| Year |
Citation |
Score |
| 2018 |
Cleator J, Wells C, Dingus J, Kurtz DT, Hildebrandt JD. The N54-αs mutant has decreased affinity for βγ and suggests a mechanism for coupling heterotrimeric G protein nucleotide exchange with subunit dissociation. The Journal of Pharmacology and Experimental Therapeutics. PMID 29491039 DOI: 10.1124/Jpet.117.245779 |
0.493 |
|
| 2012 |
Dingus J, Hildebrandt JD. Synthesis and assembly of G protein βγ dimers: comparison of in vitro and in vivo studies. Sub-Cellular Biochemistry. 63: 155-80. PMID 23161138 DOI: 10.1007/978-94-007-4765-4_9 |
0.552 |
|
| 2011 |
Hildebrandt JD. Heterogeneous Prenyl Processing of the Heterotrimeric G protein Gamma Subunits The Enzymes. 29: 97-124. DOI: 10.1016/B978-0-12-381339-8.00006-8 |
0.542 |
|
| 2008 |
Lindsey Rose KM, Wang Z, Magrath GN, Hazard ES, Hildebrandt JD, Schey KL. Aquaporin 0−Calmodulin Interaction and the Effect of Aquaporin 0 Phosphorylation† Biochemistry. 47: 339-347. DOI: 10.1021/Bi701980T |
0.354 |
|
| 2007 |
Kilpatrick EL, Hildebrandt JD. Sequence dependence and differential expression of Ggamma5 subunit isoforms of the heterotrimeric G proteins variably processed after prenylation in mammalian cells. The Journal of Biological Chemistry. 282: 14038-47. PMID 17353195 DOI: 10.1074/Jbc.M701338200 |
0.407 |
|
| 2006 |
Wells CA, Dingus J, Hildebrandt JD. Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assembly. The Journal of Biological Chemistry. 281: 20221-32. PMID 16702223 DOI: 10.1074/Jbc.M602409200 |
0.471 |
|
| 2006 |
Hildebrandt JD. Bring your own G protein. Molecular Pharmacology. 69: 1079-82. PMID 16436587 DOI: 10.1124/Mol.106.022921 |
0.515 |
|
| 2006 |
Cook LA, Schey KL, Wilcox MD, Dingus J, Ettling R, Nelson T, Knapp DR, Hildebrandt JD. Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity. Molecular & Cellular Proteomics : McP. 5: 671-85. PMID 16332732 DOI: 10.1074/Mcp.M500223-Mcp200 |
0.512 |
|
| 2006 |
Yang W, Hildebrandt JD. Genomic analysis of G protein gamma subunits in human and mouse - the relationship between conserved gene structure and G protein betagamma dimer formation. Cellular Signalling. 18: 194-201. PMID 16006100 DOI: 10.1016/J.Cellsig.2005.04.011 |
0.468 |
|
| 2005 |
Dingus J, Wells CA, Campbell L, Cleator JH, Robinson K, Hildebrandt JD. G Protein betagamma dimer formation: Gbeta and Ggamma differentially determine efficiency of in vitro dimer formation. Biochemistry. 44: 11882-90. PMID 16128590 DOI: 10.1021/Bi0504254 |
0.505 |
|
| 2004 |
Cleator JH, Ravenell R, Kurtz DT, Hildebrandt JD. A dominant negative Galphas mutant that prevents thyroid-stimulating hormone receptor activation of cAMP production and inositol 1,4,5-trisphosphate turnover: competition by different G proteins for activation by a common receptor. The Journal of Biological Chemistry. 279: 36601-7. PMID 15234971 DOI: 10.1074/Jbc.M406232200 |
0.46 |
|
| 2003 |
Hamilton MH, Cook LA, McRackan TR, Schey KL, Hildebrandt JD. Gamma 2 subunit of G protein heterotrimer is an N-end rule ubiquitylation substrate. Proceedings of the National Academy of Sciences of the United States of America. 100: 5081-6. PMID 12700354 DOI: 10.1073/Pnas.0831228100 |
0.565 |
|
| 2002 |
Ribas C, Takesono A, Sato M, Hildebrandt JD, Lanier SM. Pertussis toxin-insensitive activation of the heterotrimeric G-proteins Gi/Go by the NG108-15 G-protein activator. The Journal of Biological Chemistry. 277: 50223-5. PMID 12426323 DOI: 10.1074/Jbc.C200567200 |
0.484 |
|
| 2002 |
Schey KL, Busman M, Cook LA, Hamm HE, Hildebrandt JD. Structural characterization of intact G protein gamma subunits by mass spectrometry. Methods in Enzymology. 344: 586-97. PMID 11771413 DOI: 10.1016/S0076-6879(02)44742-8 |
0.503 |
|
| 2002 |
McIntire WE, Schey KL, Knapp DR, Dingus J, Hildebrandt JD. Characterization of deamidated G protein subunits. Methods in Enzymology. 344: 481-505. PMID 11771405 DOI: 10.1016/S0076-6879(02)44735-0 |
0.559 |
|
| 2002 |
Cook LA, Wilcox MD, Dingus J, Schey KL, Hildebrandt JD. Separation and analysis of G protein gamma subunits. Methods in Enzymology. 344: 209-33. PMID 11771385 DOI: 10.1016/S0076-6879(02)44717-9 |
0.542 |
|
| 2002 |
Dingus J, Tatum BS, Vaidyanathan G, Hildebrandt JD. Purification of G protein beta gamma from bovine brain. Methods in Enzymology. 344: 194-208. PMID 11771384 DOI: 10.1016/S0076-6879(02)44716-7 |
0.442 |
|
| 2002 |
Ribas C, Sato M, Hildebrandt JD, Lanier SM. Analysis of signal transfer from receptor to Go/Gi in different membrane environments and receptor-independent activators of brain G protein. Methods in Enzymology. 344: 140-52. PMID 11771378 DOI: 10.1016/S0076-6879(02)44711-8 |
0.432 |
|
| 2001 |
Cook LA, Schey KL, Cleator JH, Wilcox MD, Dingus J, Hildebrandt JD. Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms. Protein Science : a Publication of the Protein Society. 10: 2548-55. PMID 11714923 DOI: 10.1110/Ps.Ps.26401 |
0.537 |
|
| 2001 |
Schey KL, Cook LA, Hildebrandt JD. Ion trap tandem mass spectrometry of intact GTP-binding protein γ-subunits International Journal of Mass Spectrometry. 212: 377-388. DOI: 10.1016/S1387-3806(01)00495-X |
0.333 |
|
| 2000 |
Wu G, Bogatkevich GS, Mukhin YV, Benovic JL, Hildebrandt JD, Lanier SM. Identification of Gbetagamma binding sites in the third intracellular loop of the M(3)-muscarinic receptor and their role in receptor regulation. The Journal of Biological Chemistry. 275: 9026-34. PMID 10722752 DOI: 10.1074/Jbc.275.12.9026 |
0.353 |
|
| 1999 |
McIntire WE, Dingus J, Wilcox MD, Hildebrandt JD. The relationship of G(o)α subunit deamidation to the tissue distribution, nucleotide binding properties, and βγ dimer interactions of G(o)α subunit isoforms Journal of Neurochemistry. 73: 633-640. PMID 10428059 DOI: 10.1046/J.1471-4159.1999.0730633.X |
0.322 |
|
| 1998 |
McIntire WE, Schey KL, Knapp DR, Hildebrandt JD. A major G protein alpha O isoform in bovine brain is deamidated at Asn346 and Asn347, residues involved in receptor coupling. Biochemistry. 37: 14651-8. PMID 9778339 DOI: 10.1021/Bi981642Q |
0.576 |
|
| 1998 |
Cook LA, Schey KL, Wilcox MD, Dingus J, Hildebrandt JD. Heterogeneous processing of a G protein gamma subunit at a site critical for protein and membrane interactions. Biochemistry. 37: 12280-6. PMID 9724542 DOI: 10.1021/Bi980230E |
0.564 |
|
| 1998 |
Wu G, Benovic JL, Hildebrandt JD, Lanier SM. Receptor docking sites for G-protein βγ subunits. Implications for signal regulation Journal of Biological Chemistry. 273: 7197-7200. PMID 9516410 DOI: 10.1074/Jbc.273.13.7197 |
0.438 |
|
| 1998 |
McIntire WE, Dingus J, Schey KL, Hildebrandt JD. Characterization of the Major Bovine Brain Go α Isoforms Journal of Biological Chemistry. 273: 33135-33141. DOI: 10.1074/Jbc.273.50.33135 |
0.445 |
|
| 1997 |
Hildebrandt JD. Role of subunit diversity in signaling by heterotrimeric G proteins Biochemical Pharmacology. 54: 325-339. PMID 9278091 DOI: 10.1016/S0006-2952(97)00269-4 |
0.555 |
|
| 1997 |
Chen Y, Weng G, Li J, Harry A, Pieroni J, Dingus J, Hildebrandt JD, Guarnieri F, Weinstein H, Iyengar R. A surface on the G protein beta-subunit involved in interactions with adenylyl cyclases. Proceedings of the National Academy of Sciences of the United States of America. 94: 2711-4. PMID 9122261 DOI: 10.1073/Pnas.94.6.2711 |
0.464 |
|
| 1997 |
Sato M, Ribas C, Hildebrandt JD, Lanier SM. Characterization of a G-protein activator in the neuroblastoma-glioma cell hybrid NG108-15. The Journal of Biological Chemistry. 271: 30052-60. PMID 8939952 DOI: 10.1074/Jbc.271.47.30052 |
0.552 |
|
| 1996 |
Weng G, Li J, Dingus J, Hildebrandt JD, Weinstein H, Iyengar R. Gbeta subunit interacts with a peptide encoding region 956-982 of adenylyl cyclase 2. Cross-linking of the peptide to free Gbetagamma but not the heterotrimer. The Journal of Biological Chemistry. 271: 26445-8. PMID 8900107 DOI: 10.1074/Jbc.271.43.26445 |
0.342 |
|
| 1996 |
Makhlouf M, Ashton SH, Hildebrandt J, Mehta N, Gettys TW, Halushka PV, Cook JA. Alterations in macrophage G proteins are associated with endotoxin tolerance. Biochimica Et Biophysica Acta. 1312: 163-8. PMID 8672540 DOI: 10.1016/0167-4889(96)00019-5 |
0.35 |
|
| 1995 |
Wilcox MD, Dingus J, Balcueva EA, McIntire WE, Mehta ND, Schey KL, Robishaw JD, Hildebrandt JD. Bovine brain GO isoforms have distinct γ subunit compositions Journal of Biological Chemistry. 270: 4189-4192. PMID 7876173 DOI: 10.1074/Jbc.270.9.4189 |
0.454 |
|
| 1995 |
Sato M, Kataoka R, Dingus J, Wilcox M, Hildebrandt JD, Lanier SM. Factors determining specificity of signal transduction by G-protein- coupled receptors. Regulation of signal transfer from receptor to G-protein Journal of Biological Chemistry. 270: 15269-15276. PMID 7797513 DOI: 10.1074/Jbc.270.25.15269 |
0.512 |
|
| 1994 |
Dingus J, Wilcox MD, Kohnken R, Hildebrandt JD. [36] Synthesis and use of biotinylated βγ complexes prepared from bovine brain G proteins Methods in Enzymology. 237: 457-471. DOI: 10.1016/S0076-6879(94)37083-4 |
0.467 |
|
| 1985 |
Codina J, Rosenthal W, Hildebrandt JD, Birnbaumer L, Sekura RD. [38] Purification of Ns and Ni, the coupling proteins of hormone-sensitive adenylyl cyclases without intervention of activating regulatory ligands Methods in Enzymology. 109: 446-465. PMID 3921803 DOI: 10.1016/0076-6879(85)09108-X |
0.406 |
|
| 1985 |
Hildebrandt JD, Codina J, Tash JS, Kirchick HJ, Lipschultz L, Sekura RD, Birnbaumer L. The membrane-bound spermatozoal adenylyl cyclase system does not share coupling characteristics with somatic cell adenylyl cyclases. Endocrinology. 116: 1357-66. PMID 3918851 DOI: 10.1210/Endo-116-4-1357 |
0.314 |
|
| 1985 |
Birnbaumer L, Codina J, Mattera R, Cerione RA, Hildebrandt JD, Sunyer T, Rojas FJ, Caron MG, Lefkowitz RJ, Iyengar R. Regulation of hormone receptors and adenylyl cyclases by guanine nucleotide binding N proteins. Recent Progress in Hormone Research. 41: 41-99. PMID 2996090 DOI: 10.1016/B978-0-12-571141-8.50006-8 |
0.439 |
|
| 1985 |
Ribeiro-Neto FA, Mattera R, Hildebrandt JD, Codina J, Field JB, Birnbaumer L, Sekura RD. ADP-ribosylation of membrane components by pertussis and cholera toxin. Methods in Enzymology. 109: 566-72. PMID 2859516 DOI: 10.1016/0076-6879(85)09115-7 |
0.349 |
|
| 1983 |
Codina J, Hildebrandt J, Iyengar R, Birnbaumer L, Sekura RD, Manclark CR. Pertussis toxin substrate, the putative Ni component of adenylyl cyclases, is an alpha beta heterodimer regulated by guanine nucleotide and magnesium. Proceedings of the National Academy of Sciences of the United States of America. 80: 4276-80. PMID 6308612 DOI: 10.1073/Pnas.80.14.4276 |
0.401 |
|
| 1983 |
Hildebrandt JD, Sekura RD, Codina J, Iyengar R, Manclark CR, Birnbaumer L. Stimulation and inhibition of adenylyl cyclases mediated by distinct regulatory proteins. Nature. 302: 706-9. PMID 6300694 DOI: 10.1038/302706A0 |
0.417 |
|
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