Stephen R. Sprang, Ph.D. - Publications

Affiliations: 
Biological Science University of Montana, Missoula, MT 
Area:
Structural Biology and Biochemistry: Biological Signal Transduction
Website:
http://www.cas.umt.edu/casweb/faculty/FacultyDetails.cfm?id=941

115 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
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  0.36
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  0.36
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  0.48
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  0.36
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  0.36
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  0.96
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  0.96
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  0.96
2013 Sprang SR. An acid test for g proteins. Molecular Cell. 51: 405-6. PMID 23973370 DOI: 10.1016/J.Molcel.2013.08.012  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
2011 Sprang SR. Cell signalling: Binding the receptor at both ends. Nature. 469: 172-3. PMID 21228868 DOI: 10.1038/469172A  0.96
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  0.96
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  0.96
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  0.96
2010 Sprang SR. Structures of heterotrimeric g proteins and their complexes Handbook of Cell Signaling, 2/E. 1: 119-128. DOI: 10.1016/B978-0-12-374145-5.00019-X  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
2008 Du X, Ferguson K, Gregory R, Sprang SR. A method to determine 18 O kinetic isotope effects in the hydrolysis of nucleotide triphosphates. Analytical Biochemistry. 372: 213-21. PMID 17963711 DOI: 10.1016/J.Ab.2007.09.013  0.96
2007 Sprang SR. Structural biology: a receptor unlocked. Nature. 450: 355-6. PMID 18004367 DOI: 10.1038/450355A  0.96
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  0.96
2007 Sprang S. Preface Advances in Protein Chemistry. 74: VII-X. DOI: 10.1016/S0065-3233(07)74009-3  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
2004 Minna JD, Gazdar AF, Sprang SR, Herz J. Cancer. A bull's eye for targeted lung cancer therapy. Science (New York, N.Y.). 304: 1458-61. PMID 15178790 DOI: 10.1126/Science.1099578  0.96
2004 Du X, Black GE, Lecchi P, Abramson FP, Sprang SR. Kinetic isotope effects in Ras-catalyzed GTP hydrolysis: evidence for a loose transition state. Proceedings of the National Academy of Sciences of the United States of America. 101: 8858-63. PMID 15178760 DOI: 10.1073/Pnas.0401675101  0.96
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  0.96
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  0.96
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  0.96
2003 Sprang SR. Structure and Function of Tumor Necrosis Factor at the Cell Surface Handbook of Cell Signaling. 1: 275-280. DOI: 10.1016/B978-012124546-7/50408-3  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.72
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
1998 Tesmer JJG, Snahara RK, Gilman AG, Sprang SR. Structural insights into G protein regulation Faseb Journal. 12: A1324.  0.96
1997 Sprang SR. GAP into the breach. Science (New York, N.Y.). 277: 329-30. PMID 9518363 DOI: 10.1126/Science.277.5324.329  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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.  0.96
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  0.96
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  0.96
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  0.96
1996 Coleman DE, Sprang SR. How G proteins work: a continuing story. Trends in Biochemical Sciences. 21: 41-4. PMID 8851656 DOI: 10.1016/S0968-0004(96)80176-9  0.96
1995 Naismith JH, Sprang SR. Tumor necrosis factor receptor superfamily. Journal of Inflammation. 47: 1-7. PMID 8913924  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
1993 Sprang SR. On a (beta-) roll. Trends in Biochemical Sciences. 18: 313-4. PMID 8236448 DOI: 10.1016/0968-0004(93)90061-Q  0.96
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  0.96
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  0.96
1992 Sprang SR. The latent tendencies of PAI-1. Trends in Biochemical Sciences. 17: 49-50. PMID 1566324 DOI: 10.1016/0968-0004(92)90495-U  0.96
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  0.96
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  0.96
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  0.96
1990 Sprang SR. The divergent receptors for TNF. Trends in Biochemical Sciences. 15: 366-8. PMID 2174582 DOI: 10.1016/0968-0004(90)90228-4  0.96
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  0.96
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  0.96
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.  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
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  0.96
1982 Fletterick RJ, Sprang SR. Glycogen phosphorylase structures and function Accounts of Chemical Research. 15: 361-369. DOI: 10.1021/Ar00083A004  0.96
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  0.36
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  0.48
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  0.96
1970 Yen TF, Sprang SR. ESR g-values of bituminous materials Preprints. 15: A65-A76.  0.96
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