| Year |
Citation |
Score |
| 2022 |
Dai S, Venturini E, Yadav S, Lin X, Clapp D, Steckiewicz M, Gocher-Demske AM, Hardie DG, Edelman AM. Calcium/calmodulin-dependent protein kinase kinase 2 mediates pleiotropic effects of epidermal growth factor in cancer cells. Biochimica Et Biophysica Acta. Molecular Cell Research. 1869: 119252. PMID 35271909 DOI: 10.1016/j.bbamcr.2022.119252 |
0.437 |
|
| 2020 |
Dai S, Gocher AM, Edelman AM. Abstract 1430: CaMKK2 regulates EGF-dependent activation of oncogenic Akt in ovarian cancer cells Immunology. 80: 1430-1430. DOI: 10.1158/1538-7445.Am2020-1430 |
0.562 |
|
| 2017 |
Gocher AM, Azabdaftari G, Euscher LM, Dai S, Karacosta LG, Franke TF, Edelman AM. Akt Activation by Ca2+/calmodulin-dependent protein Kinase Kinase 2 (CaMKK2) in Ovarian Cancer Cells. The Journal of Biological Chemistry. PMID 28634229 DOI: 10.1074/Jbc.M117.778464 |
0.786 |
|
| 2015 |
Karacosta LG, Kuroski LA, Hofmann WA, Azabdaftari G, Mastri M, Gocher AM, Dai S, Hoste AJ, Edelman AM. Nucleoporin 62 and Ca(2+) /calmodulin dependent kinase kinase 2 regulate androgen receptor activity in castrate resistant prostate cancer cells. The Prostate. PMID 26552607 DOI: 10.1002/Pros.23121 |
0.773 |
|
| 2015 |
Gocher AM, Franke TF, Azabdaftari G, Karacosta LG, Edelman AM. Abstract B13: Regulation of Akt activity, cell proliferation, and viability in ovarian cancer cells by calcium/calmodulin-dependent protein kinase kinase 2 Molecular Cancer Therapeutics. 14. DOI: 10.1158/1538-8514.Pi3K14-B13 |
0.792 |
|
| 2013 |
Gocher AM, Azabdaftari G, Edelman AM. Abstract A12: Regulation of ovarian cancer OVCAR-3 cell proliferation and viability by calcium/calmodulin-dependent protein kinase kinase 2 Clinical Cancer Research. 19. DOI: 10.1158/1078-0432.Ovca13-A12 |
0.564 |
|
| 2012 |
Karacosta LG, Foster BA, Azabdaftari G, Feliciano DM, Edelman AM. A regulatory feedback loop between Ca2+/calmodulin-dependent protein kinase kinase 2 (CaMKK2) and the androgen receptor in prostate cancer progression. The Journal of Biological Chemistry. 287: 24832-43. PMID 22654108 DOI: 10.1074/Jbc.M112.370783 |
0.738 |
|
| 2012 |
Srivastava T, Fortin DA, Nygaard S, Kaech S, Sonenberg N, Edelman AM, Soderling TR. Regulation of neuronal mRNA translation by CaM-kinase I phosphorylation of eIF4GII. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 5620-30. PMID 22514323 DOI: 10.1523/Jneurosci.0030-12.2012 |
0.653 |
|
| 2012 |
Karacosta LG, Foster BA, Gissou A, Feliciano DM, Edelman AM. Abstract A10: CaMKK2 regulates cellular proliferation and androgen receptor activity during prostate cancer progression Cancer Research. 72: A10-A10. DOI: 10.1158/1538-7445.Prca2012-A10 |
0.743 |
|
| 2009 |
Abbott MJ, Edelman AM, Turcotte LP. CaMKK is an upstream signal of AMP-activated protein kinase in regulation of substrate metabolism in contracting skeletal muscle. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. 297: R1724-32. PMID 19812359 DOI: 10.1152/Ajpregu.00179.2009 |
0.424 |
|
| 2009 |
Feliciano DM, Edelman AM. Repression of Ca2+/calmodulin-dependent protein kinase IV signaling accelerates retinoic acid-induced differentiation of human neuroblastoma cells. The Journal of Biological Chemistry. 284: 26466-81. PMID 19633294 DOI: 10.1074/Jbc.M109.027680 |
0.745 |
|
| 2005 |
Hawley SA, Pan DA, Mustard KJ, Ross L, Bain J, Edelman AM, Frenguelli BG, Hardie DG. Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metabolism. 2: 9-19. PMID 16054095 DOI: 10.1016/J.Cmet.2005.05.009 |
0.599 |
|
| 2005 |
Edelman AM, Kim WY, Higgins D, Goldstein EG, Oberdoerster M, Sigurdson W. Doublecortin kinase-2, a novel doublecortin-related protein kinase associated with terminal segments of axons and dendrites. The Journal of Biological Chemistry. 280: 8531-43. PMID 15611072 DOI: 10.1074/Jbc.M411027200 |
0.478 |
|
| 2003 |
Qin H, Raught B, Sonenberg N, Goldstein EG, Edelman AM. Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I. The Journal of Biological Chemistry. 278: 48570-9. PMID 14507913 DOI: 10.1074/Jbc.M308781200 |
0.656 |
|
| 2003 |
Shang L, Kwon YG, Nandy S, Lawrence DS, Edelman AM. Catalytic and regulatory domains of doublecortin kinase-1. Biochemistry. 42: 2185-94. PMID 12590608 DOI: 10.1021/Bi026913I |
0.683 |
|
| 1998 |
Anderson KA, Means RL, Huang QH, Kemp BE, Goldstein EG, Selbert MA, Edelman AM, Fremeau RT, Means AR. Components of a calmodulin-dependent protein kinase cascade. Molecular cloning, functional characterization and cellular localization of Ca2+/calmodulin-dependent protein kinase kinase beta. The Journal of Biological Chemistry. 273: 31880-9. PMID 9822657 DOI: 10.1074/Jbc.273.48.31880 |
0.456 |
|
| 1998 |
White RR, Kwon YG, Taing M, Lawrence DS, Edelman AM. Definition of optimal substrate recognition motifs of Ca2+-calmodulin-dependent protein kinases IV and II reveals shared and distinctive features. The Journal of Biological Chemistry. 273: 3166-72. PMID 9452427 DOI: 10.1074/Jbc.273.6.3166 |
0.487 |
|
| 1996 |
Aletta JM, Selbert MA, Nairn AC, Edelman AM. Activation of a calcium-calmodulin-dependent protein kinase I cascade in PC12 cells. The Journal of Biological Chemistry. 271: 20930-4. PMID 8702851 DOI: 10.1074/Jbc.271.34.20930 |
0.593 |
|
| 1996 |
Edelman AM, Mitchelhill KI, Selbert MA, Anderson KA, Hook SS, Stapleton D, Goldstein EG, Means AR, Kemp BE. Multiple Ca(2+)-calmodulin-dependent protein kinase kinases from rat brain. Purification, regulation by Ca(2+)-calmodulin, and partial amino acid sequence. The Journal of Biological Chemistry. 271: 10806-10. PMID 8631893 DOI: 10.1074/Jbc.271.18.10806 |
0.528 |
|
| 1995 |
Lee JC, Edelman AM. Activation of Ca(2+)-calmodulin-dependent protein kinase Ia is due to direct phosphorylation by its activator. Biochemical and Biophysical Research Communications. 210: 631-7. PMID 7755643 DOI: 10.1006/Bbrc.1995.1705 |
0.587 |
|
| 1995 |
Dale S, Wilson WA, Edelman AM, Hardie DG. Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. Febs Letters. 361: 191-5. PMID 7698321 DOI: 10.1016/0014-5793(95)00172-6 |
0.526 |
|
| 1995 |
Haribabu B, Hook SS, Selbert MA, Goldstein EG, Tomhave ED, Edelman AM, Snyderman R, Means AR. Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. The Embo Journal. 14: 3679-86. PMID 7641687 DOI: 10.1002/J.1460-2075.1995.Tb00037.X |
0.578 |
|
| 1995 |
Selbert MA, Anderson KA, Huang QH, Goldstein EG, Means AR, Edelman AM. Phosphorylation and activation of Ca(2+)-calmodulin-dependent protein kinase IV by Ca(2+)-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation. The Journal of Biological Chemistry. 270: 17616-21. PMID 7615569 DOI: 10.1074/Jbc.270.29.17616 |
0.587 |
|
| 1995 |
Hawley SA, Selbert MA, Goldstein EG, Edelman AM, Carling D, Hardie DG. 5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms. The Journal of Biological Chemistry. 270: 27186-91. PMID 7592975 DOI: 10.1074/Jbc.270.45.27186 |
0.571 |
|
| 1994 |
Lee JC, Edelman AM. A protein activator of Ca(2+)-calmodulin-dependent protein kinase Ia. The Journal of Biological Chemistry. 269: 2158-64. PMID 8294471 |
0.492 |
|
| 1994 |
Lee JC, Kwon YG, Lawrence DS, Edelman AM. A requirement of hydrophobic and basic amino acid residues for substrate recognition by Ca2+/calmodulin-dependent protein kinase Ia. Proceedings of the National Academy of Sciences of the United States of America. 91: 6413-7. PMID 8022798 DOI: 10.1073/Pnas.91.14.6413 |
0.421 |
|
| 1992 |
Edelman AM, Higgins DM, Bowman CL, Haber SN, Rabin RA, Cho-Lee J. Myosin light chain kinase is expressed in neurons and glia: immunoblotting and immunocytochemical studies. Brain Research. Molecular Brain Research. 14: 27-34. PMID 1323015 DOI: 10.1016/0169-328X(92)90006-W |
0.44 |
|
| 1992 |
Rabin RA, Edelman AM, Wagner JA. Activation of protein kinase A is necessary but not sufficient for ethanol-induced desensitization of cyclic AMP production. The Journal of Pharmacology and Experimental Therapeutics. 262: 257-62. PMID 1320686 |
0.398 |
|
| 1992 |
DeRemer MF, Saeli RJ, Brautigan DL, Edelman AM. Ca(2+)-calmodulin-dependent protein kinases Ia and Ib from rat brain. II. Enzymatic characteristics and regulation of activities by phosphorylation and dephosphorylation. The Journal of Biological Chemistry. 267: 13466-71. PMID 1320022 |
0.513 |
|
| 1992 |
DeRemer MF, Saeli RJ, Edelman AM. Ca(2+)-calmodulin-dependent protein kinases Ia and Ib from rat brain I. Identification, purification, and structural comparisons. The Journal of Biological Chemistry. 267: 13460-5. PMID 1320021 |
0.462 |
|
| 1991 |
Kennelly PJ, Colburn JC, Lorenzen J, Edelman AM, Stull JT, Krebs EG. Activation mechanism of rabbit skeletal muscle myosin light chain kinase. 5'-p-fluorosulfonylbenzoyl adenosine as a probe of the MgATP-binding site of the calmodulin-bound and calmodulin-free enzyme. Febs Letters. 286: 217-20. PMID 1864371 DOI: 10.1016/0014-5793(91)80977-B |
0.685 |
|
| 1990 |
Kennelly PJ, Starovasnik MA, Edelman AM, Krebs EG. Modulation of the stability of rabbit skeletal muscle myosin light chain kinase through the calmodulin-binding domain. The Journal of Biological Chemistry. 265: 1742-9. PMID 2295654 |
0.514 |
|
| 1990 |
Edelman AM, Lin WH, Osterhout DJ, Bennett MK, Kennedy MB, Krebs EG. Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase. Molecular and Cellular Biochemistry. 97: 87-98. PMID 2174101 DOI: 10.1007/Bf00231704 |
0.694 |
|
| 1988 |
Blumenthal DK, Charbonneau H, Edelman AM, Hinds TR, Rosenberg GB, Storm DR, Vincenzi FF, Beavo JA, Krebs EG. Synthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymes. Biochemical and Biophysical Research Communications. 156: 860-5. PMID 2903735 DOI: 10.1016/S0006-291X(88)80923-9 |
0.733 |
|
| 1987 |
Kennelly PJ, Edelman AM, Blumenthal DK, Krebs EG. Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain. The Journal of Biological Chemistry. 262: 11958-63. PMID 3624242 |
0.559 |
|
| 1987 |
Edelman AM, Blumenthal DK, Krebs EG. Protein serine/threonine kinases. Annual Review of Biochemistry. 56: 567-613. PMID 2956925 DOI: 10.1146/Annurev.Bi.56.070187.003031 |
0.586 |
|
| 1987 |
Kennelly PJ, Takio K, Blumenthal DK, Edelman AM, Glaccum MB, Klevit RE, Roush CL, Scott JD, Titani K, Walsh KA, Krebs EG. Organization Of Myosin Light Chain Kinase From Rabbit Skeletal Muscle Calcium-Binding Proteins in Health and Disease. 494-504. DOI: 10.1016/B978-0-12-521040-9.50091-7 |
0.595 |
|
| 1985 |
Edelman AM, Hunter DD, Hendrickson AE, Krebs EG. Subcellular distribution of calcium- and calmodulin-dependent myosin light chain phosphorylating activity in rat cerebral cortex. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 5: 2609-17. PMID 4045548 DOI: 10.1523/Jneurosci.05-10-02609.1985 |
0.596 |
|
| 1985 |
Edelman AM, Takio K, Blumenthal DK, Hansen RS, Walsh KA, Titani K, Krebs EG. Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. The Journal of Biological Chemistry. 260: 11275-85. PMID 3897230 |
0.559 |
|
| 1985 |
Blumenthal DK, Takio K, Edelman AM, Charbonneau H, Titani K, Walsh KA, Krebs EG. Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Proceedings of the National Academy of Sciences of the United States of America. 82: 3187-91. PMID 3858814 DOI: 10.1073/Pnas.82.10.3187 |
0.563 |
|
| 1985 |
Takio K, Blumenthal DK, Edelman AM, Walsh KA, Krebs EG, Titani K. Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase. Biochemistry. 24: 6028-37. PMID 3841288 DOI: 10.1021/Bi00343A002 |
0.612 |
|
| 1985 |
Takio K, Blumenthal DK, Edelman AM. Homology of rabbit skeletal muscle myosin light chain kinase among protein kinases Federation Proceedings. 44: No. 1729. |
0.416 |
|
| 1984 |
Olwin BB, Edelman AM, Krebs EG, Storm DR. Quantitation of energy coupling between Ca2+, calmodulin, skeletal muscle myosin light chain kinase, and kinase substrates. The Journal of Biological Chemistry. 259: 10949-55. PMID 6547956 |
0.587 |
|
| 1983 |
Gallis B, Edelman AM, Casnellie JE, Krebs EG. Epidermal growth factor stimulates tyrosine phosphorylation of the myosin regulatory light chain from smooth muscle. The Journal of Biological Chemistry. 258: 13089-93. PMID 6313687 |
0.625 |
|
| 1982 |
Edelman AM, Krebs EG. Phosphorylation of skeletal muscle myosin light chain kinase by the catalytic subunit of cAMP-dependent protein kinase. Febs Letters. 138: 293-8. PMID 6279448 DOI: 10.1016/0014-5793(82)80464-X |
0.674 |
|
| 1981 |
Andreasen TJ, Keller CH, LaPorte DC, Edelman AM, Storm DR. Preparation of azidocalmodulin: a photoaffinity label for calmodulin-binding proteins. Proceedings of the National Academy of Sciences of the United States of America. 78: 2782-5. PMID 6265911 DOI: 10.1073/Pnas.78.5.2782 |
0.442 |
|
| 1981 |
Edelman AM, Raese JD, Lazar MA, Barchas JD. Tyrosine hydroxylase: studies on the phosphorylation of a purified preparation of the brain enzyme by the cyclic AMP-dependent protein kinase. The Journal of Pharmacology and Experimental Therapeutics. 216: 647-53. PMID 6110771 |
0.68 |
|
| 1979 |
Raese JD, Edelman AM, Makk G, Bruckwick EA, Lovenberg W, Barchas JD. Brain striatal tyrosine hydroxylase: activation of the enzyme by cyclic AMP-independent phosphorylation. Communications in Psychopharmacology. 3: 295-301. PMID 44856 |
0.55 |
|
| 1978 |
Edelman AM, Raese JD, Lazar MA, Barchas JD. In vitro phosphorylation of a purified preparation of bovine corpus striatal tyrosine hydroxylase. Communications in Psychopharmacology. 2: 461-5. PMID 34498 |
0.675 |
|
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