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Kimon C. Kanelakis, Ph.D. - Publications

Affiliations: 
2002 University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Pharmacology, Molecular Biology
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17 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2013 Lim WK, Kanelakis KC, Neubig RR. Regulation of G protein signaling by the 70kDa heat shock protein. Cellular Signalling. 25: 389-96. PMID 23153586 DOI: 10.1016/J.Cellsig.2012.11.002  0.533
2004 Galigniana MD, Piwien Pilipuk G, Kanelakis KC, Burton G, Lantos CP. Molecular mechanism of activation and nuclear translocation of the mineralocorticoid receptor upon binding of pregnanesteroids. Molecular and Cellular Endocrinology. 217: 167-79. PMID 15134815 DOI: 10.1016/J.Mce.2003.10.041  0.435
2003 Kanelakis KC, Pratt WB. Regulation of glucocorticoid receptor ligand-binding activity by the hsp90/hsp70-based chaperone machinery. Methods in Enzymology. 364: 159-73. PMID 14631845 DOI: 10.1016/S0076-6879(03)64010-3  0.778
2003 Morishima Y, Kanelakis KC, Murphy PJ, Lowe ER, Jenkins GJ, Osawa Y, Sunahara RK, Pratt WB. The hsp90 cochaperone p23 is the limiting component of the multiprotein hsp90/hsp70-based chaperone system in vivo where it acts to stabilize the client protein: hsp90 complex. The Journal of Biological Chemistry. 278: 48754-63. PMID 14507910 DOI: 10.1074/Jbc.M309814200  0.78
2003 Zhang Z, Quick MK, Kanelakis KC, Gijzen M, Krishna P. Characterization of a plant homolog of hop, a cochaperone of hsp90. Plant Physiology. 131: 525-35. PMID 12586877 DOI: 10.1104/Pp.011940  0.664
2003 Krishna P, Kanelakis KC. The 70-kDa protein bound to hsp90 in wheat germ lysate is a plant homologue of animal Hop Physiologia Plantarum. 119: 456-462. DOI: 10.1034/J.1399-3054.2003.00185.X  0.642
2002 Piwien-Pilipuk G, Kanelakis KC, Galigniana MD. Correlation between pregnanesteroid conformation, receptor affinity, and anti-natriuretic effect. European Journal of Pharmacology. 454: 131-43. PMID 12421640 DOI: 10.1016/S0014-2999(02)02492-5  0.39
2002 Kanelakis KC, Shewach DS, Pratt WB. Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly. The Journal of Biological Chemistry. 277: 33698-703. PMID 12093808 DOI: 10.1074/Jbc.M204164200  0.761
2002 Billecke SS, Bender AT, Kanelakis KC, Murphy PJ, Lowe ER, Kamada Y, Pratt WB, Osawa Y. hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90. The Journal of Biological Chemistry. 277: 20504-9. PMID 11923316 DOI: 10.1074/Jbc.M201940200  0.694
2002 Piwien-Pilipuk G, Kanelakis KC, Ghini AA, Lantos CP, Litwack G, Burton G, Galigniana MD. Modification of an essential amino group in the mineralocorticoid receptor evidences a differential conformational change of the receptor protein upon binding of antagonists, natural agonists and the synthetic agonist 11,19-oxidoprogesterone. Biochimica Et Biophysica Acta. 1589: 31-48. PMID 11909639 DOI: 10.1016/S0167-4889(01)00184-7  0.477
2001 Murphy PJ, Kanelakis KC, Galigniana MD, Morishima Y, Pratt WB. Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate. The Journal of Biological Chemistry. 276: 30092-8. PMID 11404358 DOI: 10.1074/Jbc.M103773200  0.785
2001 Morishima Y, Kanelakis KC, Murphy PJ, Shewach DS, Pratt WB. Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes. Biochemistry. 40: 1109-16. PMID 11170435 DOI: 10.1021/Bi002399+  0.755
2000 Kanelakis KC, Murphy PJ, Galigniana MD, Morishima Y, Takayama S, Reed JC, Toft DO, Pratt WB. hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1. Biochemistry. 39: 14314-21. PMID 11087380 DOI: 10.1021/Bi001671C  0.732
2000 Morishima Y, Kanelakis KC, Silverstein AM, Dittmar KD, Estrada L, Pratt WB. The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system. The Journal of Biological Chemistry. 275: 6894-900. PMID 10702249 DOI: 10.1074/Jbc.275.10.6894  0.792
1999 Silverstein AM, Galigniana MD, Kanelakis KC, Radanyi C, Renoir JM, Pratt WB. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. The Journal of Biological Chemistry. 274: 36980-6. PMID 10601253 DOI: 10.1074/Jbc.274.52.36980  0.73
1999 Kanelakis KC, Morishima Y, Dittmar KD, Galigniana MD, Takayama S, Reed JC, Pratt WB. Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery. The Journal of Biological Chemistry. 274: 34134-40. PMID 10567384 DOI: 10.1074/Jbc.274.48.34134  0.787
1999 Bender AT, Silverstein AM, Demady DR, Kanelakis KC, Noguchi S, Pratt WB, Osawa Y. Neuronal nitric-oxide synthase is regulated by the Hsp90-based chaperone system in vivo. The Journal of Biological Chemistry. 274: 1472-8. PMID 9880522 DOI: 10.1074/Jbc.274.3.1472  0.735
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