Timothy A. Key, Ph.D. - Publications

Affiliations: 
2002 University of New Mexico, Albuquerque, NM, United States 
Area:
Molecular Biology, Cell Biology

6 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
2005 Key TA, Vines CM, Wagener BM, Gurevich VV, Sklar LA, Prossnitz ER. Inhibition of chemoattractant N-formyl peptide receptor trafficking by active arrestins. Traffic (Copenhagen, Denmark). 6: 87-99. PMID 15634210 DOI: 10.1111/J.1600-0854.2004.00248.X  0.622
2003 Key TA, Foutz TD, Gurevich VV, Sklar LA, Prossnitz ER. N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity. The Journal of Biological Chemistry. 278: 4041-7. PMID 12424254 DOI: 10.1074/Jbc.M204687200  0.637
2002 Potter RM, Key TA, Gurevich VV, Sklar LA, Prossnitz ER. Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus. The Journal of Biological Chemistry. 277: 8970-8. PMID 11777932 DOI: 10.1074/Jbc.M111086200  0.593
2002 Prossnitz ER, Key TA, Potter RM, Gurevich VV, Slkar LA. S2L5 Mechanisms of arrestin interactions with G protein-coupled receptors Seibutsu Butsuri. 42: S12. DOI: 10.2142/Biophys.42.S12_1  0.522
2001 Key TA, Bennett TA, Foutz TD, Gurevich VV, Sklar LA, Prossnitz ER. Regulation of formyl peptide receptor agonist affinity by reconstitution with arrestins and heterotrimeric G proteins. The Journal of Biological Chemistry. 276: 49204-12. PMID 11598142 DOI: 10.1074/Jbc.M109475200  0.635
2001 Bennett TA, Key TA, Gurevich VV, Neubig R, Prossnitz ER, Sklar LA. Real-time analysis of G protein-coupled receptor reconstitution in a solubilized system. The Journal of Biological Chemistry. 276: 22453-60. PMID 11309376 DOI: 10.1074/Jbc.M009679200  0.628
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