(en) David S. Goodsell, « The Molecular Perspective: The ras Oncogene », The Oncologist, vol. 4, no 3, , p. 263-264 (PMID10394594, lire en ligne)
ashpublications.org
(en) Christoph W. M. Reuter, Michael A. Morgan et Lothar Bergmann, « Targeting the Ras signaling pathway: a rational, mechanism-based treatment for hematologic malignancies? », Blood, vol. 96, no 5, , p. 1655-1669 (PMID10961860, DOI10.1182/blood.V96.5.1655, lire en ligne)
cell.com
(en) Carol V. Robinson, Tibor Rohacs et Scott B. Hansen, « Tools for Understanding Nanoscale Lipid Regulation of Ion Channels », Trends in Biochemical Sciences, vol. 44, no 9, , p. 795-806 (PMID31060927, PMCID6729126, DOI10.1016/j.tibs.2019.04.001, lire en ligne)
(en) Giuseppe Novelli et Maria Rosaria D'Apice, « Protein farnesylation and disease », Journal of Inherited Metabolic Diseases, vol. 35, no 5, , p. 917-926 (PMID22307208, DOI10.1007/s10545-011-9445-y, lire en ligne)
(en) Michael A. J. Ferguson, « Lipid anchors on membrane proteins », Current Opinion in Structural Biology, vol. 1, no 4, , p. 522-529 (DOI10.1016/S0959-440X(05)80072-7, lire en ligne)
(en) Kimberly T. Lane et Lorena S. Beese, « Thematic review series: Lipid Posttranslational Modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I », Journal of Lipid Research, vol. 47, no 4, , p. 681-699 (PMID16477080, DOI10.1194/jlr.R600002-JLR200, lire en ligne)
(en) Christoph W. M. Reuter, Michael A. Morgan et Lothar Bergmann, « Targeting the Ras signaling pathway: a rational, mechanism-based treatment for hematologic malignancies? », Blood, vol. 96, no 5, , p. 1655-1669 (PMID10961860, DOI10.1182/blood.V96.5.1655, lire en ligne)
(en) Marilyn D. Resh, « Trafficking and signaling by fatty-acylated and prenylated proteins », Nature Chemical Biology, vol. 2, no 11, , p. 584-590 (PMID17051234, DOI10.1038/nchembio834, lire en ligne)
(en) John P. Wilson, Anuradha S. Raghavan, Yu-Ying Yang, Guillaume Charron et Howard C. Hang, « Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters Reveals S-Acylation of Histone H3 Variants », Molecular & Cellular Proteomics, vol. 10, no 3, , article no M110.001198 (PMID21076176, PMCID3047146, DOI10.1074/mcp.M110.001198, lire en ligne)
(en) Thalia A. Farazi, Gabriel Waksman et Jeffrey I. Gordon, « The Biology and Enzymology of Protein N-Myristoylation », Journal of Biological Chemistry, vol. 276, no 43, , p. 39501-39504 (PMID11527981, DOI10.1074/jbc.R100042200, lire en ligne)
(en) Dale D. O. Martin, Erwan Beauchamp et Luc G. Berthiaume, « Post-translational myristoylation: Fat matters in cellular life and death », Biochimie, vol. 93, no 1, , p. 18-31 (PMID21056615, DOI10.1016/j.biochi.2010.10.018, lire en ligne)
(en) Clara Aicart-Ramos, Ruth Ana et Valero Ignacio Rodriguez-Crespo, « Protein palmitoylation and subcellular trafficking », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1808, no 12, , p. 2981-2994 (PMID21819967, DOI10.1016/j.bbamem.2011.07.009, lire en ligne)
(en) Ilya Levental, Daniel Lingwood, Michal Grzybek, Ünal Coskun et Kai Simons, « Palmitoylation regulates raft affinity for the majority of integral raft proteins », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 51, , p. 22050-22054 (PMID21131568, PMCID3009825, DOI10.1073/pnas.1016184107, Bibcode2010PNAS..10722050L, lire en ligne)
(en) Carol V. Robinson, Tibor Rohacs et Scott B. Hansen, « Tools for Understanding Nanoscale Lipid Regulation of Ion Channels », Trends in Biochemical Sciences, vol. 44, no 9, , p. 795-806 (PMID31060927, PMCID6729126, DOI10.1016/j.tibs.2019.04.001, lire en ligne)
(en) E. Nicholas Petersen, Mahmud Arif Pavel, Hao Wang et Scott B. Hansen, « Disruption of palmitate-mediated localization; a shared pathway of force and anesthetic activation of TREK-1 channels », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1862, no 1, , article no 183091 (PMID31672538, PMCID6907892, DOI10.1016/j.bbamem.2019.183091, lire en ligne)
(en) Taroh Kinoshita et Morihisa Fujita, « Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling », Journal of Lipid Research, vol. 57, no 1, , p. 6-24 (PMID26563290, PMCID4689344, DOI10.1194/jlr.R063313, lire en ligne)
(en) Hiroh Ikezawa, « Glycosylphosphatidylinositol (GPI)-Anchored Proteins », Biological and Pharmaceutical Bulletin, vol. 25, no 4, , p. 409-417 (PMID11995915, DOI10.1248/bpb.25.409, lire en ligne)
(en) Scott A. Coonrod, Soren Naaby-Hansen, Jagathpala Shetty, Hiroaki Shibahara, Michellee Chen, Judith M. White et John C. Herr, « Treatment of Mouse Oocytes with PI-PLC Releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) Protein Clusters from the Egg Surface and Inhibits Sperm–Oolemma Binding and Fusion », Developmental Biology, vol. 207, no 2, , p. 334-349 (PMID10068467, DOI10.1006/dbio.1998.9161, lire en ligne)
(en) Ilya Levental, Daniel Lingwood, Michal Grzybek, Ünal Coskun et Kai Simons, « Palmitoylation regulates raft affinity for the majority of integral raft proteins », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 51, , p. 22050-22054 (PMID21131568, PMCID3009825, DOI10.1073/pnas.1016184107, Bibcode2010PNAS..10722050L, lire en ligne)
(en) Thalia A. Farazi, Gabriel Waksman et Jeffrey I. Gordon, « The Biology and Enzymology of Protein N-Myristoylation », Journal of Biological Chemistry, vol. 276, no 43, , p. 39501-39504 (PMID11527981, DOI10.1074/jbc.R100042200, lire en ligne)
jlr.org
(en) Kimberly T. Lane et Lorena S. Beese, « Thematic review series: Lipid Posttranslational Modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I », Journal of Lipid Research, vol. 47, no 4, , p. 681-699 (PMID16477080, DOI10.1194/jlr.R600002-JLR200, lire en ligne)
(en) Taroh Kinoshita et Morihisa Fujita, « Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling », Journal of Lipid Research, vol. 57, no 1, , p. 6-24 (PMID26563290, PMCID4689344, DOI10.1194/jlr.R063313, lire en ligne)
jst.go.jp
jstage.jst.go.jp
(en) Hiroh Ikezawa, « Glycosylphosphatidylinositol (GPI)-Anchored Proteins », Biological and Pharmaceutical Bulletin, vol. 25, no 4, , p. 409-417 (PMID11995915, DOI10.1248/bpb.25.409, lire en ligne)
(en) John P. Wilson, Anuradha S. Raghavan, Yu-Ying Yang, Guillaume Charron et Howard C. Hang, « Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters Reveals S-Acylation of Histone H3 Variants », Molecular & Cellular Proteomics, vol. 10, no 3, , article no M110.001198 (PMID21076176, PMCID3047146, DOI10.1074/mcp.M110.001198, lire en ligne)
nature.com
(en) Marilyn D. Resh, « Trafficking and signaling by fatty-acylated and prenylated proteins », Nature Chemical Biology, vol. 2, no 11, , p. 584-590 (PMID17051234, DOI10.1038/nchembio834, lire en ligne)
(en) Giuseppe Novelli et Maria Rosaria D'Apice, « Protein farnesylation and disease », Journal of Inherited Metabolic Diseases, vol. 35, no 5, , p. 917-926 (PMID22307208, DOI10.1007/s10545-011-9445-y, lire en ligne)
(en) Kimberly T. Lane et Lorena S. Beese, « Thematic review series: Lipid Posttranslational Modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I », Journal of Lipid Research, vol. 47, no 4, , p. 681-699 (PMID16477080, DOI10.1194/jlr.R600002-JLR200, lire en ligne)
(en) David S. Goodsell, « The Molecular Perspective: The ras Oncogene », The Oncologist, vol. 4, no 3, , p. 263-264 (PMID10394594, lire en ligne)
(en) Christoph W. M. Reuter, Michael A. Morgan et Lothar Bergmann, « Targeting the Ras signaling pathway: a rational, mechanism-based treatment for hematologic malignancies? », Blood, vol. 96, no 5, , p. 1655-1669 (PMID10961860, DOI10.1182/blood.V96.5.1655, lire en ligne)
(en) Marilyn D. Resh, « Trafficking and signaling by fatty-acylated and prenylated proteins », Nature Chemical Biology, vol. 2, no 11, , p. 584-590 (PMID17051234, DOI10.1038/nchembio834, lire en ligne)
(en) John P. Wilson, Anuradha S. Raghavan, Yu-Ying Yang, Guillaume Charron et Howard C. Hang, « Proteomic Analysis of Fatty-acylated Proteins in Mammalian Cells with Chemical Reporters Reveals S-Acylation of Histone H3 Variants », Molecular & Cellular Proteomics, vol. 10, no 3, , article no M110.001198 (PMID21076176, PMCID3047146, DOI10.1074/mcp.M110.001198, lire en ligne)
(en) Thalia A. Farazi, Gabriel Waksman et Jeffrey I. Gordon, « The Biology and Enzymology of Protein N-Myristoylation », Journal of Biological Chemistry, vol. 276, no 43, , p. 39501-39504 (PMID11527981, DOI10.1074/jbc.R100042200, lire en ligne)
(en) Dale D. O. Martin, Erwan Beauchamp et Luc G. Berthiaume, « Post-translational myristoylation: Fat matters in cellular life and death », Biochimie, vol. 93, no 1, , p. 18-31 (PMID21056615, DOI10.1016/j.biochi.2010.10.018, lire en ligne)
(en) Clara Aicart-Ramos, Ruth Ana et Valero Ignacio Rodriguez-Crespo, « Protein palmitoylation and subcellular trafficking », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1808, no 12, , p. 2981-2994 (PMID21819967, DOI10.1016/j.bbamem.2011.07.009, lire en ligne)
(en) Ilya Levental, Daniel Lingwood, Michal Grzybek, Ünal Coskun et Kai Simons, « Palmitoylation regulates raft affinity for the majority of integral raft proteins », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 51, , p. 22050-22054 (PMID21131568, PMCID3009825, DOI10.1073/pnas.1016184107, Bibcode2010PNAS..10722050L, lire en ligne)
(en) Carol V. Robinson, Tibor Rohacs et Scott B. Hansen, « Tools for Understanding Nanoscale Lipid Regulation of Ion Channels », Trends in Biochemical Sciences, vol. 44, no 9, , p. 795-806 (PMID31060927, PMCID6729126, DOI10.1016/j.tibs.2019.04.001, lire en ligne)
(en) E. Nicholas Petersen, Mahmud Arif Pavel, Hao Wang et Scott B. Hansen, « Disruption of palmitate-mediated localization; a shared pathway of force and anesthetic activation of TREK-1 channels », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1862, no 1, , article no 183091 (PMID31672538, PMCID6907892, DOI10.1016/j.bbamem.2019.183091, lire en ligne)
(en) Taroh Kinoshita et Morihisa Fujita, « Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling », Journal of Lipid Research, vol. 57, no 1, , p. 6-24 (PMID26563290, PMCID4689344, DOI10.1194/jlr.R063313, lire en ligne)
(en) Hiroh Ikezawa, « Glycosylphosphatidylinositol (GPI)-Anchored Proteins », Biological and Pharmaceutical Bulletin, vol. 25, no 4, , p. 409-417 (PMID11995915, DOI10.1248/bpb.25.409, lire en ligne)
(en) Scott A. Coonrod, Soren Naaby-Hansen, Jagathpala Shetty, Hiroaki Shibahara, Michellee Chen, Judith M. White et John C. Herr, « Treatment of Mouse Oocytes with PI-PLC Releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) Protein Clusters from the Egg Surface and Inhibits Sperm–Oolemma Binding and Fusion », Developmental Biology, vol. 207, no 2, , p. 334-349 (PMID10068467, DOI10.1006/dbio.1998.9161, lire en ligne)
(en) Ilya Levental, Daniel Lingwood, Michal Grzybek, Ünal Coskun et Kai Simons, « Palmitoylation regulates raft affinity for the majority of integral raft proteins », Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no 51, , p. 22050-22054 (PMID21131568, PMCID3009825, DOI10.1073/pnas.1016184107, Bibcode2010PNAS..10722050L, lire en ligne)
sciencedirect.com
(en) Michael A. J. Ferguson, « Lipid anchors on membrane proteins », Current Opinion in Structural Biology, vol. 1, no 4, , p. 522-529 (DOI10.1016/S0959-440X(05)80072-7, lire en ligne)
(en) Dale D. O. Martin, Erwan Beauchamp et Luc G. Berthiaume, « Post-translational myristoylation: Fat matters in cellular life and death », Biochimie, vol. 93, no 1, , p. 18-31 (PMID21056615, DOI10.1016/j.biochi.2010.10.018, lire en ligne)
(en) Clara Aicart-Ramos, Ruth Ana et Valero Ignacio Rodriguez-Crespo, « Protein palmitoylation and subcellular trafficking », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1808, no 12, , p. 2981-2994 (PMID21819967, DOI10.1016/j.bbamem.2011.07.009, lire en ligne)
(en) E. Nicholas Petersen, Mahmud Arif Pavel, Hao Wang et Scott B. Hansen, « Disruption of palmitate-mediated localization; a shared pathway of force and anesthetic activation of TREK-1 channels », Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1862, no 1, , article no 183091 (PMID31672538, PMCID6907892, DOI10.1016/j.bbamem.2019.183091, lire en ligne)
(en) Scott A. Coonrod, Soren Naaby-Hansen, Jagathpala Shetty, Hiroaki Shibahara, Michellee Chen, Judith M. White et John C. Herr, « Treatment of Mouse Oocytes with PI-PLC Releases 70-kDa (pI 5) and 35- to 45-kDa (pI 5.5) Protein Clusters from the Egg Surface and Inhibits Sperm–Oolemma Binding and Fusion », Developmental Biology, vol. 207, no 2, , p. 334-349 (PMID10068467, DOI10.1006/dbio.1998.9161, lire en ligne)
wiley.com
onlinelibrary.wiley.com
(en) Giuseppe Novelli et Maria Rosaria D'Apice, « Protein farnesylation and disease », Journal of Inherited Metabolic Diseases, vol. 35, no 5, , p. 917-926 (PMID22307208, DOI10.1007/s10545-011-9445-y, lire en ligne)