| Year |
Citation |
Score |
| 2007 |
Huang L, Min JN, Masters S, Mivechi NF, Moskophidis D. Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption. Genesis (New York, N.Y. : 2000). 45: 487-501. PMID 17661394 DOI: 10.1002/Dvg.20319 |
0.366 |
|
| 2006 |
Du Y, Masters SC, Khuri FR, Fu H. Monitoring 14-3-3 protein interactions with a homogeneous fluorescence polarization assay. Journal of Biomolecular Screening. 11: 269-76. PMID 16699128 DOI: 10.1177/1087057105284862 |
0.639 |
|
| 2004 |
Masters SC. Internet resources for studying protein-protein interactions. Methods in Molecular Biology (Clifton, N.J.). 261: 519-24. PMID 15064480 DOI: 10.1385/1-59259-762-9:519 |
0.412 |
|
| 2004 |
Masters SC. Co-immunoprecipitation from transfected cells. Methods in Molecular Biology (Clifton, N.J.). 261: 337-50. PMID 15064468 DOI: 10.1385/1-59259-762-9:337 |
0.514 |
|
| 2004 |
Chen J, Williams IR, Kutok JL, Duclos N, Anastasiadou E, Masters SC, Fu H, Gilliland DG. Positive and negative regulatory roles of the WW-like domain in TEL-PDGFbetaR transformation. Blood. 104: 535-42. PMID 15054045 DOI: 10.1182/Blood-2004-01-0169 |
0.563 |
|
| 2003 |
Hamaguchi A, Suzuki E, Murayama K, Fujimura T, Hikita T, Iwabuchi K, Handa K, Withers DA, Masters SC, Fu H, Hakomori S. A sphingosine-dependent protein kinase that specifically phosphorylates 14-3-3 (SDK1) is identified as the kinase domain of PKCδ: A preliminary note Biochemical and Biophysical Research Communications. 307: 589-594. PMID 12893264 DOI: 10.1016/S0006-291X(03)01070-2 |
0.579 |
|
| 2003 |
Hamaguchi A, Suzuki E, Murayama K, Fujimura T, Hikita T, Iwabuchi K, Handa K, Withers DA, Masters SC, Fu H, Hakomori S. Sphingosine-dependent Protein Kinase-1, Directed to 14-3-3, Is Identified as the Kinase Domain of Protein Kinase Cδ Journal of Biological Chemistry. 278: 41557-41565. PMID 12855683 DOI: 10.1074/Jbc.M305294200 |
0.604 |
|
| 2002 |
Truong AB, Masters SC, Yang H, Fu H. Role of the 14-3-3 C-terminal loop in ligand interaction. Proteins. 49: 321-5. PMID 12360521 DOI: 10.1002/Prot.10210 |
0.694 |
|
| 2002 |
Masters SC, Subramanian RR, Truong A, Yang H, Fujii K, Zhang H, Fu H. Survival-promoting functions of 14-3-3 proteins. Biochemical Society Transactions. 30: 360-5. PMID 12196095 DOI: 10.1042/Bst0300360 |
0.753 |
|
| 2002 |
Masters SC, Subramanian RR, Truong A, Yang H, Fujii K, Zhang H, Fu H. Prosurvival Function of 14-3-3 Proteins Biochemical Society Transactions. 30: A62-A62. DOI: 10.1042/Bst030A062A |
0.706 |
|
| 2001 |
Masters SC, Yang H, Datta SR, Greenberg ME, Fu H. 14-3-3 inhibits Bad-induced cell death through interaction with serine-136. Molecular Pharmacology. 60: 1325-31. PMID 11723239 DOI: 10.1124/Mol.60.6.1325 |
0.65 |
|
| 2001 |
Subramanian RR, Masters SC, Zhang H, Fu H. Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis. Experimental Cell Research. 271: 142-51. PMID 11697890 DOI: 10.1006/Excr.2001.5376 |
0.757 |
|
| 2001 |
Masters SC, Fu H. 14-3-3 proteins mediate an essential anti-apoptotic signal. The Journal of Biological Chemistry. 276: 45193-200. PMID 11577088 DOI: 10.1074/Jbc.M105971200 |
0.683 |
|
| 2001 |
Yang H, Masters SC, Wang H, Fu H. The proapoptotic protein Bad binds the amphipathic groove of 14-3-3zeta. Biochimica Et Biophysica Acta. 1547: 313-9. PMID 11410287 DOI: 10.1016/S0167-4838(01)00202-3 |
0.735 |
|
| 2001 |
Chiang CW, Harris G, Ellig C, Masters SC, Subramanian R, Shenolikar S, Wadzinski BE, Yang E. Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin- 3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation. Blood. 97: 1289-97. PMID 11222372 DOI: 10.1182/Blood.V97.5.1289 |
0.702 |
|
| 2000 |
Athwal GS, Lombardo CR, Huber JL, Masters SC, Fu H, Huber SC. Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors. Plant & Cell Physiology. 41: 523-33. PMID 10845467 DOI: 10.1093/Pcp/41.4.523 |
0.622 |
|
| 2000 |
Fu H, Subramanian RR, Masters SC. 14-3-3 proteins: structure, function, and regulation. Annual Review of Pharmacology and Toxicology. 40: 617-47. PMID 10836149 DOI: 10.1146/Annurev.Pharmtox.40.1.617 |
0.762 |
|
| 1999 |
Zhang L, Wang H, Masters SC, Wang B, Barbieri JT, Fu H. Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa. Biochemistry. 38: 12159-64. PMID 10508420 DOI: 10.1021/Bi991019L |
0.608 |
|
| 1999 |
Masters SC, Pederson KJ, Zhang L, Barbieri JT, Fu H. Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa. Biochemistry. 38: 5216-21. PMID 10213629 DOI: 10.1021/Bi982492M |
0.677 |
|
| 1998 |
Petosa C, Masters SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC. 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. The Journal of Biological Chemistry. 273: 16305-10. PMID 9632691 DOI: 10.1074/jbc.273.26.16305 |
0.542 |
|
| 1998 |
Yang H, Masters SC, Wang H, Fu H. Death agonist bad and raf-1 kinase interact with 14-3-3 through a common site Faseb Journal. 12. |
0.4 |
|
| 1998 |
Subramanian RR, Yang H, Wjicox JN, Masters SC, Fu H. Isoform specificity of 14-3-3 proteins Faseb Journal. 12. |
0.724 |
|
| 1997 |
Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell. 91: 231-41. PMID 9346240 DOI: 10.1016/S0092-8674(00)80405-5 |
0.57 |
|
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