Stephen B. Long, Ph.D. - Publications

Sloan Kettering, New York, NY, United States 
Structural Biology

16 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
2014 Diver MM, Long SB. Mutational analysis of the integral membrane methyltransferase isoprenylcysteine carboxyl methyltransferase (ICMT) reveals potential substrate binding sites. The Journal of Biological Chemistry. 289: 26007-20. PMID 25059662 DOI: 10.1074/jbc.M114.585125  0.84
2012 Hou X, Pedi L, Diver MM, Long SB. Crystal structure of the calcium release-activated calcium channel Orai. Science (New York, N.Y.). 338: 1308-13. PMID 23180775 DOI: 10.1126/science.1228757  0.84
2012 Miller AN, Long SB. Crystal structure of the human two-pore domain potassium channel K2P1. Science (New York, N.Y.). 335: 432-6. PMID 22282804 DOI: 10.1126/science.1213274  0.84
2011 Cooper J, Li W, You L, Schiavon G, Pepe-Caprio A, Zhou L, Ishii R, Giovannini M, Hanemann CO, Long SB, Erdjument-Bromage H, Zhou P, Tempst P, Giancotti FG. Merlin/NF2 functions upstream of the nuclear E3 ubiquitin ligase CRL4DCAF1 to suppress oncogenic gene expression. Science Signaling. 4: pt6. PMID 21878678 DOI: 10.1126/scisignal.2002314  0.84
2010 Li W, You L, Cooper J, Schiavon G, Pepe-Caprio A, Zhou L, Ishii R, Giovannini M, Hanemann CO, Long SB, Erdjument-Bromage H, Zhou P, Tempst P, Giancotti FG. Merlin/NF2 suppresses tumorigenesis by inhibiting the E3 ubiquitin ligase CRL4(DCAF1) in the nucleus. Cell. 140: 477-90. PMID 20178741 DOI: 10.1016/j.cell.2010.01.029  0.84
2009 Nimjee SM, Oney S, Volovyk Z, Bompiani KM, Long SB, Hoffman M, Sullenger BA. Synergistic effect of aptamers that inhibit exosites 1 and 2 on thrombin. Rna (New York, N.Y.). 15: 2105-11. PMID 19846574 DOI: 10.1261/rna.1240109  0.84
2008 Long SB, Long MB, White RR, Sullenger BA. Crystal structure of an RNA aptamer bound to thrombin. Rna (New York, N.Y.). 14: 2504-12. PMID 18971322 DOI: 10.1261/rna.1239308  0.84
2007 Long SB, Tao X, Campbell EB, MacKinnon R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature. 450: 376-82. PMID 18004376 DOI: 10.1038/nature06265  0.84
2005 Long SB, Campbell EB, Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science (New York, N.Y.). 309: 897-903. PMID 16002581 DOI: 10.1126/science.1116269  0.84
2005 Long SB, Campbell EB, Mackinnon R. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science (New York, N.Y.). 309: 903-8. PMID 16002579 DOI: 10.1126/science.1116270  0.84
2004 Reid TS, Long SB, Beese LS. Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes. Biochemistry. 43: 9000-8. PMID 15248757 DOI: 10.1021/bi049280b  0.84
2002 Long SB, Casey PJ, Beese LS. Reaction path of protein farnesyltransferase at atomic resolution. Nature. 419: 645-50. PMID 12374986 DOI: 10.1038/nature00986  0.84
2001 Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. Proceedings of the National Academy of Sciences of the United States of America. 98: 12948-53. PMID 11687658 DOI: 10.1073/pnas.241407898  0.84
2001 Terry KL, Long SB, Beese LS. 2 Structure of protein farnesyltransferase Enzymes. 21: 19-46. DOI: 10.1016/S1874-6047(01)80015-9  0.84
2000 Long SB, Casey PJ, Beese LS. The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures. Structure (London, England : 1993). 8: 209-22. PMID 10673434 DOI: 10.1016/S0969-2126(00)00096-4  0.84
1998 Long SB, Casey PJ, Beese LS. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry. 37: 9612-8. PMID 9657673 DOI: 10.1021/bi980708e  0.84
Show low-probability matches.