| Year |
Citation |
Score |
| 2020 |
Farago AF, Demetri GD. Larotrectinib, a selective tropomyosin receptor kinase inhibitor for adult and pediatric tropomyosin receptor kinase fusion cancers. Future Oncology (London, England). PMID 32129093 DOI: 10.2217/fon-2019-0647 |
0.391 |
|
| 2015 |
Farago AF, Le LP, Zheng Z, Muzikansky A, Drilon A, Patel M, Bauer TM, Liu SV, Ou SI, Jackman D, Costa DB, Multani PS, Li GG, Hornby Z, Chow-Maneval E, et al. Durable Clinical Response to Entrectinib in NTRK1-Rearranged Non-Small Cell Lung Cancer. Journal of Thoracic Oncology : Official Publication of the International Association For the Study of Lung Cancer. PMID 26565381 DOI: 10.1097/01.JTO.0000473485.38553.f0 |
0.351 |
|
| 2015 |
Burris HA, Brose MS, Shaw AT, Bauer TM, Farago AF, Doebele RC, Smith S, Fernandes M, Cruickshank S, Low JA. A first-in-human study of LOXO-101, a highly selective inhibitor of the tropomyosin receptor kinase (TRK) family. Journal of Clinical Oncology. 33: TPS2624-TPS2624. DOI: 10.1200/JCO.2015.33.15_SUPPL.TPS2624 |
0.337 |
|
| 2006 |
Sipeki S, Bander E, Parker PJ, Faragó A. PKCalpha reduces the lipid kinase activity of the p110alpha/p85alpha PI3K through the phosphorylation of the catalytic subunit. Biochemical and Biophysical Research Communications. 339: 122-5. PMID 16297884 DOI: 10.1016/J.Bbrc.2005.10.194 |
0.674 |
|
| 2004 |
Gujdár A, Sipeki S, Bander E, Buday L, Faragó A. Protein kinase C modulates negatively the hepatocyte growth factor-induced migration, integrin expression and phosphatidylinositol 3-kinase activation. Cellular Signalling. 16: 505-13. PMID 14709339 DOI: 10.1016/J.Cellsig.2003.09.009 |
0.721 |
|
| 2003 |
Gujdár A, Sipeki S, Bander E, Buday L, Faragó A. Phorbol ester-induced migration of HepG2 cells is accompanied by intensive stress fibre formation, enhanced integrin expression and transient down-regulation of p21-activated kinase 1. Cellular Signalling. 15: 307-18. PMID 12531429 DOI: 10.1016/S0898-6568(02)00087-6 |
0.722 |
|
| 2003 |
Tamás P, Solti Z, Bauer P, Illés A, Sipeki S, Bauer A, Faragó A, Downward J, Buday L. Mechanism of epidermal growth factor regulation of Vav2, a guanine nucleotide exchange factor for Rac. The Journal of Biological Chemistry. 278: 5163-71. PMID 12454019 DOI: 10.1074/Jbc.M207555200 |
0.622 |
|
| 2002 |
Sipeki S, Bander E, Ways DK, Faragó A. Activation of Erk1/Erk2 and transiently increased p53 levels together may account for p21 expression associated with phorbol ester-induced transient growth inhibition in HepG2 cells. Cellular Signalling. 14: 115-21. PMID 11781135 DOI: 10.1016/S0898-6568(01)00229-7 |
0.566 |
|
| 2000 |
Sipeki S, Bander E, Farkas G, Gujdár A, Ways DK, Faragó A. Protein kinase C decreases the hepatocyte growth factor-induced activation of Erk1/Erk2 MAP kinases. Cellular Signalling. 12: 549-55. PMID 11027948 DOI: 10.1016/S0898-6568(00)00105-4 |
0.731 |
|
| 1999 |
Sipeki S, Bander E, Buday L, Farkas G, Bácsy E, Ways DK, Faragó A. Phosphatidylinositol 3-kinase contributes to Erk1/Erk2 MAP kinase activation associated with hepatocyte growth factor-induced cell scattering. Cellular Signalling. 11: 885-90. PMID 10659996 DOI: 10.1016/S0898-6568(99)00060-1 |
0.665 |
|
| 1999 |
Wunderlich L, Gohér A, Faragó A, Downward J, Buday L. Requirement of multiple SH3 domains of Nck for ligand binding. Cellular Signalling. 11: 253-62. PMID 10372803 DOI: 10.1016/S0898-6568(98)00054-0 |
0.404 |
|
| 1999 |
Wunderlich L, Faragó A, Downward J, Buday L. Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes. European Journal of Immunology. 29: 1068-75. PMID 10229072 DOI: 10.1002/(Sici)1521-4141(199904)29:04<1068::Aid-Immu1068>3.0.Co;2-P |
0.523 |
|
| 1999 |
Wunderlich L, Faragó A, Buday L. Characterization of interactions of Nck with Sos and dynamin. Cellular Signalling. 11: 25-9. PMID 10206341 DOI: 10.1016/S0898-6568(98)00027-8 |
0.334 |
|
| 1997 |
Mócsai A, Bánfi B, Kapus A, Farkas G, Geiszt M, Buday L, Faragó A, Ligeti E. Differential effects of tyrosine kinase inhibitors and an inhibitor of the mitogen-activated protein kinase cascade on degranulation and superoxide production of human neutrophil granulocytes. Biochemical Pharmacology. 54: 781-9. PMID 9353132 DOI: 10.1016/S0006-2952(97)00245-1 |
0.648 |
|
| 1996 |
Mihalik R, Farkas G, Kopper L, Benczúr M, Faragó A. Possible involvement of protein kinase C-epsilon in phorbol ester-induced growth inhibition of human lymphoblastic cells. The International Journal of Biochemistry & Cell Biology. 28: 925-33. PMID 8811841 DOI: 10.1016/1357-2725(96)00020-9 |
0.538 |
|
| 1996 |
Buday L, Khwaja A, Sipeki S, Faragó A, Downward J. Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation. The Journal of Biological Chemistry. 271: 6159-63. PMID 8626404 DOI: 10.1074/Jbc.271.11.6159 |
0.543 |
|
| 1994 |
Farkas G, Buday L, Csermely P, Faragó A. Lipocortin I is not accessible for protein kinase C bound to the cytoplasmic surface of the plasma membrane in streptolysin-O-permeabilized pig granulocytes. Biochimica Et Biophysica Acta. 1220: 315-22. PMID 8305505 DOI: 10.1016/0167-4889(94)90155-4 |
0.554 |
|
| 1994 |
Bauer PI, Farkas G, Mihalik R, Kopper L, Kun E, Faragó A. Phosphorylation of poly(ADP-ribose)polymerase protein in human peripheral lymphocytes stimulated with phytohemagglutinin. Biochimica Et Biophysica Acta. 1223: 234-9. PMID 8086493 DOI: 10.1016/0167-4889(94)90231-3 |
0.652 |
|
| 1992 |
Buday L, Farkas G, Faragó A. Synthetic oligopeptide substrates which fail to compete with H1 histone for type II and type III isoenzymes of protein kinase C. The International Journal of Biochemistry. 24: 777-82. PMID 1592153 DOI: 10.1016/0020-711X(92)90011-O |
0.495 |
|
| 1992 |
Hajnóczky G, Várnai P, Buday L, Faragó A, Spät A. The role of protein kinase-C in control of aldosterone production by rat adrenal glomerulosa cells: activation of protein kinase-C by stimulation with potassium. Endocrinology. 130: 2230-6. PMID 1547736 DOI: 10.1210/Endo.130.4.1547736 |
0.547 |
|
| 1992 |
Bauer PI, Farkas G, Buday L, Mikala G, Meszaros G, Kun E, Farago A. Inhibition of DNA binding by the phosphorylation of poly ADP-ribose polymerase protein catalysed by protein kinase C. Biochemical and Biophysical Research Communications. 187: 730-6. PMID 1530631 DOI: 10.1016/0006-291X(92)91256-P |
0.61 |
|
| 1991 |
Farkas G, Buday L, Antoni F, Faragó A. The 38 kDa Ca2+/membrane-binding protein of pig granulocytes needs a high Ca2+ concentration to be phosphorylated by protein kinase C. Biochimica Et Biophysica Acta. 1091: 81-6. PMID 1995069 DOI: 10.1016/0167-4889(91)90225-M |
0.6 |
|
| 1990 |
Farago A, Nishizuka Y. Protein kinase C in transmembrane signalling. Febs Letters. 268: 350-4. PMID 2200716 DOI: 10.1016/0014-5793(90)81284-U |
0.458 |
|
| 1990 |
Buday L, Faragó A. Dual effect of arachidonic acid on protein kinase C isoenzymes isolated from rabbit thymus cells. Febs Letters. 276: 223-6. PMID 2125008 DOI: 10.1016/0014-5793(90)80547-V |
0.489 |
|
| 1989 |
Olah Z, Bogre L, Lehel C, Farago A, Seprodi J, Dudits D. The phosphorylation site of Ca(2+)-dependent protein kinase from alfalfa. Plant Molecular Biology. 12: 453-61. PMID 24272905 DOI: 10.1007/Bf00017584 |
0.615 |
|
| 1989 |
Faragó A, Farkas G, Mészáros G, Buday L, Antoni F, Seprödi J. Isoenzyme patterns of protein kinase C and a phospholipid-dependent but Ca2+-inhibited enzyme fraction in the crude extracts of different tissues. Febs Letters. 243: 328-32. PMID 2917653 DOI: 10.1016/0014-5793(89)80155-3 |
0.529 |
|
| 1989 |
Buday L, Mészáros G, Farkas G, Seprödi J, Antoni F, Faragó A. Two components of type III protein kinase C with different substrate specificities and a phospholipid-dependent but Ca2+-inhibited protein kinase in rat brain. Febs Letters. 249: 324-8. PMID 2544454 DOI: 10.1016/0014-5793(89)80651-9 |
0.616 |
|
| 1988 |
Faragó A, Seprõdi J, Spät A. Subcellular distribution of protein kinase C in rat adrenal glomerulosa cells. Biochemical and Biophysical Research Communications. 156: 628-33. PMID 3190673 DOI: 10.1016/S0006-291X(88)80889-1 |
0.62 |
|
| 1988 |
Mandl J, Mucha I, Bánhegyi G, Mészáros G, Faragó A, Spolarics Z, Machovich R, Antoni F, Garzó T. cAMP dependent inhibition of thromboxane A2, prostacyclin and PGF2 alpha synthesis in mouse hepatocytes. Prostaglandins. 36: 761-72. PMID 2854284 DOI: 10.1016/0090-6980(88)90054-8 |
0.509 |
|
| 1988 |
Bánhegyi G, Garzó T, Mészáros G, Faragó A, Antoni F, Mandl J. Cyclic AMP-dependent phosphorylation in the control of biotransformation in the liver. Biochemical Pharmacology. 37: 849-54. PMID 2830884 DOI: 10.1016/0006-2952(88)90171-2 |
0.435 |
|
| 1987 |
Buday L, Seprödi J, Farkas G, Mészáros G, Romhányi T, Bánhegyi G, Mandl J, Antoni F, Faragó A. Proteolytic activation of protein kinase C in the extracts of cells treated for a short time with phorbol ester. Febs Letters. 223: 15-9. PMID 3666136 DOI: 10.1016/0014-5793(87)80501-X |
0.652 |
|
| 1986 |
Romhányi T, Seprödi J, Antoni F, Mészáros G, Buday L, Faragó A. The assay of the activity of protein kinase C with the synthetic oligopeptide substrate designed for histone kinase II. Biochimica Et Biophysica Acta. 888: 325-31. PMID 3019424 DOI: 10.1016/0167-4889(86)90232-6 |
0.616 |
|
| 1985 |
Romhányi T, Seprödi J, Antoni F, Mészáros G, Faragó A. Specific substrate for histone kinase II: a synthetic nonapeptide. Biochimica Et Biophysica Acta. 827: 144-9. PMID 2981556 DOI: 10.1016/0167-4838(85)90083-4 |
0.449 |
|
| 1984 |
Farkas G, Enyedi A, Sarkadi B, Gárdos G, Nagy Z, Faragó A. Cyclic AMP-dependent protein kinase stimulates the phosphorylation of phosphatidylinositol to phosphatidylinositol-4-monophosphate in a plasma membrane preparation from pig granulocytes. Biochemical and Biophysical Research Communications. 124: 871-6. PMID 6095827 DOI: 10.1016/0006-291X(84)91038-6 |
0.513 |
|
| 1984 |
Enyedi A, Faragó A, Sarkadi B, Gárdos G. Cyclic AMP-dependent protein kinase and Ca2+-calmodulin stimulate the formation of polyphosphoinositides in a sarcoplasmic reticulum preparation of rabbit heart. Febs Letters. 176: 235-8. PMID 6092135 DOI: 10.1016/0014-5793(84)80948-5 |
0.524 |
|
| 1983 |
Enyedi A, Faragó A, Sarkadi B, Szász I, Gárdos G. Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in the plasma membranes of different blood cells. Febs Letters. 161: 158-62. PMID 6309575 DOI: 10.1016/0014-5793(83)80751-0 |
0.549 |
|
| 1983 |
Sarkadi B, Enyedi A, Faragó A, Mészáros G, Kremmer T, Gárdos G. Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane. Febs Letters. 152: 195-8. PMID 6297997 DOI: 10.1016/0014-5793(83)80378-0 |
0.537 |
|
| 1982 |
Romhányi T, Seprödi J, Mészáros G, Antoni F, Faragó A. The intrinsic substrate specificity of a cyclic nucleotide-independent protein (histone) kinase. Febs Letters. 144: 223-5. PMID 6288470 DOI: 10.1016/0014-5793(82)80642-X |
0.547 |
|
| 1982 |
Romhányi T, Seprödi J, Antoni F, Nikolics K, Mészáros G, Faragó A. The site of histone H2b phosphorylated by a cyclic nucleotide independent histone kinase. Biochimica Et Biophysica Acta. 701: 57-62. PMID 6275900 DOI: 10.1016/0167-4838(82)90312-0 |
0.537 |
|
| 1981 |
Mészáros G, Romhányi T, Antoni F, Faragó A. Subcellular distribution of the subunits of cyclic AMP-dependent protein kinase isoenzymes in human tonsillar lymphocytes. Febs Letters. 134: 139-42. PMID 6273229 DOI: 10.1016/0014-5793(81)80586-8 |
0.522 |
|
| 1981 |
Faragó A, Mészáros G, Antoni F. SUBCELLULAR. DISTRIBUTION OF THE SUBUNITS OF cAMP-DEPENDENT PROTEIN KINASE ISOENZYMES IN HUMAN TONSILLAR LYMPHOCYTES Biochemical Society Transactions. 9. DOI: 10.1042/Bst009232Pe |
0.555 |
|
| 1980 |
Faragó A, Hang PL, Mészáros G, Antoni F. Low molecular weight cyclic AMP binding protein isolated from the extract of human tonsillar lymphocytes. Biochimica Et Biophysica Acta. 632: 649-60. PMID 6254578 DOI: 10.1016/0304-4165(80)90340-2 |
0.404 |
|
| 1979 |
Takáts A, Antoni F, Faragó A. Cyclic nucleotide binding properties and molecular forms of the cyclic-AMP-dependent protein kinase from bovine eye lens. Biochimica Et Biophysica Acta. 568: 475-83. PMID 226149 DOI: 10.1016/0005-2744(79)90316-4 |
0.477 |
|
| 1979 |
Takáts A, Antoni F, Faragó A. Changes of the cAMP-dependent protein kinases during differentiation of lens cells Ophthalmic Research. 11: 366-371. DOI: 10.1159/000265035 |
0.545 |
|
| 1978 |
Takáts A, Antoni F, Faragó A, Kertész P. Some properties of the cyclic AMP dependent protein kinase of epithelial cells and cortical fibers of bovine eye lens. Experimental Eye Research. 26: 389-97. PMID 205426 DOI: 10.1016/0014-4835(78)90126-4 |
0.469 |
|
| 1978 |
Faragó A, Hasznos P, Antoni F, Romhányi T. Two types of cyclic GMP binding site associated with the cyclic AMP-dependent protein kinase from lymphocytes. Biochimica Et Biophysica Acta. 538: 493-504. PMID 203328 DOI: 10.1016/0304-4165(78)90410-5 |
0.373 |
|
| 1975 |
Farago A, Romhanyi T, Antoni F, Takats A, Fabian F. The phosphorylated site of calf thymus F2b histone by the cyclic AMP-dependent protein kinase. Nature. 254: 88. PMID 163445 DOI: 10.1038/254088A0 |
0.564 |
|
| 1974 |
Faragó A, Antoni F, Fábián F. Histone kinases and cyclic AMP-binding capacity of nuclei of human tonsillar lymphocytes. Biochimica Et Biophysica Acta. 370: 459-67. PMID 4374243 DOI: 10.1016/0005-2744(74)90107-7 |
0.611 |
|
| 1973 |
Faragó A, Antoni F, Takáts A, Fábián F. Adenosine 3′:5′-monophosphate-dependent an independent histone kinases isolated from human tonsillar lymphocytes Biochimica Et Biophysica Acta. 297: 517-526. DOI: 10.1016/0304-4165(73)90099-8 |
0.475 |
|
| 1972 |
Takáts A, Faragó A, Antoni F. Adenosine 3':5'-monophosphate dependent protein kinase in the lacrymal gland. Biochimica Et Biophysica Acta. 268: 77-80. PMID 4336172 DOI: 10.1016/0005-2744(72)90199-4 |
0.534 |
|
| 1969 |
Faragó A, Dénes G. Differences between the active and the inhibited conformations of the allosteric N-acetylglutamate 5-phosphotransferase. Biochimica Et Biophysica Acta. 178: 400-2. PMID 5772415 DOI: 10.1016/0005-2744(69)90411-2 |
0.32 |
|
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