252fj.1365-2958.1992.tb02000.x&partnerID=40&md5=884dee0b4c4de91b0ea5151531ba1167

69.

Neufeld RJ, Peleg Y, Rokem JS, Pines O, Goldberg I. l-Malic acid formation by immobilized Saccharomyces cerevisiae amplified for fumarase. Enzyme and Microbial Technology [Internet]. 1991;13(12):991–6. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026410778&doi=10.1016%2f0141-0229%2891%2990122-Q&partnerID=40&md5=9aa327f711a53d2f8b2ee1b79452ca92

70.

Schonberger O, Hirst TR, Pines O. Targeting and assembly of an oligomeric bacterial enterotoxoid in the endoplasmic reticulum of Saccharomyces cerevisiae. Molecular Microbiology [Internet]. 1991;5(11):2663–71. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025930765&doi=10.1111%252fj.1365-2958.1991.tb01975.x&partnerID=40&md5=24e2a813334ac431c2b357440ee00d21

71.

Pines O, London A. Expression and secretion of staphylococcal nuclease in yeast: Effects of amino-terminal sequences. Journal of General Microbiology [Internet]. 1991;137(4):771–8. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025767689&doi=10.1099%252f00221287-137-4-771&partnerID=40&md5=3f76afe6caee13b0cd7530f05881b582

72.

London A, Pines O. Specific β‐lactam antibiotics inhibit secretion of lipo‐β‐lactamase in yeast. Molecular Microbiology [Internet]. 1990;4(12):2193–200. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025647126&doi=10.1111%252fj.1365-2958.1990.tb00581.x&partnerID=40&md5=f6c0266e5d4b75f963554a70b6885f9b

73.

Peleg Y, Rokem JS, Goldberg I, Pines O. Inducible overexpression of the FUM1 gene in Saccharomyces cerevisiae: Localization of fumarase and efficient fumaric acid bioconversion to L-malic acid. Applied and Environmental Microbiology [Internet]. 1990;56(9):2777–83. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0025075097&doi=10.1128%252faem.56.9.2777-2783.1990&partnerID=40&md5=d1895b58c027e92ed16064989fc36b8e

74.

Pines O, Shoham Y, Rosenberg E, Gutnick D. Unmasking of surface components by removal of cell-associated emulsan from Acinetobacter Sp. RAG-1. Applied Microbiology and Biotechnology [Internet]. 1988;28(1):93–9. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-9444226788&doi=10.1007%252fBF00250505&partnerID=40&md5=54bed541828dc13797097f4c6e729657

75.

Pines O, Yoon HJ, Inouye M. Expression of double-stranded-RNA-specific RNase III of Escherichia coli is lethal to Saccharomyces cerevisiae. Journal of bacteriology [Internet]. 1988;170(7):2989–93. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0024043138&doi=10.1128%252fjb.170.7.2989-2993.1988&partnerID=40&md5=cba7412dc205256badaa58182cedca69

76.

Pines O, Lunn CA, Inouye M. Defective Escherichia coli signal peptides function in yeast. Molecular Microbiology [Internet]. 1988;2(2):209–17. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023973940&doi=10.1111%252fj.1365-2958.1988.tb00022.x&partnerID=40&md5=66cf4f76e2c66148435fc48e398d9f21

77.

Andersen J, Delihas N, Ikenaka K, Green PJ, Pines O, Ilercil O, et al. The isolation and characterization of RNA coded by the micF gene in Escherichia coli. Nucleic Acids Research [Internet]. 1987;15(5):2089–101. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023650604&doi=10.1093%252fnar%252f15.5.2089&partnerID=40&md5=a18701ed13154d99a93fe25f43b1dc6d

78.

Pines O, Gutnick D. Role for emulsan in growth of Acinetobacter calcoaceticus RAG-1 on crude oil. Applied and Environmental Microbiology [Internet]. 1986;51(3):661–3. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022619721&doi=10.1128%252faem.51.3.661-663.1986&partnerID=40&md5=5b349929eb38d822de6e9a9ee1a811d1

79.

Green PJ, Pines O, Inouye M. The role of antisense RNA in gene regulation. Annual Review of Biochemistry [Internet]. 1986;VOL. 55:569–97. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0022555863&doi=10.1146%252fannurev.bi.55.070186.003033&partnerID=40&md5=7acedf47f7b43204c9d3a63e1c4464da

80.

Pines O, Inouye M. Antisense RNA regulation in prokaryotes. Trends in Genetics [Internet]. 1986;2(C):284–7. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0003738172&doi=10.1016%2f0168-9525%2886%2990270-2&partnerID=40&md5=92726cf298cff84b531c27eec70e30d9

81.

Pines O, Gutnick D. Specific binding of a bacteriophage at a hydrocarbon-water interface. Journal of Bacteriology [Internet]. 1984;157(1):179–83. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021355935&partnerID=40&md5=aacaeeb26ed2a94b502429a74d2a2f16

82.

Pines O, Gutnick D. Alternate hydrophobic sites on the cell surface of Acinetobacter calcoaceticus RAG-1. FEMS Microbiology Letters [Internet]. 1984;22(3):307–11. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0021266921&doi=10.1111%252fj.1574-6968.1984.tb00746.x&partnerID=40&md5=ce3c195105642b95d798787b5a30cca1

83.

Rosenberg E, Kaplan N, Pines O, Rosenberg M, Gutnick D. Capsular polysaccharides interfere with adherence of Acinetobacter calcoaceticus to hydrocarbon. FEMS Microbiology Letters [Internet]. 1983;17(1–3):157–60. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020636770&doi=10.1111%252fj.1574-6968.1983.tb00392.x&partnerID=40&md5=ed0606937e033578e705fdd3be00dd71

84.

Pines O, Bayer EA, Gutnick DL. Localization of emulsan-like polymers associated with the cell surface of Acinetobacter calcoaceticus. Journal of Bacteriology [Internet]. 1983;154(2):893–905. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0020535257&partnerID=40&md5=09f24034356b86ef0edfb9d86298d4a4

85.

Pines O, Gutnick DL. Relationship between phage resistance and emulsan production, interaction of phages with the cell-surface of Acinetobacter calcoaceticus RAG-1. Archives of Microbiology [Internet]. 1981;130(2):129–33. Available from: https://www.scopus.com/inward/record.uri?eid=2-s2.0-0019792023&doi=10.1007%252fBF00411064&partnerID=40&md5=7a53c3c8d2f6e619eabfcf0e2d63e564