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. 1983 Oct 15;216(1):1–9. doi: 10.1042/bj2160001

Mutations that influence the secretory path in animal cells.

A M Tartakoff
PMCID: PMC1152463  PMID: 6360156

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bell J. W., Jr, Waite M. R. Envelope antigens of Sindbis virus in cells infected with temperature-sensitive mutants. J Virol. 1977 Feb;21(2):788–791. doi: 10.1128/jvi.21.2.788-791.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bergmann J. E., Tokuyasu K. T., Singer S. J. Passage of an integral membrane protein, the vesicular stomatitis virus glycoprotein, through the Golgi apparatus en route to the plasma membrane. Proc Natl Acad Sci U S A. 1981 Mar;78(3):1746–1750. doi: 10.1073/pnas.78.3.1746. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bienkowski R. S. Intracellular degradation of newly synthesized secretory proteins. Biochem J. 1983 Jul 15;214(1):1–10. doi: 10.1042/bj2140001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bourguignon L. Y., Balazovich K., Trowbridge I. S., Hyman R. Immunoelectron microscopic localization of Thy-1 glycoprotein in wild type and Thy-1-negative lymphoma cells. Cell Biol Int Rep. 1982 Aug;6(8):745–755. doi: 10.1016/0309-1651(82)90167-9. [DOI] [PubMed] [Google Scholar]
  5. Bracha M., Schlesinger M. J. Defects in RNA+ temperature-sensitive mutants of Sindbis virus and evidence for a complex of PE2-E1 viral glycoproteins. Virology. 1976 Oct 15;74(2):441–449. doi: 10.1016/0042-6822(76)90350-0. [DOI] [PubMed] [Google Scholar]
  6. Briles E. B. Lectin-resistant cell surface variants of eukaryotic cells. Int Rev Cytol. 1982;75:101–165. doi: 10.1016/s0074-7696(08)61003-7. [DOI] [PubMed] [Google Scholar]
  7. Brown D. T., Smith J. F. Morphology of BHK-21 Cells Infected with Sindbis Virus Temperature-Sensitive Mutants in Complementation Groups D and E. J Virol. 1975 May;15(5):1262–1266. doi: 10.1128/jvi.15.5.1262-1266.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Brown J. A., Jahreis G. P., Swank R. T. The synthesis and processing of beta-glucuronidase in normal and egasyn deficient mouse kidney. Biochem Biophys Res Commun. 1981 Mar 31;99(2):691–699. doi: 10.1016/0006-291x(81)91799-x. [DOI] [PubMed] [Google Scholar]
  9. Burke B., Griffiths G., Reggio H., Louvard D., Warren G. A monoclonal antibody against a 135-K Golgi membrane protein. EMBO J. 1982;1(12):1621–1628. doi: 10.1002/j.1460-2075.1982.tb01364.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Burrows P., LeJeune M., Kearney J. F. Evidence that murine pre-B cells synthesise mu heavy chains but no light chains. Nature. 1979 Aug 30;280(5725):838–840. doi: 10.1038/280838a0. [DOI] [PubMed] [Google Scholar]
  11. Champion M. J., Shows T. B. Correction of human mucolipidosis II enzyme abnormalities in somatic cell hybrids. Nature. 1977 Nov 3;270(5632):64–66. doi: 10.1038/270064a0. [DOI] [PubMed] [Google Scholar]
  12. Chapman A., Fujimoto K., Kornfeld S. The primary glycosylation defect in class E Thy-1-negative mutant mouse lymphoma cells is an inability to synthesize dolichol-P-mannose. J Biol Chem. 1980 May 25;255(10):4441–4446. [PubMed] [Google Scholar]
  13. Chapman A., Trowbridge I. S., Hyman R., Kornfeld S. Structure of the lipid-linked oligosaccharides that accumulate in class E Thy-1-negative mutant lymphomas. Cell. 1979 Jul;17(3):509–515. doi: 10.1016/0092-8674(79)90259-9. [DOI] [PubMed] [Google Scholar]
  14. Chi E. Y., Ignácio E., Lagunoff D. Mast cell granule formation in the beige mouse. J Histochem Cytochem. 1978 Feb;26(2):131–137. doi: 10.1177/26.2.624833. [DOI] [PubMed] [Google Scholar]
  15. Coffino P., Scharff M. D. Rate of somatic mutation in immunoglobulin production by mouse myeloma cells. Proc Natl Acad Sci U S A. 1971 Jan;68(1):219–223. doi: 10.1073/pnas.68.1.219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Cohen J., Beisson J. Genetic analysis of the relationships between the cell surface and the nuclei in Paramecium tetraurella. Genetics. 1980 Aug;95(4):797–818. doi: 10.1093/genetics/95.4.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Colman A., Besley J., Valle G. Interactions of mouse immunoglobulin chains within Xenopus oocytes. J Mol Biol. 1982 Sep 25;160(3):459–474. doi: 10.1016/0022-2836(82)90308-4. [DOI] [PubMed] [Google Scholar]
  18. Cook W. D., Scharff M. D. Antigen-binding mutants of mouse myeloma cells. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5687–5691. doi: 10.1073/pnas.74.12.5687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Creek K. E., Sly W. S. Adsorptive pinocytosis of phosphorylated oligosaccharides by human fibroblasts. J Biol Chem. 1982 Sep 10;257(17):9931–9937. [PubMed] [Google Scholar]
  20. Dubovi E. J., Wagner R. R. Spatial relationships of the proteins of vesicular stomatitis virus: induction of reversible oligomers by cleavable protein cross-linkers and oxidation. J Virol. 1977 May;22(2):500–509. doi: 10.1128/jvi.22.2.500-509.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Dunnick W., Rabbitts T. H., Milstein C. An immunoglobulin deletion mutant with implications for the heavy-chain switch and RNA splicing. Nature. 1980 Aug 14;286(5774):669–675. doi: 10.1038/286669a0. [DOI] [PubMed] [Google Scholar]
  22. Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L. Two mRNAs can be produced from a single immunoglobulin mu gene by alternative RNA processing pathways. Cell. 1980 Jun;20(2):313–319. doi: 10.1016/0092-8674(80)90617-0. [DOI] [PubMed] [Google Scholar]
  23. Erwin C., Brown D. T. Intracellular distribution of Sindbis virus membrane proteins in BHK-21 cells infected with wild-type virus and maturation-defective mutants. J Virol. 1980 Dec;36(3):775–786. doi: 10.1128/jvi.36.3.775-786.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Fischer H. D., Creek K. E., Sly W. S. Binding of phosphorylated oligosaccharides to immobilized phosphomannosyl receptors. J Biol Chem. 1982 Sep 10;257(17):9938–9943. [PubMed] [Google Scholar]
  25. Fitting T., Ruta M., Kabat D. Mutant cells that abnormally process plasma membrane glycoproteins encoded by murine leukemia virus. Cell. 1981 Jun;24(3):847–858. doi: 10.1016/0092-8674(81)90110-0. [DOI] [PubMed] [Google Scholar]
  26. Flamand A. Etude génétique du virus de la stomatite vésiculaire: classement de mutants thermosensibles spontanés en groupes de complémentation. J Gen Virol. 1970 Sep;8(3):187–195. doi: 10.1099/0022-1317-8-3-187. [DOI] [PubMed] [Google Scholar]
  27. Franklin E. C., Frangione B. Structural variants of human and murine immunoglobulins. Contemp Top Mol Immunol. 1975;4:89–126. doi: 10.1007/978-1-4615-8930-3_4. [DOI] [PubMed] [Google Scholar]
  28. Fratantoni J. C., Hall C. W., Neufeld E. F. Hurler and Hunter syndromes: mutual correction of the defect in cultured fibroblasts. Science. 1968 Nov 1;162(3853):570–572. doi: 10.1126/science.162.3853.570. [DOI] [PubMed] [Google Scholar]
  29. Gabel C. A., Goldberg D. E., Kornfeld S. Identification and characterization of cells deficient in the mannose 6-phosphate receptor: evidence for an alternate pathway for lysosomal enzyme targeting. Proc Natl Acad Sci U S A. 1983 Feb;80(3):775–779. doi: 10.1073/pnas.80.3.775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Gabel C. A., Kornfeld S. Lysosomal enzyme phosphorylation in mouse lymphoma cell lines with altered asparagine-linked oligosaccharides. J Biol Chem. 1982 Sep 25;257(18):10605–10612. [PubMed] [Google Scholar]
  31. Goldstein J. L., Brown M. S. The LDL receptor defect in familial hypercholesterolemia. Implications for pathogenesis and therapy. Med Clin North Am. 1982 Mar;66(2):335–362. doi: 10.1016/s0025-7125(16)31424-9. [DOI] [PubMed] [Google Scholar]
  32. Hercz A., Harpaz N. Characterization of the oligosaccharides of liver Z variant alpha 1-antitrypsin. Can J Biochem. 1980 Aug;58(8):644–648. doi: 10.1139/o80-089. [DOI] [PubMed] [Google Scholar]
  33. Hercz A., Katona E., Cutz E., Wilson J. R., Barton M. alpha1-Antitrypsin: the presence of excess mannose in the Z variant isolated from liver. Science. 1978 Sep 29;201(4362):1229–1232. doi: 10.1126/science.308696. [DOI] [PubMed] [Google Scholar]
  34. Horton M. A., Hyman R. Genetic basis for Ly-6- defect: complementation between Ly-6- and Thy-1- mutant cell lines. Immunogenetics. 1983;17(3):261–270. doi: 10.1007/BF00364410. [DOI] [PubMed] [Google Scholar]
  35. Hyman R. Studies on surface antigen variants. Isolation of two complementary variants for Thy 1.2. J Natl Cancer Inst. 1973 Feb;50(2):415–422. doi: 10.1093/jnci/50.2.415. [DOI] [PubMed] [Google Scholar]
  36. Hyman R., Trowbridge I. Analysis of lymphocyte surface antigen expression by the use of variant cell lines. Cold Spring Harb Symp Quant Biol. 1977;41(Pt 1):407–415. doi: 10.1101/sqb.1977.041.01.049. [DOI] [PubMed] [Google Scholar]
  37. Hyman R., Trowbridge I. Two complementation classes of T200 (Ly-5) glycoprotein-negative mutants. Immunogenetics. 1981 Mar 1;12(5-6):511–523. doi: 10.1007/BF01561692. [DOI] [PubMed] [Google Scholar]
  38. Jessup W., Dean R. T. Spontaneous lysosomal enzyme secretion by a murine macrophage-like cell line. Biochem J. 1980 Sep 15;190(3):847–850. doi: 10.1042/bj1900847. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Kabat D., Ruta M., Murray M. J., Polonoff E. Immunoselection of mutants deficient in cell surface glycoproteins encoded by murine erythroleukemia viruses. Proc Natl Acad Sci U S A. 1980 Jan;77(1):57–61. doi: 10.1073/pnas.77.1.57. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Klein G., Terasaki P., Billing R., Honig R., Jondal M., Rosén A., Zeuthen J., Clements G. Somatic cell hybrids between human lymphoma lines. III. Surface markers. Int J Cancer. 1977 Jan;19(1):66–76. doi: 10.1002/ijc.2910190110. [DOI] [PubMed] [Google Scholar]
  41. Kloppel T. M., Kubo R. T., Cain P. S., Browne C. P., Colon S. M., Kearney J. F., Grey H. M. Structural analysis of the mu-chains synthesized by fetal liver hybridomas. J Immunol. 1981 Apr;126(4):1346–1350. [PubMed] [Google Scholar]
  42. Knipe D. M., Baltimore D., Lodish H. F. Maturation of viral proteins in cells infected with temperature-sensitive mutants of vesicular stomatitis virus. J Virol. 1977 Mar;21(3):1149–1158. doi: 10.1128/jvi.21.3.1149-1158.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Knipe D. M., Lodish H. F., Baltimore D. Localization of two cellular forms of the vesicular stomatitis viral glycoprotein. J Virol. 1977 Mar;21(3):1121–1127. doi: 10.1128/jvi.21.3.1121-1127.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Knipe D., Lodish H. F., Baltimore D. Analysis of the defects of temperature-sensitive mutants of vesicular stomatitis virus: intracellular degradation of specific viral proteins. J Virol. 1977 Mar;21(3):1140–1148. doi: 10.1128/jvi.21.3.1140-1148.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Krag S. S., Robbins A. R. A Chinese hamster ovary cell mutant deficient in glucosylation of lipid-linked oligosaccharide synthesizes lysosomal enzymes of altered structure and function. J Biol Chem. 1982 Jul 25;257(14):8424–8431. [PubMed] [Google Scholar]
  46. Krangel M. S., Pious D., Strominger J. L. Human histocompatibility antigen mutants immunoselected in vitro. Biochemical analysis of a mutant which synthesizes an altered HLA-A2 heavy chain. J Biol Chem. 1982 May 10;257(9):5296–5305. [PubMed] [Google Scholar]
  47. Käriäinen L., Hashimoto K., Saraste J., Virtanen I., Penttinen K. Monensin and FCCP inhibit the intracellular transport of alphavirus membrane glycoproteins. J Cell Biol. 1980 Dec;87(3 Pt 1):783–791. doi: 10.1083/jcb.87.3.783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Köhler G., Howe S. C., Milstein C. Fusion between immunoglobulin-secreting and nonsecreting myeloma cell lines. Eur J Immunol. 1976 Apr;6(4):292–295. doi: 10.1002/eji.1830060411. [DOI] [PubMed] [Google Scholar]
  49. Köhler G., Potash M. J., Lehrach H., Shulman M. J. Deletions in immunoglobulin mu chains. EMBO J. 1982;1(5):555–563. doi: 10.1002/j.1460-2075.1982.tb01208.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Lafay F. Envelope proteins of vesicular stomatitis virus: effect of temperature-sensitive mutations in complementation groups III and V. J Virol. 1974 Nov;14(5):1220–1228. doi: 10.1128/jvi.14.5.1220-1228.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Laskov R., Kim K. J., Asofsky R. Induction of amplified synthesis and secretion of IgM by fusion of murine 'b lymphoma with myeloma cells. Proc Natl Acad Sci U S A. 1979 Feb;76(2):915–919. doi: 10.1073/pnas.76.2.915. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Lefort-Tran M., Aufderheide K., Pouphile M., Rossignol M., Beisson J. Control of exocytotic processes: cytological and physiological studies of trichocyst mutants in Paramecium tetraurelia. J Cell Biol. 1981 Feb;88(2):301–311. doi: 10.1083/jcb.88.2.301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Levy R., Dilley J. Rescue of immunoglobulin secretion from human neoplastic lymphoid cells by somatic cell hybridization. Proc Natl Acad Sci U S A. 1978 May;75(5):2411–2415. doi: 10.1073/pnas.75.5.2411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Liesegang B., Radbruch A., Rajewsky K. Isolation of myeloma variants with predefined variant surface immunoglobulin by cell sorting. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3901–3905. doi: 10.1073/pnas.75.8.3901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Linial M., Fenno J., Burnette W. N., Rohrschneider L. Synthesis and processing of viral glycoproteins in two nonconditional mutants of Rous sarcoma virus. J Virol. 1980 Oct;36(1):280–290. doi: 10.1128/jvi.36.1.280-290.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Lodish H. F., Kong N. Reversible block in intracellular transport and budding of mutant vesicular stomatitis virus glycoproteins. Virology. 1983 Mar;125(2):335–348. doi: 10.1016/0042-6822(83)90206-4. [DOI] [PubMed] [Google Scholar]
  57. Lodish H. F., Weiss R. A. Selective isolation of mutants of vesicular stomatitis virus defective in production of the viral glycoprotein. J Virol. 1979 Apr;30(1):177–189. doi: 10.1128/jvi.30.1.177-189.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Lohmeyer J., Klenk H. D. A mutant of influenza virus with a temperature-sensitive defect in the posttranslational processing of the hemagglutinin. Virology. 1979 Feb;93(1):134–145. doi: 10.1016/0042-6822(79)90282-4. [DOI] [PubMed] [Google Scholar]
  59. Louvard D., Reggio H., Warren G. Antibodies to the Golgi complex and the rough endoplasmic reticulum. J Cell Biol. 1982 Jan;92(1):92–107. doi: 10.1083/jcb.92.1.92. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Lusis A. J., Tomino S., Paigen K. Inheritance in mice of the membrane anchor protein egasyn: the Eg locus determines egasyn levels. Biochem Genet. 1977 Feb;15(1-2):115–122. doi: 10.1007/BF00484554. [DOI] [PubMed] [Google Scholar]
  61. Lusis A. J., Tomino S., Paigen K. Isolation, characterization, and radioimmunoassay of murine egasyn, a protein stabilizing glucuronidase membrane binding. J Biol Chem. 1976 Dec 25;251(24):7753–7760. [PubMed] [Google Scholar]
  62. Lynch R. G., Graff R. J., Sirisinha S., Simms E. S., Eisen H. N. Myeloma proteins as tumor-specific transplantation antigens. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1540–1544. doi: 10.1073/pnas.69.6.1540. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Machtiger N. A., Pancake B. A., Eberle R., Courtney R. J., Tevethia S. S., Schaffer P. A. Herpes simplex virus glycoproteins: isolation of mutants resistant to immune cytolysis. J Virol. 1980 May;34(2):336–346. doi: 10.1128/jvi.34.2.336-346.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Mains P. E., Sibley C. H. The requirement of light chain for the surface deposition of the heavy chain of immunoglobulin M. J Biol Chem. 1983 Apr 25;258(8):5027–5033. [PubMed] [Google Scholar]
  65. Mason W. S., Yeater C. A mutant of Rous sarcoma virus with a conditional defect in the determinant(s) of viral host range. Virology. 1977 Apr;77(2):443–456. doi: 10.1016/0042-6822(77)90470-6. [DOI] [PubMed] [Google Scholar]
  66. Moriuchi T., Chang H. C., Denome R., Silver J. Thy-1 cDNA sequence suggests a novel regulatory mechanism. Nature. 1983 Jan 6;301(5895):80–82. doi: 10.1038/301080a0. [DOI] [PubMed] [Google Scholar]
  67. Morrison S. L. Murine heavy chain disease. Eur J Immunol. 1978 Mar;8(3):194–199. doi: 10.1002/eji.1830080311. [DOI] [PubMed] [Google Scholar]
  68. Morrison S. L., Scharff M. D. Heavy chain-producing variants of a mouse myeloma cell line. J Immunol. 1975 Feb;114(2 Pt 1):655–659. [PubMed] [Google Scholar]
  69. Morrison S. L., Scharff M. D. Mutational events in mouse myeloma cells. Crit Rev Immunol. 1981 Sep;3(1):1–22. [PubMed] [Google Scholar]
  70. Mosmann T. R., Gravel Y., Williamson A. R., Baumal R. Modification and fate of J chain in myeloma cells in the presence and absence of polymeric immunoglobulin secretion. Eur J Immunol. 1978 Feb;8(2):94–101. doi: 10.1002/eji.1830080205. [DOI] [PubMed] [Google Scholar]
  71. Mosmann T. R., Williamson A. R. Structural mutations in a mouse immunoglobulin light chain resulting in failure to be secreted. Cell. 1980 Jun;20(2):283–292. doi: 10.1016/0092-8674(80)90614-5. [DOI] [PubMed] [Google Scholar]
  72. Mrsny R. J., Meizel S. Potassium ion influx and Na+,K+-ATPase activity are required for the hamster sperm acrosome reaction. J Cell Biol. 1981 Oct;91(1):77–82. [PMC free article] [PubMed] [Google Scholar]
  73. Murphy D. B., Jones P. P., Loken M. R., McDevitt H. O. Interaction between I region loci influences the expression of a cell surface Ia antigen. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5404–5408. doi: 10.1073/pnas.77.9.5404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Novak E. K., Swank R. T. Lysosomal dysfunctions associated with mutations at mouse pigment genes. Genetics. 1979 May;92(1):189–204. doi: 10.1093/genetics/92.1.189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Novick P., Field C., Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 1980 Aug;21(1):205–215. doi: 10.1016/0092-8674(80)90128-2. [DOI] [PubMed] [Google Scholar]
  76. Novikoff A. B., Quintana N., Mori M. Studies on the secretory process in exocrine pancreas cells. II. C57 black and beige mice. J Histochem Cytochem. 1978 Feb;26(2):83–93. doi: 10.1177/26.2.624836. [DOI] [PubMed] [Google Scholar]
  77. Ochi A., Hawley R. G., Shulman M. J., Hozumi N. Transfer of a cloned immunoglobulin light-chain gene to mutant hybridoma cells restores specific antibody production. Nature. 1983 Mar 24;302(5906):340–342. doi: 10.1038/302340a0. [DOI] [PubMed] [Google Scholar]
  78. Paigen K. Acid hydrolases as models of genetic control. Annu Rev Genet. 1979;13:417–466. doi: 10.1146/annurev.ge.13.120179.002221. [DOI] [PubMed] [Google Scholar]
  79. Palade G. Intracellular aspects of the process of protein synthesis. Science. 1975 Aug 1;189(4200):347–358. doi: 10.1126/science.1096303. [DOI] [PubMed] [Google Scholar]
  80. Parnes J. R., Seidman J. G. Structure of wild-type and mutant mouse beta 2-microglobulin genes. Cell. 1982 Jun;29(2):661–669. doi: 10.1016/0092-8674(82)90182-9. [DOI] [PubMed] [Google Scholar]
  81. Pesonen M., Saraste J., Hashimoto K., Käriäinen L. Reversible defect in the glycosylation of the membrane proteins of Semliki Forest virus ts-1 mutant. Virology. 1981 Feb;109(1):165–173. doi: 10.1016/0042-6822(81)90481-5. [DOI] [PubMed] [Google Scholar]
  82. Ploegh H. L., Cannon L. E., Strominger J. L. Cell-free translation of the mRNAs for the heavy and light chains of HLA-A and HLA-B antigens. Proc Natl Acad Sci U S A. 1979 May;76(5):2273–2277. doi: 10.1073/pnas.76.5.2273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Pringle C. R. Genetic characteristics of conditional lethal mutants of vesicular stomatitis virus induced by 5-fluorouracil, 5-azacytidine, and ethyl methane sulfonate. J Virol. 1970 May;5(5):559–567. doi: 10.1128/jvi.5.5.559-567.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Raschke W. C., Mather E. L., Koshland M. E. Assembly and secretion of pentameric IgM in a fusion between a nonsecreting B cell lymphoma and an IgG-secreting plasmacytoma. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3469–3473. doi: 10.1073/pnas.76.7.3469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Robbins A. R., Myerowitz R. The mannose 6-phosphate receptor of Chinese hamster ovary cells. Compartmentalization of acid hydrolases in mutants with altered receptors. J Biol Chem. 1981 Oct 25;256(20):10623–10627. [PubMed] [Google Scholar]
  86. Robbins A. R., Myerowitz R., Youle R. J., Murray G. J., Neville D. M., Jr The mannose 6-phosphate receptor of Chinese Hamster ovary cells. Isolation of mutants with altered receptors. J Biol Chem. 1981 Oct 25;256(20):10618–10622. [PubMed] [Google Scholar]
  87. Robbins A. R., Peng S. S., Marshall J. L. Mutant Chinese hamster ovary cells pleiotropically defective in receptor-mediated endocytosis. J Cell Biol. 1983 Apr;96(4):1064–1071. doi: 10.1083/jcb.96.4.1064. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Rosa F., Berissi H., Weissenbach J., Maroteaux L., Fellous M., Revel M. The beta2-microglobulin mRNA in human Daudi cells has a mutated initiation codon but is still inducible by interferon. EMBO J. 1983;2(2):239–243. doi: 10.1002/j.1460-2075.1983.tb01412.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Rose J. K., Bergmann J. E. Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells. Cell. 1982 Oct;30(3):753–762. doi: 10.1016/0092-8674(82)90280-x. [DOI] [PubMed] [Google Scholar]
  90. Roth J., Berger E. G. Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. J Cell Biol. 1982 Apr;93(1):223–229. doi: 10.1083/jcb.93.1.223. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Rothman J. E. The golgi apparatus: two organelles in tandem. Science. 1981 Sep 11;213(4513):1212–1219. doi: 10.1126/science.7268428. [DOI] [PubMed] [Google Scholar]
  92. Ruta M., Clarke S., Boswell B., Kabat D. Heterogeneous metabolism and subcellular localization of a potentially leukemogenic membrane glycoprotein encoded by Friend erythroleukemia virus. Isolation of viral and cellular processing mutants. J Biol Chem. 1982 Jan 10;257(1):126–134. [PubMed] [Google Scholar]
  93. Ruta M., Murray M. J., Webb M. C., Kabat D. A murine leukemia virus mutant with a temperature-sensitive defect in membrane glycoprotein synthesis. Cell. 1979 Jan;16(1):77–88. doi: 10.1016/0092-8674(79)90189-2. [DOI] [PubMed] [Google Scholar]
  94. Saraste J., von Bonsdorff C. H., Hashimoto K., Keränen S., Käriäinen L. Reversible transport defects of virus membrane glycoproteins in Sindbis virus mutant infected cells. Cell Biol Int Rep. 1980 Mar;4(3):279–286. doi: 10.1016/0309-1651(80)90060-0. [DOI] [PubMed] [Google Scholar]
  95. Saraste J., von Bonsdorff C. H., Hashimoto K., Käriäinen L., Keränen S. Semliki forest virus mutants with temperature-sensitive transport defect of envelope proteins. Virology. 1980 Jan 30;100(2):229–245. doi: 10.1016/0042-6822(80)90516-4. [DOI] [PubMed] [Google Scholar]
  96. Schmidt M. F., Schlesinger M. J. Fatty acid binding to vesicular stomatitis virus glycoprotein: a new type of post-translational modification of the viral glycoprotein. Cell. 1979 Aug;17(4):813–819. doi: 10.1016/0092-8674(79)90321-0. [DOI] [PubMed] [Google Scholar]
  97. Schmidt M. F., Schlesinger M. J. Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins. J Biol Chem. 1980 Apr 25;255(8):3334–3339. [PubMed] [Google Scholar]
  98. Secher D. S., Cotton R. G., Milstein C. Spontaneous mutation in tissue culture-chemical nature of variant immunoglobulin from mutant clones of MOPC 21. FEBS Lett. 1973 Dec 1;37(2):311–316. doi: 10.1016/0014-5793(73)80485-5. [DOI] [PubMed] [Google Scholar]
  99. Secher D. S., Milstein C., Adetugbo K. Somatic mutants and antibody diversity. Immunol Rev. 1977;36:51–72. doi: 10.1111/j.1600-065x.1977.tb00382.x. [DOI] [PubMed] [Google Scholar]
  100. Sidman C., Potash M. J., Köhler G. Roles of protein and carbohydrate in glycoprotein processing and secretion. Studies using mutants expressing altered IgM mu chains. J Biol Chem. 1981 Dec 25;256(24):13180–13187. [PubMed] [Google Scholar]
  101. Sly W. S., Fischer H. D. The phosphomannosyl recognition system for intracellular and intercellular transport of lysosomal enzymes. J Cell Biochem. 1982;18(1):67–85. doi: 10.1002/jcb.1982.240180107. [DOI] [PubMed] [Google Scholar]
  102. Smith J. F., Brown D. T. Envelopments of Sindbis virus: synthesis and organization of proteins in cells infected with wild type and maturation-defective mutants. J Virol. 1977 Jun;22(3):662–678. doi: 10.1128/jvi.22.3.662-678.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Sonenshein G. E., Siekevitz M., Siebert G. R., Gefter M. L. Control of immunoglobulin secretion in the murine plasmacytoma line MOPC 315. J Exp Med. 1978 Jul 1;148(1):301–312. doi: 10.1084/jem.148.1.301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  104. Steimer K. S., Boettiger D. Envelope assembly mutant of rous sarcoma virus. J Virol. 1980 Dec;36(3):883–888. doi: 10.1128/jvi.36.3.883-888.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Stoll J., Robbins A. R., Krag S. S. Mutant of Chinese hamster ovary cells with altered mannose 6-phosphate receptor activity is unable to synthesize mannosylphosphoryldolichol. Proc Natl Acad Sci U S A. 1982 Apr;79(7):2296–2300. doi: 10.1073/pnas.79.7.2296. [DOI] [PMC free article] [PubMed] [Google Scholar]
  106. Sveda M. M., Markoff L. J., Lai C. J. Cell surface expression of the influenza virus hemagglutinin requires the hydrophobic carboxy-terminal sequences. Cell. 1982 Sep;30(2):649–656. doi: 10.1016/0092-8674(82)90261-6. [DOI] [PubMed] [Google Scholar]
  107. Tartakoff A. M. Perturbation of the structure and function of the Golgi complex by monovalent carboxylic ionophores. Methods Enzymol. 1983;98:47–59. doi: 10.1016/0076-6879(83)98138-7. [DOI] [PubMed] [Google Scholar]
  108. Tartakoff A. M. Perturbation of vesicular traffic with the carboxylic ionophore monensin. Cell. 1983 Apr;32(4):1026–1028. doi: 10.1016/0092-8674(83)90286-6. [DOI] [PubMed] [Google Scholar]
  109. Tartakoff A. M. The Golgi complex: crossroads for vesicular traffic. Int Rev Exp Pathol. 1980;22:227–251. [PubMed] [Google Scholar]
  110. Tartakoff A. M. The confined function model of the Golgi complex: center for ordered processing of biosynthetic products of the rough endoplasmic reticulum. Int Rev Cytol. 1983;85:221–252. doi: 10.1016/S0074-7696(08)62374-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Tolleshaug H., Hobgood K. K., Brown M. S., Goldstein J. L. The LDL receptor locus in familial hypercholesterolemia: multiple mutations disrupt transport and processing of a membrane receptor. Cell. 1983 Mar;32(3):941–951. doi: 10.1016/0092-8674(83)90079-x. [DOI] [PubMed] [Google Scholar]
  112. Trowbridge I. S., Hyman R. Abnormal lipid-linked oligosaccharides in class E Thy-1-negative mutant lymphomas. Cell. 1979 Jul;17(3):503–508. doi: 10.1016/0092-8674(79)90258-7. [DOI] [PubMed] [Google Scholar]
  113. Trowbridge I. S., Hyman R., Ferson T., Mazauskas C. Expression of Thy-1 glycoprotein on lectin-resistant lymphoma cell lines. Eur J Immunol. 1978 Oct;8(10):716–723. doi: 10.1002/eji.1830081009. [DOI] [PubMed] [Google Scholar]
  114. Trowbridge I. S., Hyman R., Mazauskas C. The synthesis and properties of T25 blycoprotein in Thy-1-negative mutant lymphoma cells. Cell. 1978 May;14(1):21–32. doi: 10.1016/0092-8674(78)90297-0. [DOI] [PubMed] [Google Scholar]
  115. Valle G., Besley J., Williamson A. R., Mosmann T. R., Colman A. Post-translational fate of variant MOPC 315 lambda chains in Xenopus oocytes and mouse myeloma cells. Eur J Biochem. 1983 Apr 15;132(1):131–138. doi: 10.1111/j.1432-1033.1983.tb07337.x. [DOI] [PubMed] [Google Scholar]
  116. Williams A. F., Gagnon J. Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin. Science. 1982 May 14;216(4547):696–703. doi: 10.1126/science.6177036. [DOI] [PubMed] [Google Scholar]
  117. Winberry L., Marks A., Baumal R. Immunoglobulin production and secretion by variant clones of the MOPC 315 mouse myeloma cell line. J Immunol. 1980 Mar;124(3):1174–1182. [PubMed] [Google Scholar]
  118. Wu G. E., Hozumi N., Murialdo H. Secretion of a lambda 2 immunoglobulin chain is prevented by a single amino acid substitution in its variable region. Cell. 1983 May;33(1):77–83. doi: 10.1016/0092-8674(83)90336-7. [DOI] [PubMed] [Google Scholar]
  119. Ziemiecki A., Garoff H., Simons K. Formation of the Semliki Forest virus membrane glycoprotein complexes in the infected cell. J Gen Virol. 1980 Sep;50(1):111–123. doi: 10.1099/0022-1317-50-1-111. [DOI] [PubMed] [Google Scholar]
  120. Zilberstein A., Snider M. D., Porter M., Lodish H. F. Mutants of vesicular stomatitis virus blocked at different stages in maturation of the viral glycoprotein. Cell. 1980 Sep;21(2):417–427. doi: 10.1016/0092-8674(80)90478-x. [DOI] [PubMed] [Google Scholar]

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