Year |
Citation |
Score |
2022 |
Rai A, Singh AK, Bleimling N, Posern G, Vetter IR, Goody RS. Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. Nature Communications. 13: 4262. PMID 35871249 DOI: 10.1038/s41467-022-31831-1 |
0.348 |
|
2020 |
Rai A, Bleimling N, Vetter IR, Goody RS. The mechanism of activation of the actin binding protein EHBP1 by Rab8 family members. Nature Communications. 11: 4187. PMID 32826901 DOI: 10.1038/s41467-020-17792-3 |
0.329 |
|
2017 |
Cigler M, Müller TG, Horn-Ghetko D, von Wrisberg MK, Fottner M, Goody RS, Itzen A, Müller MP, Lang K. Proximity-triggered covalent stabilization of low-affinity protein complexes in vitro and in vivo. Angewandte Chemie (International Ed. in English). PMID 28960788 DOI: 10.1002/Anie.201706927 |
0.423 |
|
2017 |
Rai A, Goody RS, Müller MP. Multivalency in Rab effector interactions. Small Gtpases. 1-7. PMID 28129037 DOI: 10.1080/21541248.2016.1265700 |
0.353 |
|
2017 |
Müller MP, Goody RS. Molecular control of Rab activity by GEFs, GAPs and GDI. Small Gtpases. 0. PMID 28055292 DOI: 10.1080/21541248.2016.1276999 |
0.34 |
|
2016 |
Rai A, Oprisko A, Campos J, Fu Y, Friese T, Itzen A, Goody RS, Gazdag EM, Müller MP. bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. Elife. 5. PMID 27552051 DOI: 10.7554/eLife.18675 |
0.354 |
|
2014 |
Gazdag EM, Schöbel S, Shkumatov AV, Goody RS, Itzen A. The structure of the N-terminal domain of the Legionella protein SidC. Journal of Structural Biology. 186: 188-94. PMID 24556577 DOI: 10.1016/j.jsb.2014.02.003 |
0.326 |
|
2014 |
Spiegel J, Cromm PM, Itzen A, Goody RS, Grossmann TN, Waldmann H. Direct targeting of Rab-GTPase-effector interactions. Angewandte Chemie (International Ed. in English). 53: 2498-503. PMID 24481744 DOI: 10.1002/Anie.201308568 |
0.379 |
|
2014 |
Goody RS, Itzen A. Modulation of small GTPases by Legionella. Current Topics in Microbiology and Immunology. 376: 117-33. PMID 23918171 DOI: 10.1007/82_2013_340 |
0.365 |
|
2013 |
Mihai Gazdag E, Streller A, Haneburger I, Hilbi H, Vetter IR, Goody RS, Itzen A. Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. Embo Reports. 14: 199-205. PMID 23288104 DOI: 10.1038/embor.2012.211 |
0.37 |
|
2013 |
Gogolin L, Schroeder H, Itzen A, Goody RS, Niemeyer CM, Becker CF. Protein-DNA arrays as tools for detection of protein-protein interactions by mass spectrometry. Chembiochem : a European Journal of Chemical Biology. 14: 92-9. PMID 23208955 DOI: 10.1002/Cbic.201200597 |
0.328 |
|
2013 |
Hagemann N, Hou X, Goody RS, Itzen A, Erdmann KS. Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome. Small Gtpases. 3: 107-10. PMID 22790198 DOI: 10.4161/sgtp.19380 |
0.325 |
|
2012 |
Müller MP, Shkumatov AV, Oesterlin LK, Schoebel S, Goody PR, Goody RS, Itzen A. Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein. The Journal of Biological Chemistry. 287: 35036-35046. PMID 22872634 DOI: 10.1074/jbc.M112.396861 |
0.359 |
|
2012 |
Tnimov Z, Guo Z, Gambin Y, Nguyen UT, Wu YW, Abankwa D, Stigter A, Collins BM, Waldmann H, Goody RS, Alexandrov K. Quantitative analysis of prenylated RhoA interaction with its chaperone, RhoGDI. The Journal of Biological Chemistry. 287: 26549-62. PMID 22628549 DOI: 10.1074/Jbc.M112.371294 |
0.316 |
|
2012 |
Deraeve C, Guo Z, Bon RS, Blankenfeldt W, DiLucrezia R, Wolf A, Menninger S, Stigter EA, Wetzel S, Choidas A, Alexandrov K, Waldmann H, Goody RS, Wu YW. Psoromic acid is a selective and covalent Rab-prenylation inhibitor targeting autoinhibited RabGGTase. Journal of the American Chemical Society. 134: 7384-91. PMID 22480322 DOI: 10.1021/Ja211305J |
0.318 |
|
2012 |
Oesterlin LK, Goody RS, Itzen A. Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proceedings of the National Academy of Sciences of the United States of America. 109: 5621-6. PMID 22411835 DOI: 10.1073/pnas.1121161109 |
0.422 |
|
2012 |
Goody PR, Heller K, Oesterlin LK, Müller MP, Itzen A, Goody RS. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. The Embo Journal. 31: 1774-84. PMID 22307087 DOI: 10.1038/emboj.2012.16 |
0.328 |
|
2011 |
Schoebel S, Cichy AL, Goody RS, Itzen A. Protein LidA from Legionella is a Rab GTPase supereffector. Proceedings of the National Academy of Sciences of the United States of America. 108: 17945-50. PMID 22011575 DOI: 10.1073/pnas.1113133108 |
0.339 |
|
2011 |
Goody RS, Müller MP, Schoebel S, Oesterlin LK, Blümer J, Peters H, Blankenfeldt W, Itzen A. The versatile Legionella effector protein DrrA. Communicative & Integrative Biology. 4: 72-4. PMID 21509184 DOI: 10.4161/cib.4.1.13857 |
0.354 |
|
2011 |
Hou X, Hagemann N, Schoebel S, Blankenfeldt W, Goody RS, Erdmann KS, Itzen A. A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1. The Embo Journal. 30: 1659-70. PMID 21378754 DOI: 10.1038/emboj.2011.60 |
0.322 |
|
2011 |
Wixler V, Wixler L, Altenfeld A, Ludwig S, Goody RS, Itzen A. Identification and characterisation of novel Mss4-binding Rab GTPases. Biological Chemistry. 392: 239-48. PMID 21194374 DOI: 10.1515/BC.2011.022 |
0.348 |
|
2010 |
Itzen A, Goody RS. GTPases involved in vesicular trafficking: structures and mechanisms. Seminars in Cell & Developmental Biology. 22: 48-56. PMID 20951823 DOI: 10.1016/j.semcdb.2010.10.003 |
0.328 |
|
2010 |
Müller MP, Peters H, Blümer J, Blankenfeldt W, Goody RS, Itzen A. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science (New York, N.Y.). 329: 946-9. PMID 20651120 DOI: 10.1126/science.1192276 |
0.314 |
|
2010 |
Wu YW, Oesterlin LK, Tan KT, Waldmann H, Alexandrov K, Goody RS. Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes. Nature Chemical Biology. 6: 534-40. PMID 20512138 DOI: 10.1038/Nchembio.386 |
0.325 |
|
2010 |
Nguyen UT, Goody RS, Alexandrov K. Understanding and exploiting protein prenyltransferases. Chembiochem : a European Journal of Chemical Biology. 11: 1194-201. PMID 20432425 DOI: 10.1002/cbic.200900727 |
0.325 |
|
2010 |
Weinrich D, Lin PC, Jonkheijm P, Nguyen UT, Schröder H, Niemeyer CM, Alexandrov K, Goody R, Waldmann H. Oriented immobilization of farnesylated proteins by the thiol-ene reaction. Angewandte Chemie (International Ed. in English). 49: 1252-7. PMID 20069617 DOI: 10.1002/Anie.200906190 |
0.321 |
|
2009 |
Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Molecular Cell. 36: 1060-72. PMID 20064470 DOI: 10.1016/j.molcel.2009.11.014 |
0.409 |
|
2009 |
Wu YW, Goody RS, Abagyan R, Alexandrov K. Structure of the disordered C terminus of Rab7 GTPase induced by binding to the Rab geranylgeranyl transferase catalytic complex reveals the mechanism of Rab prenylation. The Journal of Biological Chemistry. 284: 13185-92. PMID 19240028 DOI: 10.1074/Jbc.M900579200 |
0.391 |
|
2009 |
Nguyen UT, Guo Z, Delon C, Wu Y, Deraeve C, Fränzel B, Bon RS, Blankenfeldt W, Goody RS, Waldmann H, Wolters D, Alexandrov K. Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nature Chemical Biology. 5: 227-35. PMID 19219049 DOI: 10.1038/Nchembio.149 |
0.338 |
|
2009 |
Bergbrede T, Chuky N, Schoebel S, Blankenfeldt W, Geyer M, Fuchs E, Goody RS, Barr F, Alexandrov K. Biophysical analysis of the interaction of Rab6a GTPase with its effector domains. The Journal of Biological Chemistry. 284: 2628-35. PMID 19019823 DOI: 10.1074/jbc.M806003200 |
0.404 |
|
2008 |
Bleimling N, Alexandrov K, Goody R, Itzen A. Chaperone-assisted production of active human Rab8A GTPase in Escherichia coli. Protein Expression and Purification. 65: 190-5. PMID 19116169 DOI: 10.1016/j.pep.2008.12.002 |
0.346 |
|
2008 |
Guo Z, Wu YW, Das D, Delon C, Cramer J, Yu S, Thuns S, Lupilova N, Waldmann H, Brunsveld L, Goody RS, Alexandrov K, Blankenfeldt W. Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation. The Embo Journal. 27: 2444-56. PMID 18756270 DOI: 10.1038/Emboj.2008.164 |
0.429 |
|
2008 |
Pylypenko O, Schönichen A, Ludwig D, Ungermann C, Goody RS, Rak A, Geyer M. Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding. Journal of Molecular Biology. 377: 1334-45. PMID 18329045 DOI: 10.1016/J.Jmb.2008.01.099 |
0.344 |
|
2007 |
Wu YW, Tan KT, Waldmann H, Goody RS, Alexandrov K. Interaction analysis of prenylated Rab GTPase with Rab escort protein and GDP dissociation inhibitor explains the need for both regulators. Proceedings of the National Academy of Sciences of the United States of America. 104: 12294-9. PMID 17640890 DOI: 10.1073/Pnas.0701817104 |
0.394 |
|
2007 |
Nguyen UT, Cramer J, Gomis J, Reents R, Gutierrez-Rodriguez M, Goody RS, Alexandrov K, Waldmann H. Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization. Chembiochem : a European Journal of Chemical Biology. 8: 408-23. PMID 17279592 DOI: 10.1002/Cbic.200600440 |
0.342 |
|
2006 |
Itzen A, Rak A, Goody RS. Sec2 is a highly efficient exchange factor for the Rab protein Sec4. Journal of Molecular Biology. 365: 1359-67. PMID 17134721 DOI: 10.1016/j.jmb.2006.10.096 |
0.385 |
|
2006 |
Kötting C, Blessenohl M, Suveyzdis Y, Goody RS, Wittinghofer A, Gerwert K. A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein. Proceedings of the National Academy of Sciences of the United States of America. 103: 13911-6. PMID 16968776 DOI: 10.1073/pnas.0604128103 |
0.333 |
|
2006 |
Watzke A, Gutierrez-Rodriguez M, Köhn M, Wacker R, Schroeder H, Breinbauer R, Kuhlmann J, Alexandrov K, Niemeyer CM, Goody RS, Waldmann H. A generic building block for C- and N-terminal protein-labeling and protein-immobilization. Bioorganic & Medicinal Chemistry. 14: 6288-306. PMID 16725326 DOI: 10.1016/J.Bmc.2006.05.006 |
0.327 |
|
2006 |
Itzen A, Pylypenko O, Goody RS, Alexandrov K, Rak A. Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4. The Embo Journal. 25: 1445-55. PMID 16541104 DOI: 10.1038/sj.emboj.7601044 |
0.404 |
|
2006 |
Goody RS, Durek T, Waldmann H, Brunsveld L, Alexandrov K. Application of protein semisynthesis for the construction of functionalized posttranslationally modified rab GTPases. Methods in Enzymology. 403: 29-42. PMID 16473575 DOI: 10.1016/S0076-6879(05)03004-1 |
0.378 |
|
2006 |
Pylypenko O, Rak A, Durek T, Kushnir S, Dursina BE, Thomae NH, Constantinescu AT, Brunsveld L, Watzke A, Waldmann H, Goody RS, Alexandrov K. Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-mediated Rab recycling. The Embo Journal. 25: 13-23. PMID 16395334 DOI: 10.1038/Sj.Emboj.7600921 |
0.354 |
|
2006 |
Brunsveld L, Watzke A, Durek T, Alexandrov K, Goody RS, Waldmann H. Synthesis of functionalized rab GTPases by a combination of solution- or solid-phase lipopeptide synthesis with expressed protein ligation. Chemistry (Weinheim An Der Bergstrasse, Germany). 11: 2756-72. PMID 15729676 DOI: 10.1002/Chem.200401041 |
0.303 |
|
2005 |
Watzke A, Brunsveld L, Durek T, Alexandrov K, Rak A, Goody RS, Waldmann H. Chemical biology of protein lipidation: semi-synthesis and structure elucidation of prenylated RabGTPases. Organic & Biomolecular Chemistry. 3: 1157-64. PMID 15785799 DOI: 10.1039/B417573E |
0.401 |
|
2005 |
Durek T, Alexandrov K, Goody RS, Hildebrand A, Heinemann I, Waldmann H. Synthesis of fluorescently labeled mono- and diprenylated Rab7 GTPase. Journal of the American Chemical Society. 126: 16368-78. PMID 15600338 DOI: 10.1021/Ja046164N |
0.338 |
|
2005 |
Dursina BE, Reents R, Niculae A, Veligodsky A, Breitling R, Pyatkov K, Waldmann H, Goody RS, Alexandrov K. A genetically encodable microtag for chemo-enzymatic derivatization and purification of recombinant proteins. Protein Expression and Purification. 39: 71-81. PMID 15596362 DOI: 10.1016/J.Pep.2004.09.015 |
0.35 |
|
2004 |
Durek T, Goody RS, Alexandrov K. In vitro semisynthesis and applications of C-terminally modified rab proteins. Methods in Molecular Biology (Clifton, N.J.). 283: 233-44. PMID 15197315 DOI: 10.1385/1-59259-813-7:233 |
0.315 |
|
2004 |
Rak A, Pylypenko O, Niculae A, Pyatkov K, Goody RS, Alexandrov K. Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease. Cell. 117: 749-60. PMID 15186776 DOI: 10.1016/j.cell.2004.05.017 |
0.409 |
|
2003 |
Rak A, Pylypenko O, Durek T, Watzke A, Kushnir S, Brunsveld L, Waldmann H, Goody RS, Alexandrov K. Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science (New York, N.Y.). 302: 646-50. PMID 14576435 DOI: 10.1126/Science.1087761 |
0.415 |
|
2003 |
Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thomä NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Molecular Cell. 11: 483-94. PMID 12620235 DOI: 10.1016/S1097-2765(03)00044-3 |
0.372 |
|
2002 |
Rak A, Niculae A, Kalinin A, Thomä NH, Sidorovitch V, Goody RS, Alexandrov K. In vitro assembly, purification, and crystallization of the rab geranylgeranyl transferase:substrate complex. Protein Expression and Purification. 25: 23-30. PMID 12071695 DOI: 10.1006/prep.2001.1605 |
0.415 |
|
2002 |
Dursina B, Thomä NH, Sidorovitch V, Niculae A, Iakovenko A, Rak A, Albert S, Ceacareanu AC, Kölling R, Herrmann C, Goody RS, Alexandrov K. Interaction of yeast Rab geranylgeranyl transferase with its protein and lipid substrates. Biochemistry. 41: 6805-16. PMID 12022885 DOI: 10.1021/bi016067w |
0.434 |
|
2002 |
Alexandrov K, Heinemann I, Durek T, Sidorovitch V, Goody RS, Waldmann H. Intein-mediated synthesis of geranylgeranylated Rab7 protein in vitro. Journal of the American Chemical Society. 124: 5648-9. PMID 12010032 DOI: 10.1021/Ja017799E |
0.349 |
|
1999 |
Owen DJ, Alexandrov K, Rostkova E, Scheidig AJ, Goody RS, Waldmann H. Chemo-Enzymatic Synthesis of Fluorescent Rab 7 Proteins: Tools to Study Vesicular Trafficking in Cells. Angewandte Chemie (International Ed. in English). 38: 509-512. PMID 29711783 DOI: 10.1002/(Sici)1521-3773(19990215)38:4<509::Aid-Anie509>3.3.Co;2-V |
0.323 |
|
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