Year |
Citation |
Score |
2019 |
Cash JN, Sharma PV, Tesmer JJ. Structural and biochemical characterization of the pleckstrin homology domain of the RhoGEF P-Rex2 and its regulation by PIP3 Journal of Structural Biology: X. 1: 100001. DOI: 10.1016/j.yjsbx.2018.100001 |
0.328 |
|
2017 |
Bouley R, Waldschmidt HV, Cato MC, Cannavo A, Song J, Cheung JY, Yao XQ, Koch WJ, Larsen SD, Tesmer JJ. Structural Determinants Influencing the Potency and Selectivity of Indazole-Paroxetine Hybrid G Protein-Coupled Receptor Kinase 2 Inhibitors. Molecular Pharmacology. PMID 29070696 DOI: 10.1124/mol.117.110130 |
0.37 |
|
2016 |
Cash JN, Davis EM, Tesmer JJ. Structural and Biochemical Characterization of the Catalytic Core of the Metastatic Factor P-Rex1 and Its Regulation by PtdIns(3,4,5)P3. Structure (London, England : 1993). PMID 27150042 DOI: 10.1016/j.str.2016.02.022 |
0.321 |
|
2016 |
Tesmer JJ. Hitchhiking on the heptahelical highway: structure and function of 7TM receptor complexes. Nature Reviews. Molecular Cell Biology. PMID 27093944 DOI: 10.1038/nrm.2016.36 |
0.388 |
|
2016 |
Yang P, Homan KT, Li Y, Cruz-Rodriguez O, Tesmer JJ, Chen Z. Effect of Lipid Composition on Membrane Orientation of the G protein-coupled Receptor Kinase 2-Gβ1γ2 Complex. Biochemistry. PMID 27088923 DOI: 10.1021/Acs.Biochem.6B00354 |
0.346 |
|
2016 |
Waldschmidt HV, Homan KT, Cruz-Rodriguez O, Cato MC, Waninger-Saroni J, Larimore KM, Cannavo A, Song J, Cheung JY, Kirchhoff PD, Koch WJ, Tesmer JJ, Larsen SD. Structure-Based Design, Synthesis and Biological Evaluation of Highly Selective and Potent G Protein-Coupled Receptor Kinase 2 Inhibitors. Journal of Medicinal Chemistry. PMID 27050625 DOI: 10.1021/Acs.Jmedchem.5B02000 |
0.301 |
|
2016 |
Taylor VG, Bommarito PA, Tesmer JJ. Structure of the Regulator of G Protein Signaling 8 (RGS8)-Gαq Complex: Molecular Basis for Gα Selectivity. The Journal of Biological Chemistry. PMID 26755720 DOI: 10.1074/jbc.M115.712075 |
0.377 |
|
2016 |
Taylor VG, Bommarito PA, Tesmer JJ. Structure of the Regulator of G Protein Signaling 8 (RGS8)-G alpha q Complex: MOLECULAR BASIS FOR G alpha SELECTIVITY. Journal of Biological Chemistry. 291: 5138-5145. DOI: 10.2210/Pdb5Do9/Pdb |
0.384 |
|
2015 |
Inagaki S, Ghirlando R, Vishnivetskiy SA, Homan KT, White JF, Tesmer JJ, Gurevich VV, Grisshammer R. G Protein-Coupled Receptor Kinase 2 (GRK2) and 5 (GRK5) Exhibit Selective Phosphorylation of the Neurotensin Receptor in Vitro. Biochemistry. 54: 4320-9. PMID 26120872 DOI: 10.1021/Acs.Biochem.5B00285 |
0.328 |
|
2015 |
Homan KT, Waldschmidt HV, Glukhova A, Cannavo A, Song J, Cheung JY, Koch WJ, Larsen SD, Tesmer JJ. Crystal Structure of G Protein-Coupled Receptor Kinase 5 in Complex with a Rationally Designed Inhibitor. The Journal of Biological Chemistry. PMID 26032411 DOI: 10.1074/Jbc.M115.647370 |
0.47 |
|
2015 |
Azevedo AW, Doan T, Moaven H, Sokal I, Baameur F, Vishnivetskiy SA, Homan KT, Tesmer JJ, Gurevich VV, Chen J, Rieke F. C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor. Elife. 4. PMID 25910054 DOI: 10.7554/Elife.05981 |
0.378 |
|
2015 |
Li L, Homan KT, Vishnivetskiy SA, Manglik A, Tesmer JJ, Gurevich VV, Gurevich EV. G Protein-coupled Receptor Kinases of the GRK4 Protein Subfamily Phosphorylate Inactive G Protein-coupled Receptors (GPCRs). The Journal of Biological Chemistry. 290: 10775-90. PMID 25770216 DOI: 10.1074/Jbc.M115.644773 |
0.328 |
|
2015 |
Homan KT, Tesmer JJ. Molecular basis for small molecule inhibition of G protein-coupled receptor kinases. Acs Chemical Biology. 10: 246-56. PMID 24984143 DOI: 10.1021/Cb5003976 |
0.336 |
|
2015 |
Azevedo AW, Doan T, Moaven H, Sokal I, Baameur F, Vishnivetskiy SA, Homan KT, Tesmer JJ, Gurevich VV, Chen J, Rieke F. Author response: C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor Elife. DOI: 10.7554/Elife.05981.018 |
0.32 |
|
2014 |
Lyon AM, Begley JA, Manett TD, Tesmer JJ. Molecular mechanisms of phospholipase C β3 autoinhibition. Structure (London, England : 1993). 22: 1844-54. PMID 25435326 DOI: 10.1016/j.str.2014.10.008 |
0.754 |
|
2014 |
Beautrait A, Michalski KR, Lopez TS, Mannix KM, McDonald DJ, Cutter AR, Medina CB, Hebert AM, Francis CJ, Bouvier M, Tesmer JJ, Sterne-Marr R. Mapping the putative G protein-coupled receptor (GPCR) docking site on GPCR kinase 2: insights from intact cell phosphorylation and recruitment assays. The Journal of Biological Chemistry. 289: 25262-75. PMID 25049229 DOI: 10.1074/Jbc.M114.593178 |
0.366 |
|
2014 |
Swanson CJ, Ritt M, Wang W, Lang MJ, Narayan A, Tesmer JJ, Westfall M, Sivaramakrishnan S. Conserved modular domains team up to latch-open active protein kinase Cα. The Journal of Biological Chemistry. 289: 17812-29. PMID 24790081 DOI: 10.1074/Jbc.M113.534750 |
0.497 |
|
2014 |
Homan KT, Tesmer JJ. Structural insights into G protein-coupled receptor kinase function. Current Opinion in Cell Biology. 27: 25-31. PMID 24680427 DOI: 10.1016/J.Ceb.2013.10.009 |
0.4 |
|
2014 |
Ding B, Glukhova A, Sobczyk-Kojiro K, Mosberg HI, Tesmer JJ, Chen Z. Unveiling the membrane-binding properties of N-terminal and C-terminal regions of G protein-coupled receptor kinase 5 by combined optical spectroscopies. Langmuir : the Acs Journal of Surfaces and Colloids. 30: 823-31. PMID 24401145 DOI: 10.1021/La404055A |
0.325 |
|
2014 |
Lyon AM, Taylor VG, Tesmer JJ. Strike a pose: Gαq complexes at the membrane. Trends in Pharmacological Sciences. 35: 23-30. PMID 24287282 DOI: 10.1016/j.tips.2013.10.008 |
0.743 |
|
2014 |
Homan KT, Wu E, Wilson MW, Singh P, Larsen SD, Tesmer JJ. Structural and functional analysis of g protein-coupled receptor kinase inhibition by paroxetine and a rationally designed analog. Molecular Pharmacology. 85: 237-48. PMID 24220010 DOI: 10.1124/Mol.113.089631 |
0.33 |
|
2014 |
Swanson CJ, Ritt M, Wang W, Lang M, Tesmer JJ, Westfall M, Sivaramakrishnan S. Non-Canonical Modular Domain Interactions Dictate PKCα Function Biophysical Journal. 106: 467. DOI: 10.1016/J.Bpj.2013.11.2643 |
0.514 |
|
2013 |
Lyon AM, Tesmer JJ. Structural insights into phospholipase C-β function. Molecular Pharmacology. 84: 488-500. PMID 23880553 DOI: 10.1124/mol.113.087403 |
0.764 |
|
2013 |
Vishnivetskiy SA, Ostermaier MK, Singhal A, Panneels V, Homan KT, Glukhova A, Sligar SG, Tesmer JJ, Schertler GF, Standfuss J, Gurevich VV. Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding. Cellular Signalling. 25: 2155-62. PMID 23872075 DOI: 10.1016/J.Cellsig.2013.07.009 |
0.305 |
|
2013 |
Nance MR, Kreutz B, Tesmer VM, Sterne-Marr R, Kozasa T, Tesmer JJ. Structural and functional analysis of the regulator of G protein signaling 2-gαq complex. Structure (London, England : 1993). 21: 438-48. PMID 23434405 DOI: 10.1016/J.Str.2012.12.016 |
0.426 |
|
2013 |
Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. Nature Structural & Molecular Biology. 20: 355-62. PMID 23377541 DOI: 10.1038/Nsmb.2497 |
0.766 |
|
2012 |
Thal DM, Homan KT, Chen J, Wu EK, Hinkle PM, Huang ZM, Chuprun JK, Song J, Gao E, Cheung JY, Sklar LA, Koch WJ, Tesmer JJ. Paroxetine is a direct inhibitor of g protein-coupled receptor kinase 2 and increases myocardial contractility. Acs Chemical Biology. 7: 1830-9. PMID 22882301 DOI: 10.1021/Cb3003013 |
0.363 |
|
2012 |
Tesmer VM, Lennarz S, Mayer G, Tesmer JJ. Molecular mechanism for inhibition of g protein-coupled receptor kinase 2 by a selective RNA aptamer. Structure (London, England : 1993). 20: 1300-9. PMID 22727813 DOI: 10.1016/J.Str.2012.05.002 |
0.34 |
|
2012 |
Tesmer JJ, Nance MR, Singh P, Lee H. Structure of a monomeric variant of rhodopsin kinase at 2.5 Å resolution. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68: 622-5. PMID 22684056 DOI: 10.1107/S1744309112017435 |
0.461 |
|
2012 |
Orban T, Huang CC, Homan KT, Jastrzebska B, Tesmer JJ, Palczewski K. Substrate-induced changes in the dynamics of rhodopsin kinase (G protein-coupled receptor kinase 1). Biochemistry. 51: 3404-11. PMID 22480180 DOI: 10.1021/Bi300295Y |
0.398 |
|
2012 |
Gurevich EV, Tesmer JJ, Mushegian A, Gurevich VV. G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharmacology & Therapeutics. 133: 40-69. PMID 21903131 DOI: 10.1016/J.Pharmthera.2011.08.001 |
0.398 |
|
2011 |
Boughton AP, Yang P, Tesmer VM, Ding B, Tesmer JJ, Chen Z. Heterotrimeric G protein beta1gamma2 subunits change orientation upon complex formation with G protein-coupled receptor kinase 2 (GRK2) on a model membrane. Proceedings of the National Academy of Sciences of the United States of America. 108: E667-73. PMID 21876134 DOI: 10.1073/Pnas.1108236108 |
0.365 |
|
2011 |
Aittaleb M, Nishimura A, Linder ME, Tesmer JJ. Plasma membrane association of p63 Rho guanine nucleotide exchange factor (p63RhoGEF) is mediated by palmitoylation and is required for basal activity in cells. The Journal of Biological Chemistry. 286: 34448-56. PMID 21832057 DOI: 10.1074/jbc.M111.273342 |
0.358 |
|
2011 |
Lyon AM, Tesmer VM, Dhamsania VD, Thal DM, Gutierrez J, Chowdhury S, Suddala KC, Northup JK, Tesmer JJ. An autoinhibitory helix in the C-terminal region of phospholipase C-β mediates Gαq activation. Nature Structural & Molecular Biology. 18: 999-1005. PMID 21822282 DOI: 10.1038/Nsmb.2095 |
0.757 |
|
2011 |
Thal DM, Yeow RY, Schoenau C, Huber J, Tesmer JJ. Molecular mechanism of selectivity among G protein-coupled receptor kinase 2 inhibitors. Molecular Pharmacology. 80: 294-303. PMID 21596927 DOI: 10.1124/mol.111.071522 |
0.358 |
|
2011 |
Huang CC, Orban T, Jastrzebska B, Palczewski K, Tesmer JJ. Activation of G protein-coupled receptor kinase 1 involves interactions between its N-terminal region and its kinase domain. Biochemistry. 50: 1940-9. PMID 21265573 DOI: 10.1021/Bi101606E |
0.412 |
|
2011 |
Huang CC, Tesmer JJ. Recognition in the face of diversity: interactions of heterotrimeric G proteins and G protein-coupled receptor (GPCR) kinases with activated GPCRs. The Journal of Biological Chemistry. 286: 7715-21. PMID 21199869 DOI: 10.1074/jbc.R109.051847 |
0.322 |
|
2011 |
Bayburt TH, Vishnivetskiy SA, McLean MA, Morizumi T, Huang CC, Tesmer JJ, Ernst OP, Sligar SG, Gurevich VV. Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. The Journal of Biological Chemistry. 286: 1420-8. PMID 20966068 DOI: 10.1074/Jbc.M110.151043 |
0.352 |
|
2010 |
Boguth CA, Singh P, Huang CC, Tesmer JJ. Molecular basis for activation of G protein-coupled receptor kinases. The Embo Journal. 29: 3249-59. PMID 20729810 DOI: 10.1038/Emboj.2010.206 |
0.426 |
|
2010 |
Shankaranarayanan A, Boguth CA, Lutz S, Vettel C, Uhlemann F, Aittaleb M, Wieland T, Tesmer JJ. Galpha q allosterically activates and relieves autoinhibition of p63RhoGEF. Cellular Signalling. 22: 1114-23. PMID 20214977 DOI: 10.1016/j.cellsig.2010.03.006 |
0.326 |
|
2010 |
Tesmer JJ, Tesmer VM, Lodowski DT, Steinhagen H, Huber J. Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol. Journal of Medicinal Chemistry. 53: 1867-70. PMID 20128603 DOI: 10.1021/Jm9017515 |
0.688 |
|
2010 |
Talbot JN, Roman DL, Clark MJ, Roof RA, Tesmer JJ, Neubig RR, Traynor JR. Differential modulation of mu-opioid receptor signaling to adenylyl cyclase by regulators of G protein signaling proteins 4 or 8 and 7 in permeabilised C6 cells is Galpha subtype dependent. Journal of Neurochemistry. 112: 1026-34. PMID 20002516 DOI: 10.1111/J.1471-4159.2009.06519.X |
0.339 |
|
2010 |
Aittaleb M, Boguth CA, Tesmer JJ. Structure and function of heterotrimeric G protein-regulated Rho guanine nucleotide exchange factors. Molecular Pharmacology. 77: 111-25. PMID 19880753 DOI: 10.1124/mol.109.061234 |
0.38 |
|
2009 |
Tesmer JJ. Structure and function of regulator of G protein signaling homology domains. Progress in Molecular Biology and Translational Science. 86: 75-113. PMID 20374714 DOI: 10.1016/S1877-1173(09)86004-3 |
0.407 |
|
2009 |
Aittaleb M, Gao G, Evelyn CR, Neubig RR, Tesmer JJ. A conserved hydrophobic surface of the LARG pleckstrin homology domain is critical for RhoA activation in cells. Cellular Signalling. 21: 1569-78. PMID 19560536 DOI: 10.1016/j.cellsig.2009.06.003 |
0.446 |
|
2009 |
Huang CC, Yoshino-Koh K, Tesmer JJ. A surface of the kinase domain critical for the allosteric activation of G protein-coupled receptor kinases. The Journal of Biological Chemistry. 284: 17206-15. PMID 19364770 DOI: 10.1074/jbc.M809544200 |
0.361 |
|
2009 |
Sterne-Marr R, Leahey PA, Bresee JE, Dickson HM, Ho W, Ragusa MJ, Donnelly RM, Amie SM, Krywy JA, Brookins-Danz ED, Orakwue SC, Carr MJ, Yoshino-Koh K, Li Q, Tesmer JJ. GRK2 activation by receptors: role of the kinase large lobe and carboxyl-terminal tail. Biochemistry. 48: 4285-93. PMID 19338266 DOI: 10.1021/Bi900151G |
0.423 |
|
2008 |
Shankaranarayanan A, Thal DM, Tesmer VM, Roman DL, Neubig RR, Kozasa T, Tesmer JJ. Assembly of high order G alpha q-effector complexes with RGS proteins. The Journal of Biological Chemistry. 283: 34923-34. PMID 18936096 DOI: 10.1074/Jbc.M805860200 |
0.346 |
|
2008 |
Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ. Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation. The Journal of Biological Chemistry. 283: 14053-62. PMID 18339619 DOI: 10.1074/Jbc.M708974200 |
0.435 |
|
2007 |
Lutz S, Shankaranarayanan A, Coco C, Ridilla M, Nance MR, Vettel C, Baltus D, Evelyn CR, Neubig RR, Wieland T, Tesmer JJ. Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs. Science (New York, N.Y.). 318: 1923-7. PMID 18096806 DOI: 10.1126/Science.1147554 |
0.555 |
|
2007 |
Gu S, He J, Ho WT, Ramineni S, Thal DM, Natesh R, Tesmer JJ, Hepler JR, Heximer SP. Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members. The Journal of Biological Chemistry. 282: 33064-75. PMID 17848575 DOI: 10.1074/Jbc.M702685200 |
0.368 |
|
2007 |
Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ. Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain. Journal of Molecular Biology. 365: 1446-59. PMID 17134719 DOI: 10.1016/J.Jmb.2006.10.075 |
0.399 |
|
2006 |
Lodowski DT, Tesmer VM, Benovic JL, Tesmer JJ. The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs. The Journal of Biological Chemistry. 281: 16785-93. PMID 16613860 DOI: 10.1074/Jbc.M601327200 |
0.754 |
|
2005 |
Tesmer VM, Kawano T, Shankaranarayanan A, Kozasa T, Tesmer JJ. Snapshot of activated G proteins at the membrane: the Galphaq-GRK2-Gbetagamma complex. Science (New York, N.Y.). 310: 1686-90. PMID 16339447 DOI: 10.1126/Science.1118890 |
0.435 |
|
2005 |
Lodowski DT, Barnhill JF, Pyskadlo RM, Ghirlando R, Sterne-Marr R, Tesmer JJ. The role of G beta gamma and domain interfaces in the activation of G protein-coupled receptor kinase 2. Biochemistry. 44: 6958-70. PMID 15865441 DOI: 10.1021/Bi050119Q |
0.76 |
|
2004 |
Sterne-Marr R, Dhami GK, Tesmer JJ, Ferguson SS. Characterization of GRK2 RH domain-dependent regulation of GPCR coupling to heterotrimeric G proteins. Methods in Enzymology. 390: 310-36. PMID 15488186 DOI: 10.1016/S0076-6879(04)90020-1 |
0.435 |
|
2004 |
Day PW, Tesmer JJ, Sterne-Marr R, Freeman LC, Benovic JL, Wedegaertner PB. Characterization of the GRK2 binding site of Galphaq. The Journal of Biological Chemistry. 279: 53643-52. PMID 15471870 DOI: 10.1074/jbc.M401438200 |
0.345 |
|
2004 |
Kristelly R, Gao G, Tesmer JJ. Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor. The Journal of Biological Chemistry. 279: 47352-62. PMID 15331592 DOI: 10.1074/Jbc.M406056200 |
0.746 |
|
2003 |
Kristelly R, Earnest BT, Krishnamoorthy L, Tesmer JJ. Preliminary structure analysis of the DH/PH domains of leukemia-associated RhoGEF. Acta Crystallographica. Section D, Biological Crystallography. 59: 1859-62. PMID 14501138 DOI: 10.1107/S0907444903018067 |
0.744 |
|
2003 |
Lodowski DT, Barnhill JF, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ. Purification, crystallization and preliminary X-ray diffraction studies of a complex between G protein-coupled receptor kinase 2 and Gbeta1gamma2. Acta Crystallographica. Section D, Biological Crystallography. 59: 936-9. PMID 12777817 DOI: 10.1107/S0907444903002622 |
0.732 |
|
2003 |
Lodowski DT, Pitcher JA, Capel WD, Lefkowitz RJ, Tesmer JJ. Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma. Science (New York, N.Y.). 300: 1256-62. PMID 12764189 DOI: 10.1126/Science.1082348 |
0.74 |
|
2003 |
Sterne-Marr R, Tesmer JJ, Day PW, Stracquatanio RP, Cilente JA, O'Connor KE, Pronin AN, Benovic JL, Wedegaertner PB. G protein-coupled receptor Kinase 2/G alpha q/11 interaction. A novel surface on a regulator of G protein signaling homology domain for binding G alpha subunits. The Journal of Biological Chemistry. 278: 6050-8. PMID 12427730 DOI: 10.1074/jbc.M208787200 |
0.36 |
|
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 |
0.593 |
|
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 |
0.571 |
|
1999 |
Pitcher JA, Tesmer JJ, Freeman JL, Capel WD, Stone WC, Lefkowitz RJ. Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases. The Journal of Biological Chemistry. 274: 34531-4. PMID 10574913 DOI: 10.1074/Jbc.274.49.34531 |
0.349 |
|
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 |
0.584 |
|
1999 |
Posner BA, Mukhopadhyay S, Tesmer JJ, Gilman AG, Ross EM. Modulation of the affinity and selectivity of RGS protein interaction with G alpha subunits by a conserved asparagine/serine residue. Biochemistry. 38: 7773-9. PMID 10387017 DOI: 10.1021/Bi9906367 |
0.402 |
|
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 |
0.57 |
|
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 |
0.609 |
|
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 |
0.623 |
|
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 |
0.608 |
|
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 |
0.66 |
|
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 |
0.642 |
|
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 |
0.63 |
|
1996 |
Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nature Structural Biology. 3: 74-86. PMID 8548458 DOI: 10.1038/Nsb0196-74 |
0.598 |
|
1994 |
Tesmer JJ, Stemmler TL, Penner-Hahn JE, Davisson VJ, Smith JL. Preliminary X-ray analysis of Escherichia coli GMP synthetase: determination of anomalous scattering factors for a cysteinyl mercury derivative. Proteins. 18: 394-403. PMID 8208731 DOI: 10.1002/Prot.340180410 |
0.493 |
|
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