Year |
Citation |
Score |
2010 |
Moore DD, Sefton BM, Shaw RJ, Turk BE. Analysis of protein phosphorylation: Introduction Current Protocols in Molecular Biology. 18.0.1-18.0.3. DOI: 10.1002/0471142727.mb1800s78 |
0.44 |
|
2007 |
Mitchell JL, Trible RP, Emert-Sedlak LA, Weis DD, Lerner EC, Applen JJ, Sefton BM, Smithgall TE, Engen JR. Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein. Journal of Molecular Biology. 366: 1282-93. PMID 17207813 DOI: 10.1016/J.Jmb.2006.12.026 |
0.516 |
|
2006 |
Weis DD, Kjellen P, Sefton BM, Engen JR. Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Protein Science : a Publication of the Protein Society. 15: 2402-10. PMID 17008721 DOI: 10.1110/Ps.052016406 |
0.397 |
|
2005 |
Sims PA, Wong CF, Vuga D, McCammon JA, Sefton BM. Relative contributions of desolvation, inter- and intramolecular interactions to binding affinity in protein kinase systems. Journal of Computational Chemistry. 26: 668-81. PMID 15754303 DOI: 10.1002/Jcc.20207 |
0.369 |
|
2003 |
Schulte RJ, Sefton BM. Inhibition of the activity of SRC and Abl tyrosine protein kinases by the binding of the Wiskott-Aldrich syndrome protein. Biochemistry. 42: 9424-30. PMID 12899629 DOI: 10.1021/bi034519u |
0.477 |
|
2002 |
Kjellen P, Amdjadi K, Lund TC, Medveczky PG, Sefton BM. The herpesvirus saimiri tip484 and tip488 proteins both stimulate lck tyrosine protein kinase activity in vivo and in vitro. Virology. 297: 281-8. PMID 12083826 DOI: 10.1006/Viro.2002.1419 |
0.768 |
|
2001 |
Sefton BM. Detection of phosphorylation by immunological techniques. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit13.4. PMID 18429116 DOI: 10.1002/0471140864.Ps1304S00 |
0.395 |
|
2001 |
Sefton BM. Phosphoamino acid analysis. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit13.3. PMID 18429115 DOI: 10.1002/0471140864.Ps1303S04 |
0.478 |
|
2001 |
Sefton BM. Labeling cultured cells with 32P(i) and preparing cell lysates for immunoprecipitation. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit13.2. PMID 18429114 DOI: 10.1002/0471140864.Ps1302S10 |
0.343 |
|
2001 |
Sefton BM, Shenolikar S. Overview of protein phosphorylation. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit13.1. PMID 18429113 DOI: 10.1002/0471140864.Ps1301S00 |
0.508 |
|
2001 |
Sefton BM. Analysis of phosphorylation of unlabeled proteins. Current Protocols in Molecular Biology / Edited by Frederick M. Ausubel ... [Et Al.]. Unit 18.4. PMID 18265169 DOI: 10.1002/0471142727.Mb1804S40 |
0.462 |
|
2001 |
Sefton BM. Phosphoamino acid analysis. Current Protocols in Molecular Biology / Edited by Frederick M. Ausubel ... [Et Al.]. Unit 18.3. PMID 18265168 DOI: 10.1002/0471142727.Mb1803S40 |
0.481 |
|
2001 |
Sefton BM. Labeling cultured cells with 32P(i) and preparing cell lysates for immunoprecipitation. Current Protocols in Molecular Biology / Edited by Frederick M. Ausubel ... [Et Al.]. Unit 18.2. PMID 18265167 DOI: 10.1002/0471142727.Mb1802S40 |
0.322 |
|
2001 |
Sefton BM, Shenolikar S. Overview of protein phosphorylation. Current Protocols in Molecular Biology / Edited by Frederick M. Ausubel ... [Et Al.]. Unit 18.1. PMID 18265166 DOI: 10.1002/0471142727.mb1801s33 |
0.457 |
|
2001 |
Sefton BM. Phosphoamino acid analysis. Current Protocols in Cell Biology / Editorial Board, Juan S. Bonifacino ... [Et Al.]. Unit 14.5. PMID 18228327 DOI: 10.1002/0471143030.Cb1405S03 |
0.484 |
|
2001 |
Sefton BM. Labeling cultured cells with 32Pi and preparing cell lysates for immunoprecipitation. Current Protocols in Cell Biology / Editorial Board, Juan S. Bonifacino ... [Et Al.]. Unit 14.4. PMID 18228326 DOI: 10.1002/0471143030.Cb1404S03 |
0.407 |
|
2001 |
Sefton BM. Overview of protein phosphorylation. Current Protocols in Cell Biology / Editorial Board, Juan S. Bonifacino ... [Et Al.]. Unit 14.1. PMID 18228324 DOI: 10.1002/0471143030.Cb1401S00 |
0.558 |
|
2001 |
Chiang GG, Sefton BM. Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase. The Journal of Biological Chemistry. 276: 23173-8. PMID 11294838 DOI: 10.1074/Jbc.M101219200 |
0.733 |
|
2000 |
Hartley DA, Amdjadi K, Hurley TR, Lund TC, Medveczky PG, Sefton BM. Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions. Virology. 276: 339-48. PMID 11040125 DOI: 10.1006/Viro.2000.0570 |
0.726 |
|
2000 |
Amdjadi K, Sefton BM. Ultraviolet light-induced stimulation of the JNK mitogen-activated protein kinase in the absence of src family tyrosine kinase activation. The Journal of Biological Chemistry. 275: 22520-5. PMID 10801851 DOI: 10.1074/Jbc.M002573200 |
0.742 |
|
2000 |
Chiang GG, Sefton BM. Phosphorylation of a Src kinase at the autophosphorylation site in the absence of Src kinase activity. The Journal of Biological Chemistry. 275: 6055-8. PMID 10692391 DOI: 10.1074/Jbc.275.9.6055 |
0.69 |
|
1999 |
Lund TC, Coleman C, Horvath E, Sefton BM, Jove R, Medveczky MM, Medveczky PG. The Src-family kinase Lck can induce STAT3 phosphorylation and DNA binding activity. Cellular Signalling. 11: 789-96. PMID 10617281 DOI: 10.1016/S0898-6568(99)00045-5 |
0.457 |
|
1999 |
Hartley DA, Hurley TR, Hardwick JS, Lund TC, Medveczky PG, Sefton BM. Activation of the lck tyrosine-protein kinase by the binding of the tip protein of herpesvirus saimiri in the absence of regulatory tyrosine phosphorylation. The Journal of Biological Chemistry. 274: 20056-9. PMID 10400611 DOI: 10.1074/Jbc.274.29.20056 |
0.577 |
|
1998 |
Patturajan M, Schulte RJ, Sefton BM, Berezney R, Vincent M, Bensaude O, Warren SL, Corden JL. Growth-related changes in phosphorylation of yeast RNA polymerase II. The Journal of Biological Chemistry. 273: 4689-94. PMID 9468530 DOI: 10.1074/Jbc.273.8.4689 |
0.397 |
|
1997 |
Hardwick JS, Sefton BM. The activated form of the Lck tyrosine protein kinase in cells exposed to hydrogen peroxide is phosphorylated at both Tyr-394 and Tyr-505. The Journal of Biological Chemistry. 272: 25429-32. PMID 9325251 DOI: 10.1074/Jbc.272.41.25429 |
0.539 |
|
1996 |
Yurchak LK, Hardwick JS, Amrein K, Pierno K, Sefton BM. Stimulation of phosphorylation of Tyr394 by hydrogen peroxide reactivates biologically inactive, non-membrane-bound forms of Lck. The Journal of Biological Chemistry. 271: 12549-54. PMID 8647864 DOI: 10.1074/Jbc.271.21.12549 |
0.549 |
|
1995 |
Yurchak LK, Sefton BM. Palmitoylation of either Cys-3 or Cys-5 is required for the biological activity of the Lck tyrosine protein kinase. Molecular and Cellular Biology. 15: 6914-22. PMID 8524258 DOI: 10.1128/Mcb.15.12.6914 |
0.567 |
|
1995 |
Hardwick JS, Sefton BM. Activation of the Lck tyrosine protein kinase by hydrogen peroxide requires the phosphorylation of Tyr-394. Proceedings of the National Academy of Sciences of the United States of America. 92: 4527-31. PMID 7538674 DOI: 10.1073/Pnas.92.10.4527 |
0.554 |
|
1994 |
Wright DD, Sefton BM, Kamps MP. Oncogenic activation of the Lck protein accompanies translocation of the LCK gene in the human HSB2 T-cell leukemia. Molecular and Cellular Biology. 14: 2429-37. PMID 8139546 |
0.663 |
|
1994 |
Schulte RJ, Campbell MA, Fischer WH, Sefton BM. Tyrosine phosphorylation of VCP, the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein, is unusually sensitive to stimulation by sodium vanadate and hydrogen peroxide. Journal of Immunology (Baltimore, Md. : 1950). 153: 5465-72. PMID 7989749 |
0.504 |
|
1994 |
Sefton BM, Taddie JA. Role of tyrosine kinases in lymphocyte activation. Current Opinion in Immunology. 6: 372-9. PMID 7917104 DOI: 10.1016/0952-7915(94)90115-5 |
0.545 |
|
1994 |
Taddie JA, Hurley TR, Sefton BM. B-cell activation by wild type and mutant Ig-beta cytoplasmic domains. Advances in Experimental Medicine and Biology. 365: 23-34. PMID 7887308 DOI: 10.1007/978-1-4899-0987-9_3 |
0.393 |
|
1993 |
Hurley TR, Hyman R, Sefton BM. Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases. Molecular and Cellular Biology. 13: 1651-6. PMID 8441403 DOI: 10.1128/Mcb.13.3.1651 |
0.506 |
|
1993 |
Cahir McFarland ED, Hurley TR, Pingel JT, Sefton BM, Shaw A, Thomas ML. Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor. Proceedings of the National Academy of Sciences of the United States of America. 90: 1402-6. PMID 8433999 DOI: 10.1073/Pnas.90.4.1402 |
0.339 |
|
1993 |
Howard PK, Sefton BM, Firtel RA. Tyrosine phosphorylation of actin in Dictyostelium associated with cell-shape changes. Science (New York, N.Y.). 259: 241-4. PMID 7678470 DOI: 10.1126/Science.7678470 |
0.463 |
|
1992 |
Adler HT, Sefton BM. Generation and characterization of transforming variants of the lck tyrosine protein kinase. Oncogene. 7: 1191-9. PMID 1594248 |
0.388 |
|
1992 |
Campbell MA, Sefton BM. Association between B-lymphocyte membrane immunoglobulin and multiple members of the Src family of protein tyrosine kinases. Molecular and Cellular Biology. 12: 2315-21. PMID 1569953 DOI: 10.1128/Mcb.12.5.2315 |
0.517 |
|
1992 |
Howard PK, Sefton BM, Firtel RA. Analysis of a spatially regulated phosphotyrosine phosphatase identifies tyrosine phosphorylation as a key regulatory pathway in Dictyostelium. Cell. 71: 637-47. PMID 1423620 DOI: 10.1016/0092-8674(92)90597-6 |
0.435 |
|
1992 |
Reynolds PJ, Hurley TR, Sefton BM. Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase. Oncogene. 7: 1949-55. PMID 1408136 |
0.458 |
|
1992 |
Luo K, Sefton BM. Activated lck tyrosine protein kinase stimulates antigen-independent interleukin-2 production in T cells. Molecular and Cellular Biology. 12: 4724-32. PMID 1383689 DOI: 10.1128/Mcb.12.10.4724 |
0.434 |
|
1992 |
Schulte RJ, Campbell MA, Fischer WH, Sefton BM. Tyrosine phosphorylation of CD22 during B cell activation. Science (New York, N.Y.). 258: 1001-4. PMID 1279802 DOI: 10.1126/Science.1279802 |
0.471 |
|
1992 |
Hurley TR, Amrein KE, Sefton BM. Creation and characterization of temperature-sensitive mutants of the lck tyrosine protein kinase. Journal of Virology. 66: 7406-13. PMID 1279202 DOI: 10.1128/Jvi.66.12.7406-7413.1992 |
0.486 |
|
1991 |
Sefton BM. Measurement of stoichiometry of protein phosphorylation by biosynthetic labeling. Methods in Enzymology. 201: 245-51. PMID 1943767 DOI: 10.1016/0076-6879(91)01022-T |
0.513 |
|
1991 |
Luo KX, Hurley TR, Sefton BM. Cyanogen bromide cleavage and proteolytic peptide mapping of proteins immobilized to membranes. Methods in Enzymology. 201: 149-52. PMID 1943761 DOI: 10.1016/0076-6879(91)01014-S |
0.401 |
|
1991 |
Sefton BM. The lck tyrosine protein kinase. Oncogene. 6: 683-6. PMID 1905004 |
0.461 |
|
1991 |
Sefton BM, Campbell MA. The role of tyrosine protein phosphorylation in lymphocyte activation. Annual Review of Cell Biology. 7: 257-74. PMID 1667083 DOI: 10.1146/Annurev.Cb.07.110191.001353 |
0.482 |
|
1990 |
Luo KX, Sefton BM. Analysis of the sites in p56lck whose phosphorylation is induced by tetradecanoyl phorbol acetate. Oncogene. 5: 803-8. PMID 2359619 |
0.422 |
|
1990 |
Campbell MA, Sefton BM. Protein tyrosine phosphorylation is induced in murine B lymphocytes in response to stimulation with anti-immunoglobulin. The Embo Journal. 9: 2125-31. PMID 2357961 |
0.426 |
|
1990 |
Luo KX, Sefton BM. Cross-linking of T-cell surface molecules CD4 and CD8 stimulates phosphorylation of the lck tyrosine protein kinase at the autophosphorylation site. Molecular and Cellular Biology. 10: 5305-13. PMID 2118992 |
0.335 |
|
1990 |
Reynolds PJ, Lesley J, Trotter J, Schulte R, Hyman R, Sefton BM. Changes in the relative abundance of type I and type II lck mRNA transcripts suggest differential promoter usage during T-cell development. Molecular and Cellular Biology. 10: 4266-70. PMID 2115123 DOI: 10.1128/Mcb.10.8.4266 |
0.318 |
|
1989 |
Hurley TR, Luo K, Sefton BM. Activators of protein kinase C induce dissociation of CD4, but not CD8, from p56lck. Science (New York, N.Y.). 245: 407-9. PMID 2787934 DOI: 10.1126/Science.2787934 |
0.393 |
|
1989 |
Shaw AS, Amrein KE, Hammond C, Stern DF, Sefton BM, Rose JK. The lck tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell. 59: 627-36. PMID 2582490 DOI: 10.1016/0092-8674(89)90008-1 |
0.675 |
|
1989 |
Kamps MP, Sefton BM. Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. Analytical Biochemistry. 176: 22-7. PMID 2540676 DOI: 10.1016/0003-2697(89)90266-2 |
0.655 |
|
1989 |
Ostergaard HL, Shackelford DA, Hurley TR, Johnson P, Hyman R, Sefton BM, Trowbridge IS. Expression of CD45 alters phosphorylation of the lck-encoded tyrosine protein kinase in murine lymphoma T-cell lines. Proceedings of the National Academy of Sciences of the United States of America. 86: 8959-63. PMID 2530588 DOI: 10.1073/Pnas.86.22.8959 |
0.432 |
|
1989 |
Sefton BM. Protein kinases. Cancer Cells (Cold Spring Harbor, N.Y. : 1989). 1: 64-5. PMID 2484276 |
0.464 |
|
1989 |
Hurley TR, Sefton BM. Analysis of the activity and phosphorylation of the lck protein in lymphoid cells. Oncogene. 4: 265-72. PMID 2468122 |
0.515 |
|
1988 |
Amrein KE, Sefton BM. Mutation of a site of tyrosine phosphorylation in the lymphocyte-specific tyrosine protein kinase, p56lck, reveals its oncogenic potential in fibroblasts. Proceedings of the National Academy of Sciences of the United States of America. 85: 4247-51. PMID 3380789 DOI: 10.1073/Pnas.85.12.4247 |
0.612 |
|
1988 |
Kamps MP, Sefton BM. Most of the substrates of oncogenic viral tyrosine protein kinases can be phosphorylated by cellular tyrosine protein kinases in normal cells. Oncogene Research. 3: 105-15. PMID 2465525 |
0.733 |
|
1988 |
Kamps MP, Sefton BM. Identification of multiple novel polypeptide substrates of the v-src, v-yes, v-fps, v-ros, and v-erb-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine. Oncogene. 2: 305-15. PMID 2452398 |
0.58 |
|
1987 |
Buss JE, Mumby SM, Casey PJ, Gilman AG, Sefton BM. Myristoylated alpha subunits of guanine nucleotide-binding regulatory proteins. Proceedings of the National Academy of Sciences of the United States of America. 84: 7493-7. PMID 3118369 DOI: 10.1073/Pnas.84.21.7493 |
0.312 |
|
1986 |
Nigg EA, Sefton BM, Singer SJ, Vogt PK. Cytoskeletal organization, vinculin-phosphorylation, and fibronectin expression in transformed fibroblasts with different cell morphologies. Virology. 151: 50-65. PMID 3083582 DOI: 10.1016/0042-6822(86)90103-0 |
0.405 |
|
1986 |
Voronova AF, Sefton BM. Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertion. Nature. 319: 682-5. PMID 3081813 DOI: 10.1038/319682A0 |
0.555 |
|
1986 |
Buss JE, Kamps MP, Gould K, Sefton BM. The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity. Journal of Virology. 58: 468-74. PMID 3009860 DOI: 10.1128/Jvi.58.2.468-474.1986 |
0.739 |
|
1986 |
Kamps MP, Buss JE, Sefton BM. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation. Cell. 45: 105-12. PMID 3006923 DOI: 10.1016/0092-8674(86)90542-8 |
0.733 |
|
1986 |
Sefton BM, Hunter T. From c-src to v-src, or the case of the missing C terminus. Cancer Surveys. 5: 159-72. PMID 2430701 |
0.451 |
|
1986 |
Kamps MP, Sefton BM. Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src. Molecular and Cellular Biology. 6: 751-7. PMID 2430174 DOI: 10.1128/Mcb.6.3.751 |
0.731 |
|
1986 |
Patschinsky T, Hunter T, Sefton BM. Phosphorylation of the transforming protein of Rous sarcoma virus: direct demonstration of phosphorylation of serine 17 and identification of an additional site of tyrosine phosphorylation in p60v-src of Prague Rous sarcoma virus. Journal of Virology. 59: 73-81. PMID 2423705 DOI: 10.1128/Jvi.59.1.73-81.1986 |
0.52 |
|
1986 |
Sefton BM. The viral tyrosine protein kinases. Current Topics in Microbiology and Immunology. 123: 39-72. PMID 2419041 |
0.471 |
|
1985 |
Kamps MP, Buss JE, Sefton BM. Mutation of NH2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proceedings of the National Academy of Sciences of the United States of America. 82: 4625-8. PMID 2991884 DOI: 10.1073/Pnas.82.14.4625 |
0.693 |
|
1985 |
Sefton BM. Oncogenes encoding protein kinases Trends in Genetics. 1: 306-308. DOI: 10.1016/0168-9525(85)90120-9 |
0.549 |
|
1985 |
Buss JE, Kamps MP, Sefton BM. Mutant p60(src)'s which lack myristic acid do not transform cells Federation Proceedings. 44: No. 4671. |
0.577 |
|
1984 |
Voronova AF, Buss JE, Patschinsky T, Hunter T, Sefton BM. Characterization of the protein apparently responsible for the elevated tyrosine protein kinase activity in LSTRA cells. Molecular and Cellular Biology. 4: 2705-13. PMID 6543243 DOI: 10.1128/Mcb.4.12.2705 |
0.582 |
|
1984 |
Buss JE, Kamps MP, Sefton BM. Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein. Molecular and Cellular Biology. 4: 2697-704. PMID 6441887 DOI: 10.1128/Mcb.4.12.2697 |
0.669 |
|
1984 |
Kamps MP, Taylor SS, Sefton BM. Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites. Nature. 310: 589-92. PMID 6431300 DOI: 10.1038/310589A0 |
0.749 |
|
1984 |
Stern DF, Sefton B. Organization of the IBV genome. Advances in Experimental Medicine and Biology. 173: 11-23. PMID 6331104 DOI: 10.1007/978-1-4615-9373-7_2 |
0.501 |
|
1984 |
Stern DF, Sefton BM. Coronavirus multiplication: locations of genes for virion proteins on the avian infectious bronchitis virus genome. Journal of Virology. 50: 22-9. PMID 6321790 DOI: 10.1128/jvi.50.1.22-29.1984 |
0.574 |
|
1984 |
Cooper JA, Sefton BM, Hunter T. Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells. Molecular and Cellular Biology. 4: 30-7. PMID 6199661 DOI: 10.1128/Mcb.4.1.30 |
0.582 |
|
1984 |
Sefton BM, Hunter T. Tyrosine protein kinases. Advances in Cyclic Nucleotide and Protein Phosphorylation Research. 18: 195-226. PMID 6093480 |
0.46 |
|
1983 |
Sefton BM, Hunter T, Cooper JA. Some lymphoid cell lines transformed by Abelson murine leukemia virus lack a major 36,000-dalton tyrosine protein kinase substrate. Molecular and Cellular Biology. 3: 56-63. PMID 6298608 DOI: 10.1128/Mcb.3.1.56 |
0.524 |
|
1983 |
Cooper JA, Sefton BM, Hunter T. Detection and quantification of phosphotyrosine in proteins. Methods in Enzymology. 99: 387-402. PMID 6196603 DOI: 10.1016/0076-6879(83)99075-4 |
0.571 |
|
1982 |
Sefton BM, Hunter T, Nigg EA, Singer SJ, Walter G. Cytoskeletal targets for viral transforming proteins with tyrosine protein kinase activity. Cold Spring Harbor Symposia On Quantitative Biology. 46: 939-51. PMID 6809406 DOI: 10.1101/Sqb.1982.046.01.088 |
0.562 |
|
1982 |
Sefton BM, Trowbridge IS, Cooper JA, Scolnick EM. The transforming proteins of Rous sarcoma virus, Harvey sarcoma virus and Abelson virus contain tightly bound lipid. Cell. 31: 465-74. PMID 6297767 DOI: 10.1016/0092-8674(82)90139-8 |
0.435 |
|
1982 |
Stern DF, Sefton BM. Coronavirus proteins: structure and function of the oligosaccharides of the avian infectious bronchitis virus glycoproteins. Journal of Virology. 44: 804-12. PMID 6294330 DOI: 10.1128/jvi.44.3.804-812.1982 |
0.556 |
|
1982 |
Stern DF, Sefton BM. Coronavirus proteins: biogenesis of avian infectious bronchitis virus virion proteins. Journal of Virology. 44: 794-803. PMID 6294329 DOI: 10.1128/jvi.44.3.794-803.1982 |
0.586 |
|
1982 |
Sefton BM, Walter G. Antiserum specific for the carboxy terminus of the transforming protein of Rous sarcoma virus. Journal of Virology. 44: 467-74. PMID 6292511 |
0.372 |
|
1982 |
Nigg EA, Sefton BM, Hunter T, Walter G, Singer SJ. Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proceedings of the National Academy of Sciences of the United States of America. 79: 5322-6. PMID 6291037 DOI: 10.1073/Pnas.79.17.5322 |
0.426 |
|
1982 |
Stern DF, Sefton BM. Synthesis of coronavirus mRNAs: kinetics of inactivation of infectious bronchitis virus RNA synthesis by UV light. Journal of Virology. 42: 755-9. PMID 6283182 DOI: 10.1128/jvi.42.2.755-759.1982 |
0.474 |
|
1982 |
Stern DF, Burgess L, Sefton BM. Structural analysis of virion proteins of the avian coronavirus infectious bronchitis virus. Journal of Virology. 42: 208-19. PMID 6283141 DOI: 10.1128/jvi.42.1.208-219.1982 |
0.555 |
|
1982 |
Patschinsky T, Hunter T, Esch FS, Cooper JA, Sefton BM. Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation. Proceedings of the National Academy of Sciences of the United States of America. 79: 973-7. PMID 6280176 DOI: 10.1073/Pnas.79.4.973 |
0.543 |
|
1982 |
Adkins B, Hunter T, Sefton BM. The transforming proteins of PRCII virus and Rous sarcoma virus form a complex with the same two cellular phosphoproteins. Journal of Virology. 43: 448-55. PMID 6180178 DOI: 10.1128/Jvi.43.2.448-455.1982 |
0.523 |
|
1982 |
Sefton BM, Patschinsky T, Berdot C, Hunter T, Elliott T. Phosphorylation and metabolism of the transforming protein of Rous sarcoma virus. Journal of Virology. 41: 813-20. PMID 6178840 DOI: 10.1128/Jvi.41.3.813-820.1982 |
0.494 |
|
1981 |
Patschinsky T, Sefton BM. Evidence that there exist four classes of RNA tumor viruses which encode proteins with associated tyrosine protein kinase activities. Journal of Virology. 39: 104-14. PMID 6268803 |
0.401 |
|
1981 |
Sefton BM, Hunter T, Ball EH, Singer SJ. Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell. 24: 165-74. PMID 6263485 DOI: 10.1016/0092-8674(81)90512-2 |
0.528 |
|
1981 |
Sefton BM, Hunter T, Raschke WC. Evidence that the Abelson virus protein functions in vivo as a protein kinase that phosphorylates tyrosine. Proceedings of the National Academy of Sciences of the United States of America. 78: 1552-6. PMID 6262813 DOI: 10.1073/Pnas.78.3.1552 |
0.568 |
|
1980 |
Rose JK, Welch WJ, Sefton BM, Esch FS, Ling NC. Vesicular stomatitis virus glycoprotein is anchored in the viral membrane by a hydrophobic domain near the COOH terminus. Proceedings of the National Academy of Sciences of the United States of America. 77: 3884-8. PMID 6253998 DOI: 10.1073/Pnas.77.7.3884 |
0.341 |
|
1980 |
Hunter T, Sefton BM, Beemon K. Studies on the structure and function of the avian sarcoma virus transforming-gene product. Cold Spring Harbor Symposia On Quantitative Biology. 44: 931-41. PMID 6253224 DOI: 10.1101/Sqb.1980.044.01.100 |
0.533 |
|
1980 |
Sefton BM, Hunter T, Beemon K, Eckhart W. Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. Cell. 20: 807-16. PMID 6251974 DOI: 10.1016/0092-8674(80)90327-X |
0.461 |
|
1980 |
Sefton BM, Hunter T, Beemon K. Relationship of polypeptide products of the transforming gene of Rous sarcoma virus and the homologous gene of vertebrates. Proceedings of the National Academy of Sciences of the United States of America. 77: 2059-63. PMID 6246520 DOI: 10.1073/Pnas.77.4.2059 |
0.307 |
|
1980 |
Hunter T, Sefton BM. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proceedings of the National Academy of Sciences of the United States of America. 77: 1311-5. PMID 6246487 DOI: 10.1073/Pnas.77.3.1311 |
0.596 |
|
1980 |
Sefton BM, Hunter T, Beemon K. Temperature-sensitive transformation by Rous sarcoma virus and temperature-sensitive protein kinase activity. Journal of Virology. 33: 220-9. PMID 6245228 DOI: 10.1128/Jvi.33.1.220-229.1980 |
0.553 |
|
1979 |
Sefton BM, Hunter T, Beemon K. Product of in vitro translation of the Rous sarcoma virus src gene has protein kinase activity. Journal of Virology. 30: 311-8. PMID 225522 DOI: 10.1128/Jvi.30.1.311-318.1979 |
0.562 |
|
1979 |
Beemon K, Hunter T, Sefton BM. Polymorphism of avian sarcoma virus src proteins. Journal of Virology. 30: 190-200. PMID 225515 DOI: 10.1128/Jvi.30.1.190-200.1979 |
0.357 |
|
1978 |
Sefton BM, Beemon K, Hunter T. Comparison of the expression of the src gene of Rous sarcoma virus in vitro and in vivo. Journal of Virology. 28: 957-71. PMID 215787 DOI: 10.1128/Jvi.28.3.957-971.1978 |
0.379 |
|
1978 |
Fan DP, Sefton BM. The entry into host cells of Sindbis virus, vesicular stomatitis virus and Sendai virus. Cell. 15: 985-92. PMID 215317 DOI: 10.1016/0092-8674(78)90282-9 |
0.304 |
|
1977 |
Sefton BM. Immediate glycosylation of Sindbis virus membrane proteins. Cell. 10: 659-68. PMID 558830 DOI: 10.1016/0092-8674(77)90099-X |
0.362 |
|
1973 |
Sefton BM, Burge BW. Biosynthesis of the Sindbis virus carbohydrates. Journal of Virology. 12: 1366-74. PMID 4796898 |
0.318 |
|
1973 |
Sefton BM, Wickus GG, Burge BW. Enzymatic iodination of Sindbis virus proteins. Journal of Virology. 11: 730-5. PMID 4736110 |
0.315 |
|
1971 |
Sefton BM, Rubin H. Stimulation of glucose transport in cultures of density-inhibited chick embryo cells. Proceedings of the National Academy of Sciences of the United States of America. 68: 3154-7. PMID 5289253 DOI: 10.1073/Pnas.68.12.3154 |
0.487 |
|
1970 |
Sefton BM, Rubin H. Release from density dependent growth inhibition by proteolytic enzymes. Nature. 227: 843-5. PMID 5464581 DOI: 10.1038/227843A0 |
0.438 |
|
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