Thomas J. Baranski - Publications

Affiliations: 
Biology & Biomedical Sciences (Molecular Cell Biology) Washington University, Saint Louis, St. Louis, MO 
Area:
Cell Biology, Molecular Biology

37 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 Lin AJ, Baranski T, Chaterjee D, Chapman W, Foltz G, Kim H. Androgen-receptor-positive hepatocellular carcinoma in a transgender teenager taking exogenous testosterone. Lancet (London, England). 396: 198. PMID 32682485 DOI: 10.1016/S0140-6736(20)31538-5  0.342
2013 Nichols AS, Floyd DH, Bruinsma SP, Narzinski K, Baranski TJ. Frizzled receptors signal through G proteins. Cellular Signalling. 25: 1468-75. PMID 23524329 DOI: 10.1016/J.Cellsig.2013.03.009  0.696
2012 Nikiforovich GV, Baranski TJ. Structural mechanisms of constitutive activation in the C5a receptors with mutations in the extracellular loops: molecular modeling study. Proteins. 80: 71-80. PMID 21960464 DOI: 10.1002/Prot.23162  0.439
2011 Nikiforovich GV, Taylor CM, Marshall GR, Baranski TJ. Difference between restoring and predicting 3D structures of the loops in G-protein-coupled receptors by molecular modeling. Proceedings of the National Academy of Sciences of the United States of America. 108: E341; author reply E. PMID 21724986 DOI: 10.1073/Pnas.1107702108  0.411
2011 Nikiforovich GV, Marshall GR, Baranski TJ. Simplified modeling approach suggests structural mechanisms for constitutive activation of the C5a receptor. Proteins. 79: 787-802. PMID 21287612 DOI: 10.1002/Prot.22918  0.428
2010 Nikiforovich GV, Baranski TJ. Computational modeling of constitutively active mutants of GPCRs C5a receptor. Methods in Enzymology. 485: 369-91. PMID 21050928 DOI: 10.1016/B978-0-12-381296-4.00021-X  0.461
2010 Van Eps N, Anderson LL, Kisselev OG, Baranski TJ, Hubbell WL, Marshall GR. Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein alpha subunit. Biochemistry. 49: 6877-86. PMID 20695526 DOI: 10.1021/Bi100846C  0.306
2010 Rana S, Baranski TJ. Third extracellular loop (EC3)-N terminus interaction is important for seven-transmembrane domain receptor function: implications for an activation microswitch region. The Journal of Biological Chemistry. 285: 31472-83. PMID 20663868 DOI: 10.1074/Jbc.M110.129213  0.537
2010 Nikiforovich GV, Taylor CM, Marshall GR, Baranski TJ. Modeling the possible conformations of the extracellular loops in G-protein-coupled receptors. Proteins. 78: 271-85. PMID 19731375 DOI: 10.1002/Prot.22537  0.476
2009 Nikiforovich GV, Baranski TJ. Structural models for the complex of chemotaxis inhibitory protein of Staphylococcus aureus with the C5a receptor. Biochemical and Biophysical Research Communications. 390: 481-4. PMID 19799858 DOI: 10.1016/J.Bbrc.2009.09.113  0.398
2009 Klco JM, Sen S, Hansen JL, Lyngsø C, Nikiforovich GV, Sheikh SP, Baranski TJ. Complement factor 5a receptor chimeras reveal the importance of lipid-facing residues in transport competence. The Febs Journal. 276: 2786-800. PMID 19459935 DOI: 10.1111/J.1742-4658.2009.07002.X  0.682
2008 Nikiforovich GV, Marshall GR, Baranski TJ. Modeling molecular mechanisms of binding of the anaphylatoxin C5a to the C5a receptor. Biochemistry. 47: 3117-30. PMID 18275159 DOI: 10.1021/Bi702321A  0.458
2008 Sen S, Baranski TJ, Nikiforovich GV. Conformational movement of F251 contributes to the molecular mechanism of constitutive activation in the C5a receptor. Chemical Biology & Drug Design. 71: 197-204. PMID 18248350 DOI: 10.1111/J.1747-0285.2008.00630.X  0.482
2008 Hagemann IS, Miller DL, Klco JM, Nikiforovich GV, Baranski TJ. Structure of the complement factor 5a receptor-ligand complex studied by disulfide trapping and molecular modeling. The Journal of Biological Chemistry. 283: 7763-75. PMID 18195008 DOI: 10.1074/Jbc.M709467200  0.775
2007 Bruinsma SP, Baranski TJ. Beta2-chimaerin in cancer signaling: connecting cell adhesion and MAP kinase activation. Cell Cycle (Georgetown, Tex.). 6: 2440-4. PMID 17726379 DOI: 10.4161/Cc.6.20.4786  0.728
2007 Bruinsma SP, Cagan RL, Baranski TJ. Chimaerin and Rac regulate cell number, adherens junctions, and ERK MAP kinase signaling in the Drosophila eye. Proceedings of the National Academy of Sciences of the United States of America. 104: 7098-103. PMID 17438281 DOI: 10.1073/Pnas.0701686104  0.746
2007 Hagemann IS, Narzinski KD, Baranski TJ. E2F8 is a nonreceptor activator of heterotrimeric G proteins. Journal of Molecular Signaling. 2: 3. PMID 17394670 DOI: 10.1186/1750-2187-2-3  0.712
2007 Matsumoto ML, Narzinski K, Kiser PD, Nikiforovich GV, Baranski TJ. A comprehensive structure-function map of the intracellular surface of the human C5a receptor. I. Identification of critical residues. The Journal of Biological Chemistry. 282: 3105-21. PMID 17135254 DOI: 10.1074/Jbc.M607679200  0.808
2007 Matsumoto ML, Narzinski K, Nikiforovich GV, Baranski TJ. A comprehensive structure-function map of the intracellular surface of the human C5a receptor. II. Elucidation of G protein specificity determinants. The Journal of Biological Chemistry. 282: 3122-33. PMID 17090530 DOI: 10.1074/Jbc.M607683200  0.813
2007 Sen S, Klco JM, Hansen JL, Nikiforovich GV, Sheikh SP, Baranski TJ. Dimerization/oligomerization in G protein‐coupled receptors (GPCRs) involve the participation of all transmembrane domains The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A613-A  0.685
2006 Hagemann IS, Narzinski KD, Floyd DH, Baranski TJ. Random mutagenesis of the complement factor 5a (C5a) receptor N terminus provides a structural constraint for C5a docking. The Journal of Biological Chemistry. 281: 36783-92. PMID 17023413 DOI: 10.1074/Jbc.M607686200  0.79
2006 Hagemann IS, Nikiforovich GV, Baranski TJ. Comparison of the retinitis pigmentosa mutations in rhodopsin with a functional map of the C5a receptor. Vision Research. 46: 4519-31. PMID 16962629 DOI: 10.1016/J.Visres.2006.07.010  0.652
2006 Klco JM, Nikiforovich GV, Baranski TJ. Genetic analysis of the first and third extracellular loops of the C5a receptor reveals an essential WXFG motif in the first loop. The Journal of Biological Chemistry. 281: 12010-9. PMID 16505476 DOI: 10.1074/Jbc.M600548200  0.718
2005 Anderson LL, Marshall GR, Baranski TJ. Expressed protein ligation to study protein interactions: semi-synthesis of the G-protein alpha subunit. Protein and Peptide Letters. 12: 783-7. PMID 16305549 DOI: 10.2174/0929866054864175  0.48
2005 Anderson LL, Marshall GR, Crocker E, Smith SO, Baranski TJ. Motion of carboxyl terminus of Galpha is restricted upon G protein activation. A solution NMR study using semisynthetic Galpha subunits. The Journal of Biological Chemistry. 280: 31019-26. PMID 15983037 DOI: 10.1074/Jbc.M503690200  0.479
2005 Klco JM, Wiegand CB, Narzinski K, Baranski TJ. Essential role for the second extracellular loop in C5a receptor activation. Nature Structural & Molecular Biology. 12: 320-6. PMID 15768031 DOI: 10.1038/Nsmb913  0.739
2003 Klco JM, Lassere TB, Baranski TJ. C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. The Journal of Biological Chemistry. 278: 35345-53. PMID 12835319 DOI: 10.1074/Jbc.M305606200  0.749
2003 Floyd DH, Geva A, Bruinsma SP, Overton MC, Blumer KJ, Baranski TJ. C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast. The Journal of Biological Chemistry. 278: 35354-61. PMID 12835318 DOI: 10.1074/Jbc.M305607200  0.755
2002 Whistler JL, Gerber BO, Meng EC, Baranski TJ, von Zastrow M, Bourne HR. Constitutive activation and endocytosis of the complement factor 5a receptor: evidence for multiple activated conformations of a G protein-coupled receptor. Traffic (Copenhagen, Denmark). 3: 866-77. PMID 12453150 DOI: 10.1034/J.1600-0854.2002.31203.X  0.582
2001 Gerber BO, Meng EC, Dotsch V, Baranski TJ, Bourne HR. An activation switch in the ligand binding pocket of the C5a receptor. The Journal of Biological Chemistry. 276: 3394-400. PMID 11062244 DOI: 10.1074/Jbc.M007748200  0.325
2000 Hansen JL, Servant G, Baranski TJ, Fujita T, Iiri T, Haunsø S, Sheikh SP. Functional reconstitution of the angiotensin II type 2 receptor and G(i) activation Circulation Research. 87: 753-759. PMID 11055978 DOI: 10.1161/01.Res.87.9.753  0.515
2000 Geva A, Lassere TB, Lichtarge O, Pollitt SK, Baranski TJ. Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function. The Journal of Biological Chemistry. 275: 35393-401. PMID 10952985 DOI: 10.1074/Jbc.M005602200  0.533
1999 Sheikh SP, Vilardarga JP, Baranski TJ, Lichtarge O, Iiri T, Meng EC, Nissenson RA, Bourne HR. Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation. The Journal of Biological Chemistry. 274: 17033-41. PMID 10358054 DOI: 10.1074/Jbc.274.24.17033  0.403
1999 Baranski TJ, Herzmark P, Lichtarge O, Gerber BO, Trueheart J, Meng EC, Iiri T, Sheikh SP, Bourne HR. C5a receptor activation. Genetic identification of critical residues in four transmembrane helices. The Journal of Biological Chemistry. 274: 15757-65. PMID 10336477 DOI: 10.1074/Jbc.274.22.15757  0.457
1999 Iiri T, Bell SM, Baranski TJ, Fujita T, Bourne HR. A Gsalpha mutant designed to inhibit receptor signaling through Gs. Proceedings of the National Academy of Sciences of the United States of America. 96: 499-504. PMID 9892662 DOI: 10.1073/Pnas.96.2.499  0.409
1990 Holwerda BC, Galvin NJ, Baranski TJ, Rogers JC. In Vitro Processing of Aleurain, a Barley Vacuolar Thiol Protease. The Plant Cell. 2: 1091-1106. PMID 12354950 DOI: 10.1105/Tpc.2.11.1091  0.314
1990 Baranski TJ, Faust PL, Kornfeld S. Generation of a lysosomal enzyme targeting signal in the secretory protein pepsinogen. Cell. 63: 281-91. PMID 2170024 DOI: 10.1016/0092-8674(90)90161-7  0.306
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