| Year |
Citation |
Score |
| 2020 |
McClelland LJ, Zhang K, Mou TC, Johnston J, Yates-Hansen C, Li S, Thomas CJ, Doukov TI, Triest S, Wohlkonig A, Tall GG, Steyaert J, Chiu W, Sprang SR. Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1. Nature Communications. 11: 1077. PMID 32103024 DOI: 10.1038/S41467-020-14943-4 |
0.407 |
|
| 2020 |
McClelland LJ, Zhang K, Mou T, Johnston J, Yates-Hansen C, Steyaert J, Chiu W, Sprang S. Ric8A-Gα, a Complex Structure of a Guanine Nucleotide Exchange Factor Biophysical Journal. 118: 335a. DOI: 10.1016/J.Bpj.2019.11.1869 |
0.333 |
|
| 2019 |
Zeng B, Mou TC, Doukov TI, Steiner A, Yu W, Papasergi-Scott M, Tall GG, Hagn F, Sprang SR. Structure, Function, and Dynamics of the Gα Binding Domain of Ric-8A. Structure (London, England : 1993). PMID 31155309 DOI: 10.1016/J.Str.2019.04.013 |
0.45 |
|
| 2019 |
Sprang S, McClelland L, Johnston J, Yates-Hansen C, Mou T, Zhang K. The structure of the complex of the cytoplasmic guanine nucleotide exchange factor Ric-8A bound to Gαi1 Acta Crystallographica Section a Foundations and Advances. 75: a175-a175. DOI: 10.1107/S0108767319098258 |
0.324 |
|
| 2018 |
Maziarz M, Leyme A, Marivin A, Luebbers A, Patel PP, Chen Z, Sprang SR, Garcia-Marcos M. Atypical activation of Gαq by the oncogenic mutation Q209P. The Journal of Biological Chemistry. PMID 30352874 DOI: 10.1074/Jbc.Ra118.005291 |
0.359 |
|
| 2018 |
Stump S, Mou TC, Sprang SR, Natale NR, Beall HD. Crystal structure of the major quadruplex formed in the promoter region of the human c-MYC oncogene. Plos One. 13: e0205584. PMID 30312328 DOI: 10.1371/Journal.Pone.0205584 |
0.367 |
|
| 2017 |
Sprang S, Zeng B, McClelland L, Mou T, Yates-Hansen C, Tall G. Structures of Ric-8A, a G protein chaperone and activator Acta Crystallographica Section a Foundations and Advances. 73: a367-a367. DOI: 10.1107/S0108767317096416 |
0.355 |
|
| 2017 |
Black LA, Ross J, Sprang SR. Nucleotide and Nucleotide Exchange Factor Bound Nano to Millisecond Structural-Dynamics of G Alpha Biophysical Journal. 112: 281a. DOI: 10.1016/J.Bpj.2016.11.1522 |
0.395 |
|
| 2016 |
Kant R, Zeng B, Thomas CJ, Bothner B, Sprang SR. Ric-8A, a G protein chaperone with nucleotide exchange activity induces long-range secondary structure changes in Gα. Elife. 5. PMID 28008853 DOI: 10.7554/Elife.19238 |
0.414 |
|
| 2016 |
McClelland LJ, Steele HB, Whitby FG, Mou TC, Holley D, Ross JB, Sprang SR, Bowler BE. Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons. Journal of the American Chemical Society. PMID 27990813 DOI: 10.1021/Jacs.6B10745 |
0.38 |
|
| 2016 |
Yi F, Mou TC, Dorsett KN, Volkmann RA, Menniti FS, Sprang SR, Hansen KB. Structural Basis for Negative Allosteric Modulation of GluN2A-Containing NMDA Receptors. Neuron. PMID 27618671 DOI: 10.1016/J.Neuron.2016.08.014 |
0.368 |
|
| 2016 |
Black LA, Thomas CJ, Nix GN, Terwilliger MC, Sprang SR, Ross JB. Nanosecond Dynamics of Gαi1 Bound to Nucleotides or Ric-8A, a Gα Chaperone with GEF Activity. Biophysical Journal. 111: 722-31. PMID 27558716 DOI: 10.1016/J.Bpj.2016.07.021 |
0.388 |
|
| 2016 |
Sprang SR. Activation of G proteins by GTP and the mechanism of Gα-catalyzed GTP hydrolysis. Biopolymers. PMID 26996924 DOI: 10.1002/Bip.22836 |
0.511 |
|
| 2016 |
Kant R, Zeng B, Thomas CJ, Bothner B, Sprang SR. Author response: Ric-8A, a G protein chaperone with nucleotide exchange activity induces long-range secondary structure changes in Gα Elife. DOI: 10.7554/Elife.19238.017 |
0.354 |
|
| 2015 |
Hahn DK, Tusell JR, Sprang SR, Chu X. Catalytic Mechanism of Mammalian Adenylyl Cyclase: A Computational Investigation. Biochemistry. 54: 6252-62. PMID 26393535 DOI: 10.1021/Acs.Biochem.5B00655 |
0.344 |
|
| 2015 |
Van Eps N, Thomas CJ, Hubbell WL, Sprang SR. The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1. Proceedings of the National Academy of Sciences of the United States of America. 112: 1404-9. PMID 25605908 DOI: 10.1073/Pnas.1423878112 |
0.468 |
|
| 2015 |
McClelland LJ, Mou T, Sprang SR, Bowler BE. Identification and Characterization of a Yeast Iso-1-Cytochrome C C-Terminal Domain Swapped Dimer Biophysical Journal. 108: 213a. DOI: 10.1016/J.Bpj.2014.11.1176 |
0.411 |
|
| 2014 |
McClelland LJ, Mou TC, Jeakins-Cooley ME, Sprang SR, Bowler BE. Structure of a mitochondrial cytochrome c conformer competent for peroxidase activity. Proceedings of the National Academy of Sciences of the United States of America. 111: 6648-53. PMID 24760830 DOI: 10.1073/Pnas.1323828111 |
0.35 |
|
| 2014 |
Black L, Thomas C, Alexander Ross J, Sprang SR. G Protein Activation: A Dynamic Process Biophysical Journal. 106: 101a-102a. DOI: 10.1016/J.Bpj.2013.11.632 |
0.39 |
|
| 2014 |
McClelland LJ, Mou T, Jeakins-Cooley ME, Cherney MM, Sprang SR, Bowler BE. Alternative Conformations of Yeast Iso-1-Cytochrome C: Effects of a Gatekeeping Residue on Heme Crevice Dynamics Biophysical Journal. 106: 226a-227a. DOI: 10.1016/J.Bpj.2013.11.1326 |
0.367 |
|
| 2013 |
Chan P, Thomas CJ, Sprang SR, Tall GG. Molecular chaperoning function of Ric-8 is to fold nascent heterotrimeric G protein α subunits. Proceedings of the National Academy of Sciences of the United States of America. 110: 3794-9. PMID 23431197 DOI: 10.1073/Pnas.1220943110 |
0.304 |
|
| 2013 |
Black L, Nix G, Thomas C, Terwilliger M, Sprang S, Alexander Ross J. Dynamic Motions of G Proteins during Receptor Independent Cell Signaling Biophysical Journal. 104: 71a. DOI: 10.1016/J.Bpj.2012.11.428 |
0.373 |
|
| 2013 |
Thomas CJ, Eps NV, Briknarova K, Hilner JK, Movahed N, Bothner B, Black LA, Hubbell W, Sprang SR. G Protein Activation: A Protein Unfolding Event? Biophysical Journal. 104: 19a. DOI: 10.1016/J.Bpj.2012.11.136 |
0.428 |
|
| 2012 |
Thomas CJ, Shankar S, Casquilho-Gray HE, York J, Sprang SR, Nunberg JH. Biochemical reconstitution of hemorrhagic-fever arenavirus envelope glycoprotein-mediated membrane fusion. Plos One. 7: e51114. PMID 23226473 DOI: 10.1371/Journal.Pone.0051114 |
0.314 |
|
| 2012 |
Chen Z, Guo L, Hadas J, Gutowski S, Sprang SR, Sternweis PC. Activation of p115-RhoGEF requires direct association of Gα13 and the Dbl homology domain. The Journal of Biological Chemistry. 287: 25490-500. PMID 22661716 DOI: 10.1074/Jbc.M111.333716 |
0.405 |
|
| 2012 |
Sprang SR, Elk JC. Cell signaling. Structural origins of receptor bias. Science (New York, N.Y.). 335: 1055-6. PMID 22383838 DOI: 10.1126/Science.1219302 |
0.374 |
|
| 2012 |
Seifert R, Lushington GH, Mou TC, Gille A, Sprang SR. Inhibitors of membranous adenylyl cyclases. Trends in Pharmacological Sciences. 33: 64-78. PMID 22100304 DOI: 10.1016/J.Tips.2011.10.006 |
0.338 |
|
| 2012 |
Chief Elk J, Sprang SR, Ross JA. Free Energy Difference Calculations on Thermodynamic Model of Beta 2 Adrenergic Receptor Activation Biophysical Journal. 102: 514a. DOI: 10.1016/J.Bpj.2011.11.2815 |
0.304 |
|
| 2012 |
Black L, Thomas C, Ross J, Sprang S. Dynamic Motions of the G Protein Subunit G Alpha I1 While Complexed to the GEF Ric-8A Biophysical Journal. 102: 444a-445a. DOI: 10.1016/J.Bpj.2011.11.2436 |
0.427 |
|
| 2011 |
Thomas CJ, Briknarová K, Hilmer JK, Movahed N, Bothner B, Sumida JP, Tall GG, Sprang SR. The nucleotide exchange factor Ric-8A is a chaperone for the conformationally dynamic nucleotide-free state of Gαi1. Plos One. 6: e23197. PMID 21853086 DOI: 10.1371/Journal.Pone.0023197 |
0.341 |
|
| 2011 |
Pinto C, Lushington GH, Richter M, Gille A, Geduhn J, König B, Mou TC, Sprang SR, Seifert R. Structure-activity relationships for the interactions of 2'- and 3'-(O)-(N-methyl)anthraniloyl-substituted purine and pyrimidine nucleotides with mammalian adenylyl cyclases. Biochemical Pharmacology. 82: 358-70. PMID 21620805 DOI: 10.1016/J.Bcp.2011.05.010 |
0.369 |
|
| 2011 |
Hübner M, Dixit A, Mou TC, Lushington GH, Pinto C, Gille A, Geduhn J, König B, Sprang SR, Seifert R. Structural basis for the high-affinity inhibition of mammalian membranous adenylyl cyclase by 2',3'-o-(N-methylanthraniloyl)-inosine 5'-triphosphate. Molecular Pharmacology. 80: 87-96. PMID 21498658 DOI: 10.1124/Mol.111.071894 |
0.439 |
|
| 2011 |
Sprang SR. Cell signalling: Binding the receptor at both ends. Nature. 469: 172-3. PMID 21228868 DOI: 10.1038/469172A |
0.403 |
|
| 2011 |
Thomas CJ, Casquilho-Gray HE, York J, DeCamp DL, Dai D, Petrilli EB, Boger DL, Slayden RA, Amberg SM, Sprang SR, Nunberg JH. A specific interaction of small molecule entry inhibitors with the envelope glycoprotein complex of the Junín hemorrhagic fever arenavirus. The Journal of Biological Chemistry. 286: 6192-200. PMID 21159779 DOI: 10.1074/Jbc.M110.196428 |
0.345 |
|
| 2011 |
Chen Z, Guo L, Sprang SR, Sternweis PC. Modulation of a GEF switch: autoinhibition of the intrinsic guanine nucleotide exchange activity of p115-RhoGEF. Protein Science : a Publication of the Protein Society. 20: 107-17. PMID 21064165 DOI: 10.1002/Pro.542 |
0.43 |
|
| 2011 |
Elk JC, Ross JA, Sprang SR. Molecular Dynamics Investigation on Conformational Dynamics of G Proteins Biophysical Journal. 100: 533a. DOI: 10.1016/J.Bpj.2010.12.3109 |
0.41 |
|
| 2011 |
Sprang SR, Thomas C, Bricknarova K, Sumida J, Tall G. Ric-8a Catalyzed G Protein Activation Proceeds Through a Disordered State Biophysical Journal. 100: 18a. DOI: 10.1016/J.Bpj.2010.12.310 |
0.383 |
|
| 2010 |
Chen Z, Medina F, Liu MY, Thomas C, Sprang SR, Sternweis PC. Activated RhoA binds to the pleckstrin homology (PH) domain of PDZ-RhoGEF, a potential site for autoregulation. The Journal of Biological Chemistry. 285: 21070-81. PMID 20430886 DOI: 10.1074/Jbc.M110.122549 |
0.377 |
|
| 2009 |
Du X, Sprang SR. Transition state structures and the roles of catalytic residues in GAP-facilitated GTPase of Ras as elucidated by (18)O kinetic isotope effects. Biochemistry. 48: 4538-47. PMID 19610677 DOI: 10.1021/Bi802359B |
0.302 |
|
| 2009 |
Suryanarayana S, Göttle M, Hübner M, Gille A, Mou TC, Sprang SR, Richter M, Seifert R. Differential inhibition of various adenylyl cyclase isoforms and soluble guanylyl cyclase by 2',3'-O-(2,4,6-trinitrophenyl)-substituted nucleoside 5'-triphosphates. The Journal of Pharmacology and Experimental Therapeutics. 330: 687-95. PMID 19494187 DOI: 10.1124/Jpet.109.155432 |
0.36 |
|
| 2009 |
Pinto C, Hübner M, Gille A, Richter M, Mou TC, Sprang SR, Seifert R. Differential interactions of the catalytic subunits of adenylyl cyclase with forskolin analogs. Biochemical Pharmacology. 78: 62-9. PMID 19447224 DOI: 10.1016/J.Bcp.2009.03.023 |
0.336 |
|
| 2009 |
Mou TC, Masada N, Cooper DM, Sprang SR. Structural basis for inhibition of mammalian adenylyl cyclase by calcium. Biochemistry. 48: 3387-97. PMID 19243146 DOI: 10.1021/Bi802122K |
0.342 |
|
| 2008 |
Chen Z, Singer WD, Danesh SM, Sternweis PC, Sprang SR. Recognition of the activated states of Galpha13 by the rgRGS domain of PDZRhoGEF. Structure (London, England : 1993). 16: 1532-43. PMID 18940608 DOI: 10.1016/J.Str.2008.07.009 |
0.472 |
|
| 2008 |
Thomas CJ, Tall GG, Adhikari A, Sprang SR. Ric-8A catalyzes guanine nucleotide exchange on G alphai1 bound to the GPR/GoLoco exchange inhibitor AGS3. The Journal of Biological Chemistry. 283: 23150-60. PMID 18541531 DOI: 10.1074/Jbc.M802422200 |
0.332 |
|
| 2007 |
Sprang SR. Structural biology: a receptor unlocked. Nature. 450: 355-6. PMID 18004367 DOI: 10.1038/450355A |
0.349 |
|
| 2007 |
Sprang SR, Chen Z, Du X. Structural basis of effector regulation and signal termination in heterotrimeric Galpha proteins. Advances in Protein Chemistry. 74: 1-65. PMID 17854654 DOI: 10.1016/S0065-3233(07)74001-9 |
0.526 |
|
| 2006 |
Sinha SC, Sprang SR. Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases. Reviews of Physiology, Biochemistry and Pharmacology. 157: 105-40. PMID 17236651 DOI: 10.1007/112_0603 |
0.423 |
|
| 2006 |
Mou TC, Gille A, Suryanarayana S, Richter M, Seifert R, Sprang SR. Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors. Molecular Pharmacology. 70: 878-86. PMID 16766715 DOI: 10.1124/Mol.106.026427 |
0.42 |
|
| 2005 |
Davis TL, Bonacci TM, Sprang SR, Smrcka AV. Structural and molecular characterization of a preferred protein interaction surface on G protein beta gamma subunits. Biochemistry. 44: 10593-604. PMID 16060668 DOI: 10.1021/Bi050655I |
0.399 |
|
| 2005 |
Ja WW, Adhikari A, Austin RJ, Sprang SR, Roberts RW. A peptide core motif for binding to heterotrimeric G protein alpha subunits. The Journal of Biological Chemistry. 280: 32057-60. PMID 16051611 DOI: 10.1074/Jbc.C500319200 |
0.353 |
|
| 2005 |
Sinha SC, Wetterer M, Sprang SR, Schultz JE, Linder JU. Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c. The Embo Journal. 24: 663-73. PMID 15678099 DOI: 10.1038/Sj.Emboj.7600573 |
0.464 |
|
| 2005 |
Chen Z, Singer WD, Sternweis PC, Sprang SR. Structure of the p115RhoGEF rgRGS domain-Galpha13/i1 chimera complex suggests convergent evolution of a GTPase activator. Nature Structural & Molecular Biology. 12: 191-7. PMID 15665872 DOI: 10.1038/Nsmb888 |
0.449 |
|
| 2005 |
Mou TC, Gille A, Fancy DA, Seifert R, Sprang SR. Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate. The Journal of Biological Chemistry. 280: 7253-61. PMID 15591060 DOI: 10.1074/Jbc.M409076200 |
0.485 |
|
| 2004 |
Thomas CJ, Du X, Li P, Wang Y, Ross EM, Sprang SR. Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alpha-subunit. Proceedings of the National Academy of Sciences of the United States of America. 101: 7560-5. PMID 15128951 DOI: 10.1073/Pnas.0304091101 |
0.429 |
|
| 2003 |
Adhikari A, Sprang SR. Thermodynamic characterization of the binding of activator of G protein signaling 3 (AGS3) and peptides derived from AGS3 with G alpha i1. The Journal of Biological Chemistry. 278: 51825-32. PMID 14530282 DOI: 10.1074/Jbc.M306300200 |
0.455 |
|
| 2003 |
Chen Z, Singer WD, Wells CD, Sprang SR, Sternweis PC. Mapping the Galpha13 binding interface of the rgRGS domain of p115RhoGEF. The Journal of Biological Chemistry. 278: 9912-9. PMID 12525488 DOI: 10.1074/Jbc.M212695200 |
0.423 |
|
| 2002 |
Xiao T, Gardner KH, Sprang SR. Cosolvent-induced transformation of a death domain tertiary structure. Proceedings of the National Academy of Sciences of the United States of America. 99: 11151-6. PMID 12177432 DOI: 10.1073/Pnas.172188399 |
0.788 |
|
| 2002 |
Gille A, Liu HY, Sprang SR, Seifert R. Distinct interactions of GTP, UTP, and CTP with G(s) proteins. The Journal of Biological Chemistry. 277: 34434-42. PMID 12080068 DOI: 10.1074/Jbc.M204259200 |
0.371 |
|
| 2002 |
Tesmer JJ, Sunahara RK, Fancy DA, Gilman AG, Sprang SR. Crystallization of complex between soluble domains of adenylyl cyclase and activated Gs alpha. Methods in Enzymology. 345: 198-206. PMID 11665605 DOI: 10.1016/S0076-6879(02)45017-3 |
0.722 |
|
| 2001 |
Chen Z, Wells CD, Sternweis PC, Sprang SR. Structure of the rgRGS domain of p115RhoGEF. Nature Structural Biology. 8: 805-9. PMID 11524686 DOI: 10.1038/Nsb0901-805 |
0.461 |
|
| 2001 |
Sprang S. GEFs: Master regulators of G-protein activation Trends in Biochemical Sciences. 26: 266-267. PMID 11295560 DOI: 10.1016/S0968-0004(01)01818-7 |
0.328 |
|
| 2001 |
Nalefski EA, Wisner MA, Chen JZ, Sprang SR, Fukuda M, Mikoshiba K, Falke JJ. C2 domains from different Ca2+ signaling pathways display functional and mechanistic diversity. Biochemistry. 40: 3089-100. PMID 11258923 DOI: 10.1021/Bi001968A |
0.348 |
|
| 2000 |
Sprang SR. Conformational display: a role for switch polymorphism in the superfamily of regulatory GTPases. Science's Stke : Signal Transduction Knowledge Environment. 2000: pe1. PMID 11752609 DOI: 10.1126/Stke.2000.50.Pe1 |
0.422 |
|
| 2000 |
Xiao T, DeCamp DL, Sprang SR. Structure of a rat α₁-macroglobulin receptor-binding domain dimer. Protein Science : a Publication of the Protein Society. 9: 1889-97. PMID 11106161 DOI: 10.1110/Ps.9.10.1889 |
0.485 |
|
| 2000 |
Tesmer JJ, Dessauer CW, Sunahara RK, Murray LD, Johnson RA, Gilman AG, Sprang SR. Molecular basis for P-site inhibition of adenylyl cyclase. Biochemistry. 39: 14464-71. PMID 11087399 DOI: 10.1021/Bi0015562 |
0.716 |
|
| 1999 |
Xiao T, Towb P, Wasserman SA, Sprang SR. Three-dimensional structure of a complex between the death domains of Pelle and Tube. Cell. 99: 545-55. PMID 10589682 DOI: 10.1016/S0092-8674(00)81542-1 |
0.371 |
|
| 1999 |
Coleman DE, Sprang SR. Reaction dynamics of G-protein catalyzed hydrolysis of GTP as viewed by X-ray crystallographic snapshots of Gi alpha 1. Methods in Enzymology. 308: 70-92. PMID 10507001 DOI: 10.1016/S0076-6879(99)08006-4 |
0.343 |
|
| 1999 |
Tesmer JJ, Sunahara RK, Johnson RA, Gosselin G, Gilman AG, Sprang SR. Two-metal-Ion catalysis in adenylyl cyclase. Science (New York, N.Y.). 285: 756-60. PMID 10427002 DOI: 10.1126/Science.285.5428.756 |
0.712 |
|
| 1999 |
Coleman DE, Sprang SR. Structure of Gialpha1.GppNHp, autoinhibition in a galpha protein-substrate complex. The Journal of Biological Chemistry. 274: 16669-72. PMID 10358003 DOI: 10.1074/Jbc.274.24.16669 |
0.426 |
|
| 1999 |
Dessauer CW, Tesmer JJ, Sprang SR, Gilman AG. The interactions of adenylate cyclases with P-site inhibitors. Trends in Pharmacological Sciences. 20: 205-10. PMID 10354616 DOI: 10.1016/S0165-6147(99)01310-3 |
0.713 |
|
| 1998 |
Tesmer JJ, Sprang SR. The structure, catalytic mechanism and regulation of adenylyl cyclase. Current Opinion in Structural Biology. 8: 713-9. PMID 9914249 DOI: 10.1016/S0959-440X(98)80090-0 |
0.637 |
|
| 1998 |
Sutton RB, Sprang SR. Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+. Structure (London, England : 1993). 6: 1395-405. PMID 9817842 DOI: 10.1016/S0969-2126(98)00139-7 |
0.513 |
|
| 1998 |
Sprang SR, Coleman DE. Invasion of the nucleotide snatchers: structural insights into the mechanism of G protein GEFs. Cell. 95: 155-8. PMID 9790522 DOI: 10.1016/S0092-8674(00)81746-8 |
0.458 |
|
| 1998 |
Coleman DE, Sprang SR. Crystal structures of the G protein Gi alpha 1 complexed with GDP and Mg2+: a crystallographic titration experiment. Biochemistry. 37: 14376-85. PMID 9772163 DOI: 10.1021/Bi9810306 |
0.43 |
|
| 1998 |
Wall MA, Posner BA, Sprang SR. Structural basis of activity and subunit recognition in G protein heterotrimers. Structure (London, England : 1993). 6: 1169-83. PMID 9753695 DOI: 10.1016/S0969-2126(98)00117-8 |
0.483 |
|
| 1998 |
Dessauer CW, Tesmer JJ, Sprang SR, Gilman AG. Identification of a Gialpha binding site on type V adenylyl cyclase. The Journal of Biological Chemistry. 273: 25831-9. PMID 9748257 DOI: 10.1074/Jbc.273.40.25831 |
0.739 |
|
| 1998 |
Posner BA, Mixon MB, Wall MA, Sprang SR, Gilman AG. The A326S mutant of Gialpha1 as an approximation of the receptor-bound state. The Journal of Biological Chemistry. 273: 21752-8. PMID 9705312 DOI: 10.1074/Jbc.273.34.21752 |
0.646 |
|
| 1998 |
Sunahara RK, Beuve A, Tesmer JJ, Sprang SR, Garbers DL, Gilman AG. Exchange of substrate and inhibitor specificities between adenylyl and guanylyl cyclases. The Journal of Biological Chemistry. 273: 16332-8. PMID 9632695 DOI: 10.1074/Jbc.273.26.16332 |
0.726 |
|
| 1998 |
Naismith JH, Sprang SR. Modularity in the TNF-receptor family. Trends in Biochemical Sciences. 23: 74-9. PMID 9538693 DOI: 10.1016/S0968-0004(97)01164-X |
0.57 |
|
| 1998 |
Tesmer JJG, Snahara RK, Gilman AG, Sprang SR. Structural insights into G protein regulation Faseb Journal. 12: A1324. |
0.54 |
|
| 1997 |
Sprang SR. GAP into the breach. Science (New York, N.Y.). 277: 329-30. PMID 9518363 DOI: 10.1126/Science.277.5324.329 |
0.312 |
|
| 1997 |
Sprang SR. G proteins, effectors and GAPs: structure and mechanism. Current Opinion in Structural Biology. 7: 849-56. PMID 9434906 DOI: 10.1016/S0959-440X(97)80157-1 |
0.434 |
|
| 1997 |
Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR. Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS. Science (New York, N.Y.). 278: 1907-16. PMID 9417641 DOI: 10.1126/Science.278.5345.1907 |
0.763 |
|
| 1997 |
Raw AS, Coleman DE, Gilman AG, Sprang SR. Structural and biochemical characterization of the GTPgammaS-, GDP.Pi-, and GDP-bound forms of a GTPase-deficient Gly42 --> Val mutant of Gialpha1. Biochemistry. 36: 15660-9. PMID 9398294 DOI: 10.1021/Bi971912P |
0.642 |
|
| 1997 |
Sunahara RK, Tesmer JJ, Gilman AG, Sprang SR. Crystal structure of the adenylyl cyclase activator Gsalpha. Science (New York, N.Y.). 278: 1943-7. PMID 9395396 DOI: 10.1126/Science.278.5345.1943 |
0.761 |
|
| 1997 |
Sprang SR. G protein mechanisms: insights from structural analysis. Annual Review of Biochemistry. 66: 639-78. PMID 9242920 DOI: 10.1146/Annurev.Biochem.66.1.639 |
0.451 |
|
| 1997 |
Tesmer JJ, Berman DM, Gilman AG, Sprang SR. Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Cell. 89: 251-61. PMID 9108480 DOI: 10.1016/S0092-8674(00)80204-4 |
0.754 |
|
| 1997 |
Sprang SR, Coleman DE, Lee AM, Berghuis MA, Wall MB, Mixon JJG, Tesmer DM, Berman, Posner BA, Gilman AG. Structural insights into g-protein signalling Faseb Journal. 11: A1295. |
0.53 |
|
| 1996 |
Berghuis AM, Lee E, Raw AS, Gilman AG, Sprang SR. Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis. Structure (London, England : 1993). 4: 1277-90. PMID 8939752 DOI: 10.1016/S0969-2126(96)00136-0 |
0.676 |
|
| 1996 |
Naismith JH, Devine TQ, Kohno T, Sprang SR. Structures of the extracellular domain of the type I tumor necrosis factor receptor. Structure (London, England : 1993). 4: 1251-62. PMID 8939750 DOI: 10.1016/S0969-2126(96)00134-7 |
0.606 |
|
| 1996 |
Naismith JH, Brandhuber BJ, Devine TQ, Sprang SR. Seeing double: crystal structures of the type I TNF receptor. Journal of Molecular Recognition : Jmr. 9: 113-7. PMID 8877801 DOI: 10.1002/(Sici)1099-1352(199603)9:2<113::Aid-Jmr253>3.0.Co;2-H |
0.587 |
|
| 1996 |
Sprang SR, Wall MA, Coleman DE, Lee E, Iniguez-Lluhi JA, Posner BA, Gilman AG. The crystallographic structure of a G protein heterotrimer Acta Crystallographica Section a Foundations of Crystallography. 52: C175-C175. DOI: 10.1107/S0108767396092276 |
0.59 |
|
| 1995 |
Naismith JH, Sprang SR. Tumor necrosis factor receptor superfamily. Journal of Inflammation. 47: 1-7. PMID 8913924 |
0.532 |
|
| 1995 |
Sprang SR. How Ras works: structure of a Rap-Raf complex. Structure (London, England : 1993). 3: 641-3. PMID 8591040 DOI: 10.1016/S0969-2126(01)00198-8 |
0.37 |
|
| 1995 |
Wall MA, Coleman DE, Lee E, Iñiguez-Lluhi JA, Posner BA, Gilman AG, Sprang SR. The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Cell. 83: 1047-58. PMID 8521505 DOI: 10.1016/0092-8674(95)90220-1 |
0.589 |
|
| 1995 |
Naismith JH, Devine TQ, Brandhuber BJ, Sprang SR. Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor. The Journal of Biological Chemistry. 270: 13303-7. PMID 7768931 DOI: 10.1074/Jbc.270.22.13303 |
0.599 |
|
| 1995 |
Sutton RB, Davletov BA, Berghuis AM, Südhof TC, Sprang SR. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell. 80: 929-38. PMID 7697723 DOI: 10.1016/0092-8674(95)90296-1 |
0.451 |
|
| 1995 |
Mixon MB, Lee E, Coleman DE, Berghuis AM, Gilman AG, Sprang SR. Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis. Science (New York, N.Y.). 270: 954-60. PMID 7481799 DOI: 10.1126/Science.270.5238.954 |
0.636 |
|
| 1994 |
Rodseth LE, Brandhuber B, Devine TQ, Eck MJ, Hale K, Naismith JH, Sprang SR. Two crystal forms of the extracellular domain of type I tumor necrosis factor receptor. Journal of Molecular Biology. 239: 332-5. PMID 8196061 DOI: 10.1006/Jmbi.1994.1371 |
0.69 |
|
| 1994 |
Coleman DE, Lee E, Mixon MB, Linder ME, Berghuis AM, Gilman AG, Sprang SR. Crystallization and preliminary crystallographic studies of Gi alpha 1 and mutants of Gi alpha 1 in the GTP and GDP-bound states. Journal of Molecular Biology. 238: 630-4. PMID 8176751 DOI: 10.1006/Jmbi.1994.1320 |
0.599 |
|
| 1994 |
Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Science (New York, N.Y.). 265: 1405-12. PMID 8073283 DOI: 10.1126/Science.8073283 |
0.642 |
|
| 1994 |
Kleuss C, Raw AS, Lee E, Sprang SR, Gilman AG. Mechanism of GTP hydrolysis by G-protein alpha subunits. Proceedings of the National Academy of Sciences of the United States of America. 91: 9828-31. PMID 7937899 DOI: 10.1073/Pnas.91.21.9828 |
0.643 |
|
| 1993 |
Blond-Elguindi S, Cwirla SE, Dower WJ, Lipshutz RJ, Sprang SR, Sambrook JF, Gething MJ. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell. 75: 717-28. PMID 7902213 DOI: 10.1016/0092-8674(93)90492-9 |
0.324 |
|
| 1993 |
Sprang SR, Fernando Bazan J. Cytokine structural taxonomy and mechanisms of receptor engagement. Current opinion in structural biology 1993, 3:815-827 Current Opinion in Structural Biology. 3: 815-827. DOI: 10.1016/0959-440X(93)90144-A |
0.359 |
|
| 1992 |
Eck MJ, Ultsch M, Rinderknecht E, de Vos AM, Sprang SR. The structure of human lymphotoxin (tumor necrosis factor-beta) at 1.9-A resolution. The Journal of Biological Chemistry. 267: 2119-22. PMID 1733919 |
0.621 |
|
| 1992 |
Sprang SR, Madsen NB, Withers SG. Multiple phosphate positions in the catalytic site of glycogen phosphorylase: structure of the pyridoxal-5'-pyrophosphate coenzyme-substrate analog. Protein Science : a Publication of the Protein Society. 1: 1100-11. PMID 1304389 DOI: 10.1002/Pro.5560010904 |
0.434 |
|
| 1991 |
Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB. Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate. Science (New York, N.Y.). 254: 1367-71. PMID 1962195 DOI: 10.1126/Science.1962195 |
0.629 |
|
| 1991 |
Zhang JD, Cousens LS, Barr PJ, Sprang SR. Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta. Proceedings of the National Academy of Sciences of the United States of America. 88: 3446-50. PMID 1849658 DOI: 10.1073/Pnas.88.8.3446 |
0.383 |
|
| 1989 |
Goldsmith EJ, Sprang SR, Hamlin R, Xuong NH, Fletterick RJ. Domain separation in the activation of glycogen phosphorylase a. Science (New York, N.Y.). 245: 528-32. PMID 2756432 DOI: 10.1126/Science.2756432 |
0.632 |
|
| 1989 |
Eck MJ, Sprang SR. The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding. The Journal of Biological Chemistry. 264: 17595-605. PMID 2551905 DOI: 10.2210/Pdb1Tnf/Pdb |
0.636 |
|
| 1989 |
Goldsmith EJ, Sprang SR, Fletterick RJ. Alternative binding modes for maltopentaose in the activation site of glycogen phosphorylase a Transactions of the American Crystallographic Association. 25: 87-104. |
0.485 |
|
| 1988 |
Eck MJ, Beutler B, Kuo G, Merryweather JP, Sprang SR. Crystallization of trimeric recombinant human tumor necrosis factor (cachectin). The Journal of Biological Chemistry. 263: 12816-9. PMID 3417634 |
0.531 |
|
| 1988 |
Sprang SR, Acharya KR, Goldsmith EJ, Stuart DI, Varvill K, Fletterick RJ, Madsen NB, Johnson LN. Structural changes in glycogen phosphorylase induced by phosphorylation. Nature. 336: 215-21. PMID 3194008 DOI: 10.1038/336215A0 |
0.636 |
|
| 1988 |
Sprang SR, Fletterick RJ, Gráf L, Rutter WJ, Craik CS. Studies of specificity and catalysis in trypsin by structural analysis of site-directed mutants. Critical Reviews in Biotechnology. 8: 225-36. PMID 3063392 DOI: 10.1107/S0108767387085143 |
0.579 |
|
| 1987 |
Sprang S, Goldsmith E, Fletterick R. Structure of the nucleotide activation switch in glycogen phosphorylase a. Science (New York, N.Y.). 237: 1012-9. PMID 3616621 DOI: 10.1126/Science.3616621 |
0.608 |
|
| 1987 |
Craik CS, Roczniak S, Sprang S, Fletterick R, Rutter W. Redesigning trypsin via genetic engineering. Journal of Cellular Biochemistry. 33: 199-211. PMID 3553217 DOI: 10.1002/Jcb.240330307 |
0.435 |
|
| 1987 |
Rath VL, Newgard CB, Sprang SR, Goldsmith EJ, Fletterick RJ. Modeling the biochemical differences between rabbit muscle and human liver phosphorylase. Proteins. 2: 225-35. PMID 3447179 DOI: 10.1002/Prot.340020307 |
0.51 |
|
| 1987 |
Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik CS. The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis. Science (New York, N.Y.). 237: 905-9. PMID 3112942 DOI: 10.1126/Science.3112942 |
0.586 |
|
| 1982 |
Withers SG, Madsen NB, Sprang SR, Fletterick RJ. Catalytic site of glycogen phosphorylase: structural changes during activation and mechanistic implications. Biochemistry. 21: 5372-82. PMID 7171564 DOI: 10.1021/Bi00264A039 |
0.582 |
|
| 1982 |
Craik CS, Sprang S, Fletterick R, Rutter WJ. Intron-exon splice junctions map at protein surfaces. Nature. 299: 180-2. PMID 7110339 DOI: 10.1038/299180A0 |
0.522 |
|
| 1982 |
Sprang S, Fletterick R, Stern M, Yang D, Madsen N, Sturtevant J. Analysis of an allosteric binding site: the nucleoside inhibitor site of phosphorylase alpha Biochemistry. 21: 2036-2048. PMID 7093228 DOI: 10.1021/Bi00538A010 |
0.585 |
|
| 1982 |
Goldsmith E, Sprang S, Fletterick R. Structure of maltoheptaose by difference Fourier methods and a model for glycogen. Journal of Molecular Biology. 156: 411-27. PMID 7086906 DOI: 10.1016/0022-2836(82)90336-9 |
0.558 |
|
| 1982 |
Sprang SR, Goldsmith EJ, Fletterick RJ, Withers SG, Madsen NB. Catalytic site of glycogen phosphorylase: structure of the T state and specificity for alpha-D-glucose. Biochemistry. 21: 5364-71. PMID 6816272 DOI: 10.1021/Bi00264A038 |
0.562 |
|
| 1982 |
Fletterick RJ, Sprang SR. Glycogen phosphorylase structures and function Accounts of Chemical Research. 15: 361-369. DOI: 10.1021/Ar00083A004 |
0.528 |
|
| 1981 |
Sprang S, Fletterick RJ. Subunit interactions and the allosteric response in phosphorylase. Biophysical Journal. 32: 175-92. PMID 6788104 DOI: 10.1016/S0006-3495(80)84932-0 |
0.533 |
|
| 1981 |
Goldsmith E, Sprang S, Fletterick RJ. Maltoheptaose binding to phosphorylaseaat 0.25 nm resolution Acta Crystallographica Section a Foundations of Crystallography. 37: C34-C34. DOI: 10.1107/S0108767381098577 |
0.52 |
|
| 1981 |
Sprang SR, Fletterick RJ. X-ray studies of activation/catalysis in glycogen phosphorylasea Acta Crystallographica Section a Foundations of Crystallography. 37: C35-C35. DOI: 10.1107/S0108767381098565 |
0.407 |
|
| 1980 |
Sprang S, Fletterick RJ. The structure of glycogen phosphorylase alpha at 2.5 A resolution. Journal of Molecular Biology. 131: 523-51. PMID 513128 DOI: 10.1016/0022-2836(79)90006-8 |
0.53 |
|
| 1979 |
Fletterick RJ, Sprang S, Madsen NB. Analysis of the surface topography of glycogen phosphorylase a: implications for metabolic interconversion and regulatory mechanisms. Canadian Journal of Biochemistry. 57: 789-97. PMID 476522 DOI: 10.1139/O79-098 |
0.543 |
|
| 1979 |
Sprang S, Yang D, Fletterick RJ. Solvent accessibility properties of complex proteins. Nature. 280: 333-5. PMID 460408 DOI: 10.1038/280333A0 |
0.532 |
|
| 1978 |
Sprang S, Rohrer DC, Sundaralingam M. The crystal structure and conformation of 2',3'-O-isopropylideneadenosine: the co-existence of a planar and a puckered ribofuranose ring Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 34: 2803-2810. DOI: 10.1107/S0567740878009279 |
0.47 |
|
| 1978 |
Sprang S, Scheller R, Rohrer D, Sundaralingam M. Conformational analysis of 8-azanucleosides. Crystal and molecular structure of 8-azatubercidin monohydrate, a nucleoside analog exhibiting the "high anti" conformation Journal of the American Chemical Society. 100: 2867-2872. DOI: 10.1021/ja00477a049 |
0.502 |
|
| 1978 |
SPRANG S, SCHELLER R, ROHRER D, SUNDARALINGAM M. ChemInform Abstract: CONFORMATIONAL ANALYSIS OF 8-AZANUCLEOSIDES. CRYSTAL AND MOLECULAR STRUCTURE OF 8-AZATUBERCIDIN MONOHYDRATE, A NUCLEOSIDE ANALOG EXHIBITING THE ′HIGH ANTI′ CONFORMATION Chemischer Informationsdienst. 9. DOI: 10.1002/chin.197833069 |
0.509 |
|
| 1973 |
Sprang S, Sundaralingam M. Crystal structure of 2-chloro-1-(β-D-ribofuranosyl)benzimidazole. Hydrogen bonding to the furanose ring oxygen Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry. 29: 1910-1916. DOI: 10.1107/S0567740873005741 |
0.425 |
|
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