Year |
Citation |
Score |
2011 |
McKay J, Wang X, Ding J, Buss JE, Ambrosio L. H-ras resides on clathrin-independent ARF6 vesicles that harbor little RAF-1, but not on clathrin-dependent endosomes. Biochimica Et Biophysica Acta. 1813: 298-307. PMID 21145357 DOI: 10.1016/J.Bbamcr.2010.11.019 |
0.799 |
|
2010 |
Barnhill AE, Hecker LA, Kohutyuk O, Buss JE, Honavar VG, Greenlee HW. Characterization of the retinal proteome during rod photoreceptor genesis. Bmc Research Notes. 3: 25. PMID 20181029 DOI: 10.1186/1756-0500-3-25 |
0.343 |
|
2010 |
McKay J, Buss JE. The influence of intracellular location on function of ras proteins Handbook of Cell Signaling, 2/E. 2: 1745-1752. DOI: 10.1016/B978-0-12-374145-5.00213-8 |
0.519 |
|
2007 |
Zheng H, McKay J, Buss JE. H-Ras does not need COP I- or COP II-dependent vesicular transport to reach the plasma membrane. The Journal of Biological Chemistry. 282: 25760-8. PMID 17588947 DOI: 10.1074/Jbc.M700437200 |
0.804 |
|
2005 |
Berzat AC, Buss JE, Chenette EJ, Weinbaum CA, Shutes A, Der CJ, Minden A, Cox AD. Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif. The Journal of Biological Chemistry. 280: 33055-65. PMID 16046391 DOI: 10.1074/Jbc.M507362200 |
0.485 |
|
2003 |
Heather West Greenlee M, Uemura E, Carpenter SL, Doyle RT, Buss JE. Glucose uptake in PC12 cells: GLUT3 vesicle trafficking and fusion as revealed with a novel GLUT3-GFP fusion protein. Journal of Neuroscience Research. 73: 518-25. PMID 12898536 DOI: 10.1002/Jnr.10684 |
0.379 |
|
2003 |
Baker TL, Zheng H, Walker J, Coloff JL, Buss JE. Distinct rates of palmitate turnover on membrane-bound cellular and oncogenic H-ras. The Journal of Biological Chemistry. 278: 19292-300. PMID 12642594 DOI: 10.1074/Jbc.M206956200 |
0.552 |
|
2003 |
Buss JE, Booden MA, Stickney JT. The Influence of Cellular Location on Ras Function Handbook of Cell Signaling. 2: 675-679. DOI: 10.1016/B978-012124546-7/50594-5 |
0.749 |
|
2002 |
Prapong T, Buss J, Hsu WH, Heine P, West Greenlee H, Uemura E. Amyloid beta-peptide decreases neuronal glucose uptake despite causing increase in GLUT3 mRNA transcription and GLUT3 translocation to the plasma membrane. Experimental Neurology. 174: 253-8. PMID 11922666 DOI: 10.1006/Exnr.2001.7861 |
0.316 |
|
2001 |
Stickney JT, Booden MA, Buss JE. Targeting proteins to membranes, using signal sequences for lipid modifications. Methods in Enzymology. 332: 64-77. PMID 11305118 |
0.756 |
|
2001 |
Mallis RJ, Buss JE, Thomas JA. Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines Biochemical Journal. 355: 145-153. PMID 11256959 DOI: 10.1042/Bj3550145 |
0.515 |
|
2001 |
Stickney JT, Booden MA, Buss JE. [4] Targeting proteins to membranes, using signal sequences for lipid modifications Methods in Enzymology. 332: 64-77. DOI: 10.1016/S0076-6879(01)32192-4 |
0.756 |
|
2000 |
Reuther GW, Buss JE, Quilliam LA, Clark GJ, Der CJ. Analysis of function and regulation of proteins that mediate signal transduction by use of lipid-modified plasma membrane-targeting sequences Methods in Enzymology. 327: 331-350. PMID 11044995 DOI: 10.1016/S0076-6879(00)27288-1 |
0.574 |
|
2000 |
Stickney JT, Buss JE. Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein. Molecular Biology of the Cell. 11: 2191-200. PMID 10888661 DOI: 10.1091/Mbc.11.7.2191 |
0.806 |
|
2000 |
Baker TL, Booden MA, Buss JE. S-Nitrosocysteine increases palmitate turnover on Ha-Ras in NIH 3T3 cells. The Journal of Biological Chemistry. 275: 22037-47. PMID 10801823 DOI: 10.1074/Jbc.M001813200 |
0.79 |
|
2000 |
Booden MA, Sakaguchi DS, Buss JE. Mutation of Ha-Ras C terminus changes effector pathway utilization. The Journal of Biological Chemistry. 275: 23559-68. PMID 10801808 DOI: 10.1074/Jbc.M001368200 |
0.799 |
|
1999 |
Coats SG, Booden MA, Buss JE. Transient palmitoylation supports H-Ras membrane binding but only partial biological activity. Biochemistry. 38: 12926-34. PMID 10504264 DOI: 10.1021/Bi9909290 |
0.822 |
|
1999 |
Booden MA, Baker TL, Solski PA, Der CJ, Punke SG, Buss JE. A non-farnesylated Ha-Ras protein can be palmitoylated and trigger potent differentiation and transformation. The Journal of Biological Chemistry. 274: 1423-31. PMID 9880516 DOI: 10.1074/Jbc.274.3.1423 |
0.833 |
|
1998 |
Vestal DJ, Buss JE, McKercher SR, Jenkins NA, Copeland NG, Kelner GS, Asundi VK, Maki RA. Murine GBP-2: A new IFN-y-induced member of the GBP family of GTPases isolated from macrophages Journal of Interferon and Cytokine Research. 18: 977-985. PMID 9858320 DOI: 10.1089/Jir.1998.18.977 |
0.347 |
|
1998 |
Booden MA, Baker TL, Buss JE. A non-farnesylated H-ras can be palmitoylated and trigger potent differentiation and transformation Faseb Journal. 12: A1319. |
0.825 |
|
1997 |
Buss JE, Punke SG, Baker TL. H-ras palmitoylation is prenylation-independent and activation-sensitive Faseb Journal. 11: A1084. |
0.535 |
|
1997 |
Stickney JT, Buss JE. A failure in prenylation: MGBP1, an IFN-inducible gtpase with a C20-type caax motif Faseb Journal. 11: A1088. |
0.785 |
|
1996 |
Willumsen BM, Cox AD, Solski PA, Der CJ, Buss JE. Novel determinants of H-Ras plasma membrane localization and transformation. Oncogene. 13: 1901-9. PMID 8934536 |
0.575 |
|
1996 |
Nantais DE, Schwemmle M, Stickney JT, Vestal DJ, Buss JE. Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1. Journal of Leukocyte Biology. 60: 423-31. PMID 8830800 DOI: 10.1002/Jlb.60.3.423 |
0.766 |
|
1995 |
Buss JE, Marsters JC. Farnesyl transferase inhibitors: the successes and surprises of a new class of potential cancer chemotherapeutics Chemistry and Biology. 2: 787-791. PMID 8807811 DOI: 10.1016/1074-5521(95)90083-7 |
0.449 |
|
1995 |
Solski PA, Quilliam LA, Coats SG, Der CJ, Buss JE. Targeting proteins to membranes using signal sequences for lipid modification. Methods in Enzymology. 250: 435-54. PMID 7651170 DOI: 10.1016/0076-6879(95)50089-8 |
0.441 |
|
1995 |
Vestal DJ, Maki RA, Buss JE. Induction of a prenylated 65-kd protein in macrophages by interferon or lipopolysaccharide Journal of Leukocyte Biology. 58: 607-615. PMID 7595063 DOI: 10.1002/Jlb.58.5.607 |
0.391 |
|
1995 |
Casey PJ, Buss JE. Lipid modifications of protein: Preface Methods in Enzymology. 250: xvii-xviii. DOI: 10.1016/0076-6879(95)50055-3 |
0.33 |
|
1994 |
Jackson JH, Li JW, Buss JE, Der CJ, Cochrane CG. Polylysine domain of K-ras 4B protein is crucial for malignant transformation. Proceedings of the National Academy of Sciences of the United States of America. 91: 12730-4. PMID 7809111 DOI: 10.1073/Pnas.91.26.12730 |
0.534 |
|
1993 |
Cox AD, Graham SM, Solski PA, Buss JE, Der CJ. The carboxyl-terminal CXXX sequence of Gi alpha, but not Rab5 or Rab11, supports Ras processing and transforming activity. The Journal of Biological Chemistry. 268: 11548-52. PMID 8505289 |
0.44 |
|
1993 |
Rilling HC, Bruenger E, Leining LM, Buss JE, Epstein WW. Differential prenylation of proteins as a function of mevalonate concentration in CHO cells. Archives of Biochemistry and Biophysics. 301: 210-5. PMID 8460935 DOI: 10.1006/abbi.1993.1135 |
0.313 |
|
1992 |
Kato K, Cox AD, Hisaka MM, Graham SM, Buss JE, Der CJ. Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity Proceedings of the National Academy of Sciences of the United States of America. 89: 6403-6407. PMID 1631135 DOI: 10.1073/Pnas.89.14.6403 |
0.525 |
|
1992 |
Kato K, Der CJ, Buss JE. Prenoids and palmitate: Lipids that control the biological activity of Ras proteins Seminars in Cancer Biology. 3: 179-188. PMID 1421162 |
0.587 |
|
1992 |
Chow M, Der CJ, Buss JE. Structure and biological effects of lipid modifications on proteins Current Opinion in Cell Biology. 4: 629-636. PMID 1419045 DOI: 10.1016/0955-0674(92)90082-N |
0.339 |
|
1992 |
Cox AD, Hisaka MM, Buss JE, Der CJ. Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein Molecular and Cellular Biology. 12: 2606-2615. PMID 1375323 DOI: 10.1128/Mcb.12.6.2606 |
0.589 |
|
1991 |
Buss JE, Quilliam LA, Kato K, Casey PJ, Solski PA, Wong G, Clark R, McCormick F, Bokoch GM, Der CJ. The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein. Molecular and Cellular Biology. 11: 1523-30. PMID 1899909 DOI: 10.1128/Mcb.11.3.1523 |
0.635 |
|
1991 |
Khosravi-Far R, Lutz RJ, Cox AD, Conroy L, Bourne JR, Sinensky M, Balch WE, Buss JE, Der CJ. Isoprenoid modification of rab proteins terminating in CC or CXC motifs. Proceedings of the National Academy of Sciences of the United States of America. 88: 6264-8. PMID 1648736 DOI: 10.1073/Pnas.88.14.6264 |
0.541 |
|
1990 |
Johnson DR, Cox AD, Solski PA, Devadas B, Adams SP, Leimgruber RM, Heuckeroth RO, Buss JE, Gordon JI. Functional analysis of protein N-myristoylation: metabolic labeling studies using three oxygen-substituted analogs of myristic acid and cultured mammalian cells provide evidence for protein-sequence-specific incorporation and analog-specific redistribution. Proceedings of the National Academy of Sciences of the United States of America. 87: 8511-5. PMID 2236060 DOI: 10.1073/Pnas.87.21.8511 |
0.498 |
|
1990 |
Jackson JH, Cochrane CG, Bourne JR, Solski PA, Buss JE, Der CJ. Farnesol modification of Kirsten-ras exon 4B protein is essential for transformation. Proceedings of the National Academy of Sciences of the United States of America. 87: 3042-6. PMID 2183224 DOI: 10.1073/Pnas.87.8.3042 |
0.577 |
|
1990 |
Mumby SM, Buss JE. Metabolic radiolabeling techniques for identification of prenylated and fatty acylated proteins Methods. 1: 216-220. DOI: 10.1016/S1046-2023(05)80320-2 |
0.416 |
|
1989 |
Buss JE, Solski PA, Schaeffer JP, MacDonald MJ, Der CJ. Activation of cellular p21ras by myristoylation. Biochemical Society Transactions. 17: 867-9. PMID 2695362 DOI: 10.1042/Bst0170867 |
0.652 |
|
1989 |
Casey PJ, Solski PA, Der CJ, Buss JE. p21ras is modified by a farnesyl isoprenoid. Proceedings of the National Academy of Sciences of the United States of America. 86: 8323-7. PMID 2682646 DOI: 10.1073/Pnas.86.21.8323 |
0.614 |
|
1989 |
Buss JE, Solski PA, Schaeffer JP, MacDonald MJ, Der CJ. Activation of the cellular proto-oncogene product p21Ras by addition of a myristylation signal. Science (New York, N.Y.). 243: 1600-3. PMID 2648572 DOI: 10.1126/Science.2648572 |
0.591 |
|
1988 |
Buss JE, Der CJ, Solski PA. The six amino-terminal amino acids of p60src are sufficient to cause myristylation of p21v-ras. Molecular and Cellular Biology. 8: 3960-3. PMID 3146693 DOI: 10.1128/Mcb.8.9.3960 |
0.46 |
|
1988 |
Brown JH, Orellana SA, Buss JE, Quilliam LA. Regulation of phosphoinositide hydrolysis by GTP-binding proteins, phorbol esters and botulinum toxin type D Advances in Experimental Medicine and Biology. 236: 229-237. PMID 2853564 DOI: 10.1007/978-1-4757-5971-6_18 |
0.351 |
|
1988 |
Quilliam LA, Brown JH, Buss JE. A 22 kDa ras-related G-protein is the substrate for an ADP-ribosyltransferase from Clostridium botulinum Febs Letters. 238: 22-26. PMID 2844595 DOI: 10.1016/0014-5793(88)80217-5 |
0.534 |
|
1987 |
Sefton BM, Buss JE. The covalent modification of eukaryotic proteins with lipid. The Journal of Cell Biology. 104: 1449-53. PMID 3294853 |
0.331 |
|
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 |
0.31 |
|
1986 |
Buss JE, Sefton BM. Direct identification of palmitic acid as the lipid attached to p21ras. Molecular and Cellular Biology. 6: 116-22. PMID 3023817 |
0.42 |
|
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 |
0.419 |
|
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 |
0.406 |
|
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