| Year |
Citation |
Score |
| 2024 |
Zheng C, Nguyen KK, Vishnivetskiy SA, Gurevich VV, Gurevich EV. Arrestin-3 binds parkin and enhances parkin-dependent mitophagy. Journal of Neurochemistry. PMID 38196269 DOI: 10.1111/jnc.16043 |
0.443 |
|
| 2023 |
Ahmed MR, Zheng C, Dunning JL, Ahmed MS, Ge C, Pair FS, Gurevich VV, Gurevich EV. Arrestin-3-assisted activation of JNK3 mediates dopaminergic behavioral and signaling plasticity in vivo. Biorxiv : the Preprint Server For Biology. PMID 37961199 DOI: 10.1101/2023.10.27.564447 |
0.736 |
|
| 2023 |
Zheng C, Javitch JA, Lambert NA, Donthamsetti P, Gurevich VV. In-Cell Arrestin-Receptor Interaction Assays. Current Protocols. 3: e890. PMID 37787634 DOI: 10.1002/cpz1.890 |
0.589 |
|
| 2023 |
Zhan X, Kaoud TS, Dalby KN, Gurevich EV, Gurevich VV. Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs). Current Protocols. 3: e839. PMID 37668419 DOI: 10.1002/cpz1.839 |
0.32 |
|
| 2023 |
Gurevich VV. Do arrestin oligomers have specific functions? Cell Signaling. 1: 42-46. PMID 37664541 DOI: 10.46439/signaling.1.009 |
0.374 |
|
| 2023 |
Zheng C, Weinstein LD, Nguyen KK, Grewal A, Gurevich EV, Gurevich VV. GPCR Binding and JNK3 Activation by Arrestin-3 Have Different Structural Requirements. Cells. 12. PMID 37371033 DOI: 10.3390/cells12121563 |
0.431 |
|
| 2023 |
Gurevich VV, Gurevich EV. Mechanisms of Arrestin-Mediated Signaling. Current Protocols. 3: e821. PMID 37367499 DOI: 10.1002/cpz1.821 |
0.439 |
|
| 2023 |
Vishnivetskiy SA, Weinstein LD, Zheng C, Gurevich EV, Gurevich VV. Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements. International Journal of Molecular Sciences. 24. PMID 37240250 DOI: 10.3390/ijms24108903 |
0.355 |
|
| 2023 |
Zheng C, Weinstein LD, Nguyen KK, Grewal A, Gurevich EV, Gurevich VV. GPCR binding and JNK3 activation by arrestin-3 have different structural requirements. Biorxiv : the Preprint Server For Biology. PMID 37205393 DOI: 10.1101/2023.05.01.538990 |
0.431 |
|
| 2022 |
Vishnivetskiy SA, Huh EK, Karnam PC, Oviedo S, Gurevich EV, Gurevich VV. The Role of Arrestin-1 Middle Loop in Rhodopsin Binding. International Journal of Molecular Sciences. 23. PMID 36430370 DOI: 10.3390/ijms232213887 |
0.459 |
|
| 2022 |
Perry-Hauser NA, Kaoud TS, Stoy H, Zhan X, Chen Q, Dalby KN, Iverson TM, Gurevich VV, Gurevich EV. Short Arrestin-3-Derived Peptides Activate JNK3 in Cells. International Journal of Molecular Sciences. 23. PMID 35955810 DOI: 10.3390/ijms23158679 |
0.663 |
|
| 2022 |
Asher WB, Terry DS, Gregorio GGA, Kahsai AW, Borgia A, Xie B, Modak A, Zhu Y, Jang W, Govindaraju A, Huang LY, Inoue A, Lambert NA, Gurevich VV, Shi L, et al. GPCR-mediated β-arrestin activation deconvoluted with single-molecule precision. Cell. PMID 35483373 DOI: 10.1016/j.cell.2022.03.042 |
0.676 |
|
| 2022 |
Seyedabadi M, Gharghabi M, Gurevich EV, Gurevich VV. Structural basis of GPCR coupling to distinct signal transducers: implications for biased signaling. Trends in Biochemical Sciences. 47: 570-581. PMID 35396120 DOI: 10.1016/j.tibs.2022.03.009 |
0.415 |
|
| 2022 |
Hsieh CL, Yao Y, Gurevich VV, Chen J. Arrestin facilitates rhodopsin dephosphorylation . The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. PMID 35332081 DOI: 10.1523/JNEUROSCI.0141-22.2022 |
0.43 |
|
| 2022 |
Perry-Hauser NA, Bennett Hopkins J, Zhuo Y, Zheng C, Perez I, Schultz KM, Vishnivetskiy SA, Kaya AI, Sharma P, Dalby KN, Young Chung K, Klug CS, Gurevich VV, Iverson TM. The two non-visual arrestins engage ERK2 differently. Journal of Molecular Biology. 167465. PMID 35077767 DOI: 10.1016/j.jmb.2022.167465 |
0.429 |
|
| 2021 |
Perez I, Berndt S, Agarwal R, Castro MA, Vishnivetskiy SA, Smith JC, Sanders CR, Gurevich VV, Iverson TM. A Model for the Signal Initiation Complex Between Arrestin-3 and the Src Family Kinase Fgr. Journal of Molecular Biology. 434: 167400. PMID 34902430 DOI: 10.1016/j.jmb.2021.167400 |
0.391 |
|
| 2021 |
Karnam PC, Vishnivetskiy SA, Gurevich VV. Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors. International Journal of Molecular Sciences. 22. PMID 34830362 DOI: 10.3390/ijms222212481 |
0.447 |
|
| 2021 |
Qu C, Park JY, Yun MW, He QT, Yang F, Kim K, Ham D, Li RR, Iverson TM, Gurevich VV, Sun JP, Chung KY. Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34507982 DOI: 10.1073/pnas.2026491118 |
0.412 |
|
| 2021 |
Seyedabadi M, Gharghabi M, Gurevich EV, Gurevich VV. Receptor-Arrestin Interactions: The GPCR Perspective. Biomolecules. 11. PMID 33557162 DOI: 10.3390/biom11020218 |
0.435 |
|
| 2020 |
Gurevich EV, Gurevich VV. GRKs as Modulators of Neurotransmitter Receptors. Cells. 10. PMID 33396400 DOI: 10.3390/cells10010052 |
0.439 |
|
| 2020 |
Chen Q, Zhuo Y, Sharma P, Perez I, Francis DJ, Chakravarthy S, Vishnivetskiy SA, Berndt S, Hanson SM, Zhan X, Brooks EK, Altenbach C, Hubbell WL, Klug CS, Iverson TM, ... Gurevich VV, et al. An eight amino acid segment controls oligomerization and preferred conformation of the two non-visual arrestins. Journal of Molecular Biology. 166790. PMID 33387531 DOI: 10.1016/j.jmb.2020.166790 |
0.433 |
|
| 2020 |
Vishnivetskiy SA, Huh EK, Gurevich EV, Gurevich VV. The finger loop as an activation sensor in arrestin. Journal of Neurochemistry. PMID 33159335 DOI: 10.1111/jnc.15232 |
0.415 |
|
| 2020 |
Samaranayake S, Vishnivetskiy SA, Shores CR, Thibeault KC, Kook S, Chen J, Burns ME, Gurevich EV, Gurevich VV. Biological role of arrestin-1 oligomerization. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. PMID 32948676 DOI: 10.1523/Jneurosci.0749-20.2020 |
0.343 |
|
| 2020 |
Böttke T, Ernicke S, Serfling R, Ihling C, Burda E, Gurevich VV, Sinz A, Coin I. Exploring GPCR-arrestin interfaces with genetically encoded crosslinkers. Embo Reports. e50437. PMID 32929862 DOI: 10.15252/Embr.202050437 |
0.479 |
|
| 2020 |
Krug U, Gloge A, Schmidt P, Becker-Baldus J, Bernhard F, Kaiser A, Montag C, Gauglitz M, Vishnivetskiy SA, Gurevich VV, Beck-Sickinger AG, Glaubitz C, Huster D. The Conformational Equilibrium of the Neuropeptide Y2 Receptor in Bilayer Membranes. Angewandte Chemie (International Ed. in English). PMID 32790043 DOI: 10.1002/Anie.202006075 |
0.438 |
|
| 2020 |
Zhuo Y, Gurevich VV, Vishnivetskiy SA, Klug CS, Marchese A. A non-GPCR binding partner interacts with a novel surface on β-arrestin1 to mediate GPCR signaling. The Journal of Biological Chemistry. PMID 32753481 DOI: 10.1074/Jbc.Ra120.015074 |
0.449 |
|
| 2020 |
Gurevich VV, Gurevich EV. Corrigendum to "Biased GPCR signaling: Possible mechanisms and inherent limitations" [Pharmacology & Therapeutics 211 (2020) 107540]. Pharmacology & Therapeutics. 107615. PMID 32622639 DOI: 10.1016/J.Pharmthera.2020.107615 |
0.344 |
|
| 2020 |
Vishnivetskiy SA, Zheng C, May MB, Karnam PC, Gurevich EV, Gurevich VV. Lysine in the lariat loop of arrestins does not serve as phosphate sensor. Journal of Neurochemistry. PMID 32594524 DOI: 10.1111/Jnc.15110 |
0.508 |
|
| 2020 |
Kaya AI, Perry NA, Gurevich VV, Iverson TM. Phosphorylation barcode-dependent signal bias of the dopamine D1 receptor. Proceedings of the National Academy of Sciences of the United States of America. PMID 32503917 DOI: 10.1073/Pnas.1918736117 |
0.733 |
|
| 2020 |
Gurevich VV, Gurevich EV. Targeting arrestin interactions with its partners for therapeutic purposes. Advances in Protein Chemistry and Structural Biology. 121: 169-197. PMID 32312421 DOI: 10.1016/Bs.Apcsb.2019.11.011 |
0.471 |
|
| 2020 |
Gurevich VV, Gurevich EV. Biased GPCR signaling: Possible mechanisms and inherent limitations. Pharmacology & Therapeutics. 107540. PMID 32201315 DOI: 10.1016/J.Pharmthera.2020.107540 |
0.529 |
|
| 2020 |
Kook S, Zhan X, Thibeault K, Ahmed MR, Gurevich VV, Gurevich EV. Mdm2 enhances ligase activity of parkin and facilitates mitophagy. Scientific Reports. 10: 5028. PMID 32193420 DOI: 10.1038/S41598-020-61796-4 |
0.353 |
|
| 2019 |
Meister J, Bone DBJ, Godlewski G, Liu Z, Lee RJ, Vishnivetskiy SA, Gurevich VV, Springer D, Kunos G, Wess J. Metabolic effects of skeletal muscle-specific deletion of beta-arrestin-1 and -2 in mice. Plos Genetics. 15: e1008424. PMID 31622341 DOI: 10.1371/Journal.Pgen.1008424 |
0.303 |
|
| 2019 |
Gurevich VV, Gurevich EV. Plethora of functions packed into 45 kDa arrestins: biological implications and possible therapeutic strategies. Cellular and Molecular Life Sciences : Cmls. 76: 4413-4421. PMID 31422444 DOI: 10.1007/S00018-019-03272-5 |
0.521 |
|
| 2019 |
Gurevich VV. Protein multi-functionality: introduction. Cellular and Molecular Life Sciences : Cmls. 76: 4405-4406. PMID 31422443 DOI: 10.1007/S00018-019-03271-6 |
0.363 |
|
| 2019 |
Perry NA, Fialkowski KP, Kaoud TS, Kaya AI, Chen AL, Taliaferro JM, Gurevich VV, Dalby KN, Iverson TM. Arrestin-3 interaction with maternal embryonic leucine-zipper kinase. Cellular Signalling. 109366. PMID 31352007 DOI: 10.1016/J.Cellsig.2019.109366 |
0.65 |
|
| 2019 |
Sammons RM, Perry NA, Li Y, Cho EJ, Piserchio A, Zamora-Olivares DP, Ghose R, Kaoud TS, Debevec G, Bartholomeusz C, Gurevich VV, Iverson TM, Giulianotti M, Houghten RA, Dalby KN. A Novel Class of Common Docking Domain Inhibitors That Prevent ERK2 Activation and Substrate Phosphorylation. Acs Chemical Biology. PMID 31058487 DOI: 10.1021/Acschembio.9B00093 |
0.687 |
|
| 2019 |
Berndt S, Gurevich VV, Iverson TM. Crystal structure of the SH3 domain of human Lyn non-receptor tyrosine kinase. Plos One. 14: e0215140. PMID 30969999 DOI: 10.1371/Journal.Pone.0215140 |
0.664 |
|
| 2019 |
Perry NA, Zhan X, Gurevich EV, Iverson TM, Gurevich VV. Using In Vitro Pull-Down and In-Cell Overexpression Assays to Study Protein Interactions with Arrestin. Methods in Molecular Biology (Clifton, N.J.). 1957: 107-120. PMID 30919350 DOI: 10.1007/978-1-4939-9158-7_7 |
0.707 |
|
| 2019 |
Zheng C, Tholen J, Gurevich VV. Critical role of the finger loop in arrestin binding to the receptors. Plos One. 14: e0213792. PMID 30875392 DOI: 10.1371/Journal.Pone.0213792 |
0.495 |
|
| 2019 |
Gurevich VV, Gurevich EV. GPCR Signaling Regulation: The Role of GRKs and Arrestins. Frontiers in Pharmacology. 10: 125. PMID 30837883 DOI: 10.3389/Fphar.2019.00125 |
0.543 |
|
| 2019 |
Gurevich VV, Gurevich EV. Arrestin mutations: Some cause diseases, others promise cure. Progress in Molecular Biology and Translational Science. 161: 29-45. PMID 30711028 DOI: 10.1016/Bs.Pmbts.2018.09.004 |
0.437 |
|
| 2019 |
Gurevich VV, Gurevich EV. The structural basis of the arrestin binding to GPCRs. Molecular and Cellular Endocrinology. 484: 34-41. PMID 30703488 DOI: 10.1016/J.Mce.2019.01.019 |
0.573 |
|
| 2019 |
Kook S, Vishnivetskiy SA, Gurevich VV, Gurevich EV. Cleavage of arrestin-3 by caspases attenuates cell death by precluding arrestin-dependent JNK activation. Cellular Signalling. 54: 161-169. PMID 30529266 DOI: 10.1016/J.Cellsig.2018.11.023 |
0.435 |
|
| 2018 |
Gurevich VV, Gurevich EV. Arrestin-mediated signaling: Is there a controversy? World Journal of Biological Chemistry. 9: 25-35. PMID 30595812 DOI: 10.4331/Wjbc.V9.I3.25 |
0.514 |
|
| 2018 |
Perry NA, Kaoud TS, Ortega OO, Kaya AI, Marcus DJ, Pleinis JM, Berndt S, Chen Q, Zhan X, Dalby KN, Lopez CF, Iverson TM, Gurevich VV. Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification. Proceedings of the National Academy of Sciences of the United States of America. PMID 30591558 DOI: 10.1073/Pnas.1819230116 |
0.689 |
|
| 2018 |
Gurevich VV, Chen Q, Gurevich EV. Arrestins: Introducing Signaling Bias Into Multifunctional Proteins. Progress in Molecular Biology and Translational Science. 160: 47-61. PMID 30470292 DOI: 10.1016/Bs.Pmbts.2018.07.007 |
0.555 |
|
| 2018 |
Gurevich VV, Gurevich EV. Arrestins and G proteins in cellular signaling: The coin has two sides. Science Signaling. 11. PMID 30254054 DOI: 10.1126/Scisignal.Aav1646 |
0.447 |
|
| 2018 |
Samaranayake S, Song X, Vishnivetskiy SA, Chen J, Gurevich EV, Gurevich VV. Enhanced Mutant Compensates for Defects in Rhodopsin Phosphorylation in the Presence of Endogenous Arrestin-1. Frontiers in Molecular Neuroscience. 11: 203. PMID 29973866 DOI: 10.3389/Fnmol.2018.00203 |
0.335 |
|
| 2018 |
Gurevich VV, Gurevich EV. GPCRs and Signal Transducers: Interaction Stoichiometry. Trends in Pharmacological Sciences. 39: 672-684. PMID 29739625 DOI: 10.1016/J.Tips.2018.04.002 |
0.501 |
|
| 2018 |
Chen Q, Iverson TM, Gurevich VV. Structural Basis of Arrestin-Dependent Signal Transduction. Trends in Biochemical Sciences. PMID 29636212 DOI: 10.1016/J.Tibs.2018.03.005 |
0.723 |
|
| 2018 |
Gurevich VV, Gurevich EV, Uversky VN. Arrestins: structural disorder creates rich functionality. Protein & Cell. 9: 986-1003. PMID 29453740 DOI: 10.1007/S13238-017-0501-8 |
0.452 |
|
| 2017 |
Gurevich VV, Gurevich EV. Molecular Mechanisms of GPCR Signaling: A Structural Perspective. International Journal of Molecular Sciences. 18. PMID 29186792 DOI: 10.3390/Ijms18122519 |
0.525 |
|
| 2017 |
Tóth AD, Prokop S, Gyombolai P, Várnai P, Balla A, Gurevich VV, Hunyady L, Turu G. Heterologous phosphorylation-induced formation of a stability lock permits regulation of inactive receptors by β-arrestins. The Journal of Biological Chemistry. PMID 29146594 DOI: 10.1074/Jbc.M117.813139 |
0.495 |
|
| 2017 |
Cleghorn WM, Bulus N, Kook S, Gurevich VV, Zent R, Gurevich EV. Non-visual arrestins regulate the focal adhesion formation via small GTPases RhoA and Rac1 independently of GPCRs. Cellular Signalling. PMID 29133163 DOI: 10.1016/J.Cellsig.2017.11.003 |
0.466 |
|
| 2017 |
Chen Q, Perry NA, Vishnivetskiy SA, Berndt S, Gilbert NC, Zhuo Y, Singh PK, Tholen J, Ohi MD, Gurevich EV, Brautigam CA, Klug CS, Gurevich VV, Iverson TM. Structural basis of arrestin-3 activation and signaling. Nature Communications. 8: 1427. PMID 29127291 DOI: 10.1038/S41467-017-01218-8 |
0.711 |
|
| 2017 |
Tso SC, Chen Q, Vishnivetskiy SA, Gurevich VV, Iverson TM, Brautigam CA. Using two-site binding models to analyze microscale thermophoresis data. Analytical Biochemistry. PMID 29054528 DOI: 10.1016/J.Ab.2017.10.013 |
0.619 |
|
| 2017 |
Zhou XE, He Y, de Waal PW, Gao X, Kang Y, Van Eps N, Yin Y, Pal K, Goswami D, White TA, Barty A, Latorraca NR, Chapman HN, Hubbell WL, Dror RO, ... ... Gurevich VV, et al. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors. Cell. 170: 457-469.e13. PMID 28753425 DOI: 10.1016/J.Cell.2017.07.002 |
0.54 |
|
| 2017 |
Indrischek H, Prohaska SJ, Gurevich VV, Gurevich EV, Stadler PF. Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes. Bmc Evolutionary Biology. 17: 163. PMID 28683816 DOI: 10.1186/S12862-017-1001-4 |
0.529 |
|
| 2017 |
Zhu L, Rossi M, Cui Y, Lee RJ, Sakamoto W, Perry NA, Urs NM, Caron MG, Gurevich VV, Godlewski G, Kunos G, Chen M, Chen W, Wess J. Hepatic β-arrestin 2 is essential for maintaining euglycemia. The Journal of Clinical Investigation. PMID 28650340 DOI: 10.1172/Jci92913 |
0.305 |
|
| 2017 |
Vishnivetskiy SA, Lee RJ, Zhou XE, Franz A, Xu Q, Xu HE, Gurevich VV. Functional role of the three conserved cysteines in the N-domain of visual arrestin-1. The Journal of Biological Chemistry. PMID 28536260 DOI: 10.1074/Jbc.M117.790386 |
0.494 |
|
| 2017 |
Prokop S, Perry NA, Vishnivetskiy SA, Toth AD, Inoue A, Milligan G, Iverson TM, Hunyady L, Gurevich VV. Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors. Cellular Signalling. PMID 28461104 DOI: 10.1016/J.Cellsig.2017.04.021 |
0.718 |
|
| 2017 |
Zurkovsky L, Sedaghat K, Ahmed MR, Gurevich VV, Gurevich EV. Arrestin-2 and arrestin-3 differentially modulate locomotor responses and sensitization to amphetamine. Neuropharmacology. PMID 28419873 DOI: 10.1016/J.Neuropharm.2017.04.021 |
0.408 |
|
| 2016 |
Wanka L, Babilon S, Burkert K, Mörl K, Gurevich VV, Beck-Sickinger AG. C-terminal motif of human neuropeptide Y4 receptor determines internalization and arrestin recruitment. Cellular Signalling. PMID 27818291 DOI: 10.1016/J.Cellsig.2016.11.003 |
0.493 |
|
| 2016 |
Gurevich EV, Gainetdinov RR, Gurevich VV. G protein-coupled receptor kinases as regulators of dopamine receptor functions. Pharmacological Research. PMID 27178731 DOI: 10.1016/J.Phrs.2016.05.010 |
0.493 |
|
| 2016 |
Zhan X, Stoy H, Kaoud TS, Perry NA, Chen Q, Perez A, Els-Heindl S, Slagis JV, Iverson TM, Beck-Sickinger AG, Gurevich EV, Dalby KN, Gurevich VV. Peptide mini-scaffold facilitates JNK3 activation in cells. Scientific Reports. 6: 21025. PMID 26868142 DOI: 10.1038/Srep21025 |
0.663 |
|
| 2016 |
Hu J, Stern M, Gimenez LE, Wanka L, Zhu L, Rossi M, Meister J, Inoue A, Beck-Sickinger AG, Gurevich VV, Wess J. A G Protein-Biased Designer G Protein-Coupled Receptor Useful for Studying the Physiological Relevance of Gq/11-Dependent Signaling Pathways. The Journal of Biological Chemistry. PMID 26851281 DOI: 10.1074/Jbc.M115.702282 |
0.489 |
|
| 2016 |
Wanka L, Babilon S, Burkert K, Gurevich VV, Beck-Sickinger AG. Influence of distinct motifs within the carboxyl-terminusof the human neuropeptide Y4 receptor on internalization and arrestin3 recruitment Neuropeptides. 55: 23. DOI: 10.1016/J.Npep.2015.11.065 |
0.389 |
|
| 2016 |
Chen Q, Zhuo Y, Kook S, Francis DJ, Vishnivetskiy SA, Hanson SM, Zhan X, Brooks EK, Iverson TM, Altenbach C, Hubbell WL, Klug CS, Gurevich VV. The two non-visual arrestins form distinct oligomers with different functional capabilities Neuropeptides. 55: 23. DOI: 10.1016/J.Npep.2015.11.064 |
0.592 |
|
| 2016 |
Schubert M, Stichel JD, Sliwosky GR, Gurevich VV, Weaver CD, Meiler J, Beck-Sickinger AG. Allosteric modulators to target the human Y4 receptor Neuropeptides. 55: 18. DOI: 10.1016/J.Npep.2015.11.049 |
0.345 |
|
| 2015 |
Gurevich VV, Gurevich EV. Analyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKs. Critical Reviews in Biochemistry and Molecular Biology. 50: 440-52. PMID 26453028 DOI: 10.3109/10409238.2015.1067185 |
0.37 |
|
| 2015 |
Chatterjee D, Eckert CE, Slavov C, Saxena K, Fürtig B, Sanders CR, Gurevich VV, Wachtveitl J, Schwalbe H. Influence of Arrestin on the Photodecay of Bovine Rhodopsin. Angewandte Chemie (International Ed. in English). 54: 13555-60. PMID 26383645 DOI: 10.1002/Anie.201505798 |
0.341 |
|
| 2015 |
Donthamsetti P, Quejada JR, Javitch JA, Gurevich VV, Lambert NA. Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist-Induced Arrestin Recruitment to Modified and Unmodified G Protein-Coupled Receptors. Current Protocols in Pharmacology / Editorial Board, S.J. Enna (Editor-in-Chief) ... [Et Al.]. 70: 2.14.1-2.14.14. PMID 26331887 DOI: 10.1002/0471141755.Ph0214S70 |
0.638 |
|
| 2015 |
Stoy H, Gurevich VV. How genetic errors in GPCRs affect their function: Possible therapeutic strategies. Genes & Diseases. 2: 108-132. PMID 26229975 DOI: 10.1016/J.Gendis.2015.02.005 |
0.391 |
|
| 2015 |
Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, Barty A, White TA, Yefanov O, Han GW, Xu Q, de Waal PW, Ke J, Tan MH, Zhang C, ... ... Gurevich VV, et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature. PMID 26200343 DOI: 10.1038/Nature14656 |
0.439 |
|
| 2015 |
Chang SD, Mascarella SW, Spangler SM, Gurevich VV, Navarro HA, Carroll FI, Bruchas MR. Quantitative Signaling and Structure-Activity Analyses Demonstrate Functional Selectivity at the Nociceptin/Orphanin FQ Opioid Receptor. Molecular Pharmacology. 88: 502-11. PMID 26134494 DOI: 10.1124/Mol.115.099150 |
0.473 |
|
| 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 |
0.511 |
|
| 2015 |
Gurevich VV, Gurevich EV. Arrestins: Critical Players in Trafficking of Many GPCRs. Progress in Molecular Biology and Translational Science. 132: 1-14. PMID 26055052 DOI: 10.1016/Bs.Pmbts.2015.02.010 |
0.524 |
|
| 2015 |
Ahmed MR, Bychkov E, Li L, Gurevich VV, Gurevich EV. GRK3 suppresses L-DOPA-induced dyskinesia in the rat model of Parkinson's disease via its RGS homology domain. Scientific Reports. 5: 10920. PMID 26043205 DOI: 10.1038/Srep10920 |
0.384 |
|
| 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 |
0.498 |
|
| 2015 |
Heifetz A, Schertler GF, Seifert R, Tate CG, Sexton PM, Gurevich VV, Fourmy D, Cherezov V, Marshall FH, Storer RI, Moraes I, Tikhonova IG, Tautermann CS, Hunt P, Ceska T, et al. GPCR structure, function, drug discovery and crystallography: report from Academia-Industry International Conference (UK Royal Society) Chicheley Hall, 1-2 September 2014. Naunyn-Schmiedeberg's Archives of Pharmacology. 388: 883-903. PMID 25772061 DOI: 10.1007/S00210-015-1111-8 |
0.348 |
|
| 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 |
0.534 |
|
| 2015 |
Zhan X, Kook S, Kaoud TS, Dalby KN, Gurevich EV, Gurevich VV. Arrestin-3-Dependent Activation of c-Jun N-Terminal Kinases (JNKs). Current Protocols in Pharmacology / Editorial Board, S.J. Enna (Editor-in-Chief) ... [Et Al.]. 68: 2.12.1-2.12.26. PMID 25737158 DOI: 10.1002/0471141755.Ph0212S68 |
0.445 |
|
| 2015 |
Chen Q, Vishnivetskiy SA, Zhuang T, Cho MK, Thaker TM, Sanders CR, Gurevich VV, Iverson TM. The rhodopsin-arrestin-1 interaction in bicelles. Methods in Molecular Biology (Clifton, N.J.). 1271: 77-95. PMID 25697518 DOI: 10.1007/978-1-4939-2330-4_6 |
0.705 |
|
| 2015 |
Cleghorn WM, Branch KM, Kook S, Arnette C, Bulus N, Zent R, Kaverina I, Gurevich EV, Weaver AM, Gurevich VV. Arrestins regulate cell spreading and motility via focal adhesion dynamics. Molecular Biology of the Cell. 26: 622-35. PMID 25540425 DOI: 10.1091/Mbc.E14-02-0740 |
0.339 |
|
| 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 |
0.432 |
|
| 2014 |
Vishnivetskiy SA, Zhan X, Chen Q, Iverson TM, Gurevich VV. Arrestin expression in E. coli and purification. Current Protocols in Pharmacology / Editorial Board, S.J. Enna (Editor-in-Chief) ... [Et Al.]. 67: Unit 2.11.. PMID 25446290 DOI: 10.1002/0471141755.Ph0211S67 |
0.636 |
|
| 2014 |
Gurevich VV, Gurevich EV. Overview of different mechanisms of arrestin-mediated signaling. Current Protocols in Pharmacology. 67: Unit 2.10.1-9. PMID 25446289 DOI: 10.1002/0471141755.Ph0210S67 |
0.565 |
|
| 2014 |
Mäde V, Babilon S, Jolly N, Wanka L, Bellmann-Sickert K, Diaz Gimenez LE, Mörl K, Cox HM, Gurevich VV, Beck-Sickinger AG. Peptide modifications differentially alter G protein-coupled receptor internalization and signaling bias. Angewandte Chemie (International Ed. in English). 53: 10067-71. PMID 25065900 DOI: 10.1002/Anie.201403750 |
0.412 |
|
| 2014 |
Zhuo Y, Vishnivetskiy SA, Zhan X, Gurevich VV, Klug CS. Identification of receptor binding-induced conformational changes in non-visual arrestins. The Journal of Biological Chemistry. 289: 20991-1002. PMID 24867953 DOI: 10.1074/Jbc.M114.560680 |
0.539 |
|
| 2014 |
Gimenez LE, Babilon S, Wanka L, Beck-Sickinger AG, Gurevich VV. Mutations in arrestin-3 differentially affect binding to neuropeptide Y receptor subtypes. Cellular Signalling. 26: 1523-31. PMID 24686081 DOI: 10.1016/J.Cellsig.2014.03.019 |
0.451 |
|
| 2014 |
Gurevich VV, Gurevich EV. Extensive shape shifting underlies functional versatility of arrestins. Current Opinion in Cell Biology. 27: 1-9. PMID 24680424 DOI: 10.1016/J.Ceb.2013.10.007 |
0.535 |
|
| 2014 |
Gurevich VV, Gurevich EV. Arrestin makes T cells stop and become active. The Embo Journal. 33: 531-3. PMID 24502974 DOI: 10.1002/Embj.201387724 |
0.362 |
|
| 2014 |
Zhan X, Perez A, Gimenez LE, Vishnivetskiy SA, Gurevich VV. Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains. Cellular Signalling. 26: 766-76. PMID 24412749 DOI: 10.1016/J.Cellsig.2014.01.001 |
0.457 |
|
| 2014 |
Zhan X, Kook S, Gurevich EV, Gurevich VV. Arrestin-dependent activation of JNK family kinases Handbook of Experimental Pharmacology. 219: 259-280. PMID 24292834 DOI: 10.1007/978-3-642-41199-1_13 |
0.516 |
|
| 2014 |
Gimenez LE, Vishnivetskiy SA, Gurevich VV. Targeting individual GPCRs with redesigned nonvisual arrestins. Handbook of Experimental Pharmacology. 219: 153-70. PMID 24292829 DOI: 10.1007/978-3-642-41199-1_8 |
0.56 |
|
| 2014 |
Gurevich VV, Song X, Vishnivetskiy SA, Gurevich EV. Enhanced phosphorylation-independent arrestins and gene therapy. Handbook of Experimental Pharmacology. 219: 133-52. PMID 24292828 DOI: 10.1007/978-3-642-41199-1_7 |
0.461 |
|
| 2014 |
Gurevich EV, Gurevich VV. Therapeutic potential of small molecules and engineered proteins. Handbook of Experimental Pharmacology. 219: 1-12. PMID 24292822 DOI: 10.1007/978-3-642-41199-1_1 |
0.387 |
|
| 2014 |
Kook S, Zhan X, Cleghorn WM, Benovic JL, Gurevich VV, Gurevich EV. Caspase-cleaved arrestin-2 and BID cooperatively facilitate cytochrome C release and cell death Cell Death and Differentiation. 21: 172-184. PMID 24141717 DOI: 10.1038/Cdd.2013.143 |
0.386 |
|
| 2013 |
Kook S, Zhan X, Kaoud TS, Dalby KN, Gurevich VV, Gurevich EV. Arrestin-3 binds c-Jun N-terminal kinase 1 (JNK1) and JNK2 and facilitates the activation of these ubiquitous JNK isoforms in cells via scaffolding. The Journal of Biological Chemistry. 288: 37332-42. PMID 24257757 DOI: 10.1074/Jbc.M113.510412 |
0.454 |
|
| 2013 |
Song X, Seo J, Baameur F, Vishnivetskiy SA, Chen Q, Kook S, Kim M, Brooks EK, Altenbach C, Hong Y, Hanson SM, Palazzo MC, Chen J, Hubbell WL, Gurevich EV, ... Gurevich VV, et al. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant. Cellular Signalling. 25: 2613-24. PMID 24012956 DOI: 10.1016/J.Cellsig.2013.08.022 |
0.403 |
|
| 2013 |
Zhan X, Kaoud TS, Kook S, Dalby KN, Gurevich VV. JNK3 enzyme binding to arrestin-3 differentially affects the recruitment of upstream mitogen-activated protein (MAP) kinase kinases. The Journal of Biological Chemistry. 288: 28535-47. PMID 23960075 DOI: 10.1074/Jbc.M113.508085 |
0.499 |
|
| 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 |
0.505 |
|
| 2013 |
Gurevich VV, Gurevich EV. Structural determinants of arrestin functions. Progress in Molecular Biology and Translational Science. 118: 57-92. PMID 23764050 DOI: 10.1016/B978-0-12-394440-5.00003-6 |
0.518 |
|
| 2013 |
Moaven H, Koike Y, Jao CC, Gurevich VV, Langen R, Chen J. Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina. Proceedings of the National Academy of Sciences of the United States of America. 110: 9463-8. PMID 23690606 DOI: 10.1073/Pnas.1301126110 |
0.518 |
|
| 2013 |
Singhal A, Ostermaier MK, Vishnivetskiy SA, Panneels V, Homan KT, Tesmer JJ, Veprintsev D, Deupi X, Gurevich VV, Schertler GF, Standfuss J. Insights into congenital stationary night blindness based on the structure of G90D rhodopsin. Embo Reports. 14: 520-6. PMID 23579341 DOI: 10.1038/Embor.2013.44 |
0.394 |
|
| 2013 |
Vishnivetskiy SA, Baameur F, Findley KR, Gurevich VV. Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. The Journal of Biological Chemistry. 288: 11741-50. PMID 23476014 DOI: 10.1074/Jbc.M113.450031 |
0.46 |
|
| 2013 |
Zhuang T, Chen Q, Cho MK, Vishnivetskiy SA, Iverson TM, Gurevich VV, Sanders CR. Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 110: 942-7. PMID 23277586 DOI: 10.1073/Pnas.1215176110 |
0.657 |
|
| 2013 |
Vishnivetskiy SA, Chen Q, Palazzo MC, Brooks EK, Altenbach C, Iverson TM, Hubbell WL, Gurevich VV. Engineering visual arrestin-1 with special functional characteristics. The Journal of Biological Chemistry. 288: 3394-405. PMID 23250748 DOI: 10.1074/Jbc.M112.445437 |
0.699 |
|
| 2013 |
Chen YJ, Oldfield S, Butcher AJ, Tobin AB, Saxena K, Gurevich VV, Benovic JL, Henderson G, Kelly E. Identification of phosphorylation sites in the COOH-terminal tail of the μ-opioid receptor. Journal of Neurochemistry. 124: 189-99. PMID 23106126 DOI: 10.1111/Jnc.12071 |
0.466 |
|
| 2012 |
Kim M, Vishnivetskiy SA, Van Eps N, Alexander NS, Cleghorn WM, Zhan X, Hanson SM, Morizumi T, Ernst OP, Meiler J, Gurevich VV, Hubbell WL. Conformation of receptor-bound visual arrestin. Proceedings of the National Academy of Sciences of the United States of America. 109: 18407-12. PMID 23091036 DOI: 10.1073/Pnas.1216304109 |
0.432 |
|
| 2012 |
Schattauer SS, Miyatake M, Shankar H, Zietz C, Levin JR, Liu-Chen LY, Gurevich VV, Rieder MJ, Chavkin C. Ligand directed signaling differences between rodent and human κ-opioid receptors. The Journal of Biological Chemistry. 287: 41595-607. PMID 23086943 DOI: 10.1074/Jbc.M112.381368 |
0.486 |
|
| 2012 |
Gimenez LE, Vishnivetskiy SA, Baameur F, Gurevich VV. Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins. The Journal of Biological Chemistry. 287: 29495-505. PMID 22787152 DOI: 10.1074/Jbc.M112.366674 |
0.495 |
|
| 2012 |
Gurevich VV, Gurevich EV. Synthetic biology with surgical precision: targeted reengineering of signaling proteins. Cellular Signalling. 24: 1899-908. PMID 22664341 DOI: 10.1016/J.Cellsig.2012.05.012 |
0.407 |
|
| 2012 |
Breitman M, Kook S, Gimenez LE, Lizama BN, Palazzo MC, Gurevich EV, Gurevich VV. Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant. The Journal of Biological Chemistry. 287: 19653-64. PMID 22523077 DOI: 10.1074/Jbc.M112.358192 |
0.506 |
|
| 2012 |
Mushegian A, Gurevich VV, Gurevich EV. The origin and evolution of G protein-coupled receptor kinases. Plos One. 7: e33806. PMID 22442725 DOI: 10.1371/Journal.Pone.0033806 |
0.54 |
|
| 2012 |
Gimenez LE, Kook S, Vishnivetskiy SA, Ahmed MR, Gurevich EV, Gurevich VV. Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors. The Journal of Biological Chemistry. 287: 9028-40. PMID 22275358 DOI: 10.1074/Jbc.M111.311803 |
0.539 |
|
| 2012 |
Aguila B, Coulbault L, Davis A, Marie N, Hasbi A, Le bras F, Tóth G, Borsodi A, Gurevich VV, Jauzac P, Allouche S. ßarrestin1-biased agonism at human δ-opioid receptor by peptidic and alkaloid ligands. Cellular Signalling. 24: 699-707. PMID 22101011 DOI: 10.1016/J.Cellsig.2011.10.018 |
0.473 |
|
| 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 |
0.534 |
|
| 2011 |
Coffa S, Breitman M, Hanson SM, Callaway K, Kook S, Dalby KN, Gurevich VV. The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation. Plos One. 6: e28723. PMID 22174878 DOI: 10.1371/Journal.Pone.0028723 |
0.582 |
|
| 2011 |
Zhan X, Kaoud TS, Dalby KN, Gurevich VV. Nonvisual arrestins function as simple scaffolds assembling the MKK4-JNK3α2 signaling complex. Biochemistry. 50: 10520-9. PMID 22047447 DOI: 10.1021/Bi201506G |
0.504 |
|
| 2011 |
Gurevich VV, Hanson SM, Song X, Vishnivetskiy SA, Gurevich EV. The functional cycle of visual arrestins in photoreceptor cells. Progress in Retinal and Eye Research. 30: 405-30. PMID 21824527 DOI: 10.1016/J.Preteyeres.2011.07.002 |
0.468 |
|
| 2011 |
Cleghorn WM, Tsakem EL, Song X, Vishnivetskiy SA, Seo J, Chen J, Gurevich EV, Gurevich VV. Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery. Plos One. 6: e22797. PMID 21818392 DOI: 10.1371/Journal.Pone.0022797 |
0.309 |
|
| 2011 |
Bychkov ER, Ahmed MR, Gurevich VV, Benovic JL, Gurevich EV. Reduced expression of G protein-coupled receptor kinases in schizophrenia but not in schizoaffective disorder. Neurobiology of Disease. 44: 248-58. PMID 21784156 DOI: 10.1016/J.Nbd.2011.07.009 |
0.349 |
|
| 2011 |
Coffa S, Breitman M, Spiller BW, Gurevich VV. A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding. Biochemistry. 50: 6951-8. PMID 21732673 DOI: 10.1021/Bi200745K |
0.545 |
|
| 2011 |
Seo J, Tsakem EL, Breitman M, Gurevich VV. Identification of arrestin-3-specific residues necessary for JNK3 kinase activation. The Journal of Biological Chemistry. 286: 27894-901. PMID 21715332 DOI: 10.1074/Jbc.M111.260448 |
0.556 |
|
| 2011 |
Vishnivetskiy SA, Gimenez LE, Francis DJ, Hanson SM, Hubbell WL, Klug CS, Gurevich VV. Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. The Journal of Biological Chemistry. 286: 24288-99. PMID 21471193 DOI: 10.1074/Jbc.M110.213835 |
0.552 |
|
| 2011 |
Ahmed MR, Zhan X, Song X, Kook S, Gurevich VV, Gurevich EV. Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination. Biochemistry. 50: 3749-63. PMID 21466165 DOI: 10.1021/Bi200175Q |
0.477 |
|
| 2011 |
Kim M, Hanson SM, Vishnivetskiy SA, Song X, Cleghorn WM, Hubbell WL, Gurevich VV. Robust self-association is a common feature of mammalian visual arrestin-1. Biochemistry. 50: 2235-42. PMID 21288033 DOI: 10.1021/Bi1018607 |
0.309 |
|
| 2011 |
Zhan X, Gimenez LE, Gurevich VV, Spiller BW. Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. Journal of Molecular Biology. 406: 467-78. PMID 21215759 DOI: 10.1016/J.Jmb.2010.12.034 |
0.554 |
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| 2011 |
Song X, Vishnivetskiy SA, Seo J, Chen J, Gurevich EV, Gurevich VV. Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health. Neuroscience. 174: 37-49. PMID 21075174 DOI: 10.1016/J.Neuroscience.2010.11.009 |
0.348 |
|
| 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 |
0.508 |
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| 2010 |
Zhuang T, Vishnivetskiy SA, Gurevich VV, Sanders CR. Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance. Biochemistry. 49: 10473-85. PMID 21050017 DOI: 10.1021/Bi101596G |
0.523 |
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| 2010 |
Walther C, Nagel S, Gimenez LE, Mörl K, Gurevich VV, Beck-Sickinger AG. Ligand-induced internalization and recycling of the human neuropeptide Y2 receptor is regulated by its carboxyl-terminal tail Journal of Biological Chemistry. 285: 41578-41590. PMID 20959467 DOI: 10.1074/Jbc.M110.162156 |
0.46 |
|
| 2010 |
Gurevich VV, Gurevich EV. Custom-designed proteins as novel therapeutic tools? The case of arrestins Expert Reviews in Molecular Medicine. 12. PMID 20412604 DOI: 10.1017/S1462399410001444 |
0.498 |
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| 2010 |
Ahmed MR, Berthet A, Bychkov E, Porras G, Li Q, Bioulac BH, Carl YT, Bloch B, Kook S, Aubert I, Dovero S, Doudnikoff E, Gurevich VV, Gurevich EV, Bezard E. Lentiviral overexpression of GRK6 alleviates L-dopa-induced dyskinesia in experimental Parkinson's disease. Science Translational Medicine. 2: 28ra28. PMID 20410529 DOI: 10.1126/Scitranslmed.3000664 |
0.309 |
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| 2010 |
Shankar H, Michal A, Kern RC, Kang DS, Gurevich VV, Benovic JL. Non-visual arrestins are constitutively associated with the centrosome and regulate centrosome function. The Journal of Biological Chemistry. 285: 8316-29. PMID 20056609 DOI: 10.1074/Jbc.M109.062521 |
0.402 |
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| 2010 |
Shen L, Caruso G, Bisegna P, Andreucci D, Gurevich VV, Hamm HE, DiBenedetto E. Dynamics of mouse rod phototransduction and its sensitivity to variation of key parameters Iet Systems Biology. 4: 12-32. PMID 20001089 DOI: 10.1049/Iet-Syb.2008.0154 |
0.325 |
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| 2010 |
Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, Klug CS, Hubbell WL, Gurevich VV. The role of arrestin alpha-helix I in receptor binding. Journal of Molecular Biology. 395: 42-54. PMID 19883657 DOI: 10.1016/J.Jmb.2009.10.058 |
0.495 |
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| 2009 |
Song X, Vishnivetskiy SA, Gross OP, Emelianoff K, Mendez A, Chen J, Gurevich EV, Burns ME, Gurevich VV. Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation. Current Biology : Cb. 19: 700-5. PMID 19361994 DOI: 10.1016/J.Cub.2009.02.065 |
0.535 |
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| 2009 |
Dinieri JA, Nemeth CL, Parsegian A, Carle T, Gurevich VV, Gurevich E, Neve RL, Nestler EJ, Carlezon WA. Altered sensitivity to rewarding and aversive drugs in mice with inducible disruption of cAMP response element-binding protein function within the nucleus accumbens. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 29: 1855-9. PMID 19211892 DOI: 10.1523/Jneurosci.5104-08.2009 |
0.38 |
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| 2009 |
Song X, Coffa S, Fu H, Gurevich VV. How does arrestin assemble MAPKs into a signaling complex? The Journal of Biological Chemistry. 284: 685-95. PMID 19001375 DOI: 10.1074/Jbc.M806124200 |
0.551 |
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| 2009 |
Lan H, Teeter MM, Gurevich VV, Neve KA. An intracellular loop 2 amino acid residue determines differential binding of arrestin to the dopamine D2 and D3 receptors. Molecular Pharmacology. 75: 19-26. PMID 18820126 DOI: 10.1124/Mol.108.050542 |
0.416 |
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| 2009 |
Lan H, Liu Y, Bell MI, Gurevich VV, Neve KA. A dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin binding. Molecular Pharmacology. 75: 113-23. PMID 18809670 DOI: 10.1124/Mol.108.050534 |
0.492 |
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| 2009 |
Song X, Vishnivetskiy SA, Gross OP, Emelianoff K, Mendez A, Chen J, Gurevich EV, Burns ME, Gurevich VV. Enhanced Arrestin Facilitates Recovery and Protects Rods Lacking Rhodopsin Phosphorylation (DOI:10.1016/j.cub.2009.02.065) Current Biology. 19: 798. DOI: 10.1016/J.Cub.2009.04.050 |
0.331 |
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| 2009 |
DiBenedetto E, Bisegna P, Caruso G, Shen L, Andreucci D, Gurevich V, Hamm HE. Mathematical aspects of Variability and Variability Suppression of the Single Photon Response in Vertebrate Phototransduction Biophysical Journal. 96: 200a. DOI: 10.1016/J.Bpj.2008.12.1073 |
0.398 |
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| 2008 |
Hanson SM, Dawson ES, Francis DJ, Van Eps N, Klug CS, Hubbell WL, Meiler J, Gurevich VV. A model for the solution structure of the rod arrestin tetramer. Structure (London, England : 1993). 16: 924-34. PMID 18547524 DOI: 10.1016/J.Str.2008.03.006 |
0.331 |
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| 2008 |
Gurevich VV, Gurevich EV. Rich tapestry of G protein-coupled receptor signaling and regulatory mechanisms. Molecular Pharmacology. 74: 312-316. PMID 18515421 DOI: 10.1124/Mol.108.049015 |
0.47 |
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| 2008 |
Gurevich VV, Gurevich EV, Cleghorn WM. Arrestins as multi-functional signaling adaptors Handbook of Experimental Pharmacology. 186: 15-37. PMID 18491047 DOI: 10.1007/978-3-540-72843-6_2 |
0.535 |
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| 2008 |
Bisegna P, Caruso G, Andreucci D, Shen L, Gurevich VV, Hamm HE, Dibenedetto E. Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction Biophysical Journal. 94: 3363-3383. PMID 18400950 DOI: 10.1529/Biophysj.107.114058 |
0.334 |
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| 2008 |
Gurevich VV, Gurevich EV. How and why do GPCRs dimerize Trends in Pharmacological Sciences. 29: 234-240. PMID 18384890 DOI: 10.1016/J.Tips.2008.02.004 |
0.504 |
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| 2008 |
Gurevich VV, Gurevich EV. GPCR monomers and oligomers: it takes all kinds Trends in Neurosciences. 31: 74-81. PMID 18199492 DOI: 10.1016/J.Tins.2007.11.007 |
0.459 |
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| 2008 |
Ahmed MR, Gurevich VV, Dalby KN, Benovic JL, Gurevich EV. Haloperidol and clozapine differentially affect the expression of arrestins, receptor kinases, and extracellular signal-regulated kinase activation. The Journal of Pharmacology and Experimental Therapeutics. 325: 276-83. PMID 18178904 DOI: 10.1124/Jpet.107.131987 |
0.473 |
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| 2008 |
Ahmed MR, Bychkov E, Gurevich VV, Benovic JL, Gurevich EV. Altered expression and subcellular distribution of GRK subtypes in the dopamine-depleted rat basal ganglia is not normalized by l-DOPA treatment. Journal of Neurochemistry. 104: 1622-36. PMID 17996024 DOI: 10.1111/J.1471-4159.2007.05104.X |
0.364 |
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| 2008 |
Bychkov ER, Gurevich VV, Joyce JN, Benovic JL, Gurevich EV. Arrestins and two receptor kinases are upregulated in Parkinson's disease with dementia Neurobiology of Aging. 29: 379-396. PMID 17125886 DOI: 10.1016/J.Neurobiolaging.2006.10.012 |
0.408 |
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| 2007 |
Vishnivetskiy SA, Raman D, Wei J, Kennedy MJ, Hurley JB, Gurevich VV. Regulation of arrestin binding by rhodopsin phosphorylation level. The Journal of Biological Chemistry. 282: 32075-83. PMID 17848565 DOI: 10.1074/Jbc.M706057200 |
0.512 |
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| 2007 |
Song X, Gurevich EV, Gurevich VV. Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites. Journal of Neurochemistry. 103: 1053-62. PMID 17680991 DOI: 10.1111/J.1471-4159.2007.04842.X |
0.504 |
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| 2007 |
Hanson SM, Gurevich EV, Vishnivetskiy SA, Ahmed MR, Song X, Gurevich VV. Each rhodopsin molecule binds its own arrestin. Proceedings of the National Academy of Sciences of the United States of America. 104: 3125-8. PMID 17360618 DOI: 10.1073/Pnas.0610886104 |
0.52 |
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| 2007 |
Hanson SM, Cleghorn WM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Nair KS, Slepak VZ, Klug CS, Gurevich VV. Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. Journal of Molecular Biology. 368: 375-87. PMID 17359998 DOI: 10.1016/J.Jmb.2007.02.053 |
0.545 |
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| 2007 |
Hanson SM, Van Eps N, Francis DJ, Altenbach C, Vishnivetskiy SA, Arshavsky VY, Klug CS, Hubbell WL, Gurevich VV. Structure and function of the visual arrestin oligomer. The Embo Journal. 26: 1726-36. PMID 17332750 DOI: 10.1038/Sj.Emboj.7601614 |
0.368 |
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| 2007 |
Cleghorn WM, Hanson SM, Francis DJ, Vishnivetskiy SA, Raman D, Song X, Klug CS, Gurevich VV. Arrestin‐dependent mobilization of signaling proteins to the cytoskeleton The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A613-C |
0.354 |
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| 2007 |
Gurevich VV, Hanson SM, Gurevich EV, Vishnivetskiy SA, Ahmed MR, Song X. Each receptor molecule binds its own arrestin The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A613-B |
0.428 |
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| 2006 |
Wu N, Hanson SM, Francis DJ, Vishnivetskiy SA, Thibonnier M, Klug CS, Shoham M, Gurevich VV. Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins. Journal of Molecular Biology. 364: 955-63. PMID 17054984 DOI: 10.1016/J.Jmb.2006.09.075 |
0.532 |
|
| 2006 |
Gurevich EV, Gurevich VV. Arrestins: ubiquitous regulators of cellular signaling pathways Genome Biology. 7: 236-236. PMID 17020596 DOI: 10.1186/Gb-2006-7-9-236 |
0.531 |
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| 2006 |
Song X, Raman D, Gurevich EV, Vishnivetskiy SA, Gurevich VV. Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm. The Journal of Biological Chemistry. 281: 21491-9. PMID 16737965 DOI: 10.1074/Jbc.M603659200 |
0.527 |
|
| 2006 |
Wu N, Macion-Dazard R, Nithianantham S, Xu Z, Hanson SM, Vishnivetskiy SA, Gurevich VV, Thibonnier M, Shoham M. Soluble mimics of the cytoplasmic face of the human V1-vascular vasopressin receptor bind arrestin2 and calmodulin. Molecular Pharmacology. 70: 249-58. PMID 16574744 DOI: 10.1124/Mol.105.018804 |
0.543 |
|
| 2006 |
Hanson SM, Francis DJ, Vishnivetskiy SA, Kolobova EA, Hubbell WL, Klug CS, Gurevich VV. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proceedings of the National Academy of Sciences of the United States of America. 103: 4900-5. PMID 16547131 DOI: 10.1073/Pnas.0600733103 |
0.491 |
|
| 2006 |
Hanson SM, Francis DJ, Vishnivetskiy SA, Klug CS, Gurevich VV. Visual arrestin binding to microtubules involves a distinct conformational change. The Journal of Biological Chemistry. 281: 9765-72. PMID 16461350 DOI: 10.1074/Jbc.M510738200 |
0.409 |
|
| 2006 |
Gurevich VV, Gurevich EV. The structural basis of arrestin-mediated regulation of G-protein-coupled receptors Pharmacology & Therapeutics. 110: 465-502. PMID 16460808 DOI: 10.1016/J.Pharmthera.2005.09.008 |
0.536 |
|
| 2006 |
Hanson SM, Gurevich VV. The differential engagement of arrestin surface charges by the various functional forms of the receptor. The Journal of Biological Chemistry. 281: 3458-62. PMID 16339758 DOI: 10.1074/Jbc.M512148200 |
0.534 |
|
| 2005 |
Sutton RB, Vishnivetskiy SA, Robert J, Hanson SM, Raman D, Knox BE, Kono M, Navarro J, Gurevich VV. Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. Journal of Molecular Biology. 354: 1069-80. PMID 16289201 DOI: 10.1016/J.Jmb.2005.10.023 |
0.442 |
|
| 2005 |
Carter JM, Gurevich VV, Prossnitz ER, Engen JR. Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry. Journal of Molecular Biology. 351: 865-78. PMID 16045931 DOI: 10.1016/J.Jmb.2005.06.048 |
0.533 |
|
| 2005 |
Nair KS, Hanson SM, Mendez A, Gurevich EV, Kennedy MJ, Shestopalov VI, Vishnivetskiy SA, Chen J, Hurley JB, Gurevich VV, Slepak VZ. Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron. 46: 555-67. PMID 15944125 DOI: 10.1016/J.Neuron.2005.03.023 |
0.378 |
|
| 2005 |
Guigoni C, Aubert I, Li Q, Gurevich VV, Benovic JL, Ferry S, Mach U, Stark H, Leriche L, HÃ¥kansson K, Bioulac BH, Gross CE, Sokoloff P, Fisone G, Gurevich EV, et al. Pathogenesis of levodopa-induced dyskinesia: focus on D1 and D3 dopamine receptors. Parkinsonism & Related Disorders. 11: S25-9. PMID 15885624 DOI: 10.1016/J.Parkreldis.2004.11.005 |
0.359 |
|
| 2005 |
Zhang R, Khoo MS, Wu Y, Yang Y, Grueter CE, Ni G, Price EE, Thiel W, Guatimosim S, Song LS, Madu EC, Shah AN, Vishnivetskaya TA, Atkinson JB, Gurevich VV, et al. Calmodulin kinase II inhibition protects against structural heart disease. Nature Medicine. 11: 409-17. PMID 15793582 DOI: 10.1038/Nm1215 |
0.328 |
|
| 2005 |
Macey TA, Liu Y, Gurevich VV, Neve KA. Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons. Journal of Neurochemistry. 93: 128-34. PMID 15773912 DOI: 10.1111/J.1471-4159.2004.02998.X |
0.394 |
|
| 2005 |
Bezard E, Gross CE, Qin L, Gurevich VV, Benovic JL, Gurevich EV. L-DOPA reverses the MPTP-induced elevation of the arrestin2 and GRK6 expression and enhanced ERK activation in monkey brain. Neurobiology of Disease. 18: 323-35. PMID 15686961 DOI: 10.1016/J.Nbd.2004.10.005 |
0.422 |
|
| 2005 |
Key TA, Vines CM, Wagener BM, Gurevich VV, Sklar LA, Prossnitz ER. Inhibition of chemoattractant N-formyl peptide receptor trafficking by active arrestins. Traffic (Copenhagen, Denmark). 6: 87-99. PMID 15634210 DOI: 10.1111/J.1600-0854.2004.00248.X |
0.455 |
|
| 2004 |
Gurevich EV, Benovic JL, Gurevich VV. Arrestin2 expression selectively increases during neural differentiation. Journal of Neurochemistry. 91: 1404-16. PMID 15584917 DOI: 10.1111/J.1471-4159.2004.02830.X |
0.417 |
|
| 2004 |
Macey TA, Gurevich VV, Neve KA. Preferential Interaction between the dopamine D2 receptor and Arrestin2 in neostriatal neurons. Molecular Pharmacology. 66: 1635-42. PMID 15361545 DOI: 10.1124/Mol.104.001495 |
0.4 |
|
| 2004 |
Nair KS, Hanson SM, Kennedy MJ, Hurley JB, Gurevich VV, Slepak VZ. Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors. The Journal of Biological Chemistry. 279: 41240-8. PMID 15272005 DOI: 10.1074/Jbc.M406768200 |
0.408 |
|
| 2004 |
Gurevich VV, Gurevich EV. The molecular acrobatics of arrestin activation. Trends in Pharmacological Sciences. 25: 105-111. PMID 15102497 DOI: 10.1016/J.Tips.2003.12.008 |
0.56 |
|
| 2004 |
Vishnivetskiy SA, Hosey MM, Benovic JL, Gurevich VV. Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins. The Journal of Biological Chemistry. 279: 1262-8. PMID 14530255 DOI: 10.1074/Jbc.M308834200 |
0.522 |
|
| 2003 |
Gurevich VV, Gurevich EV. The New Face of Active Receptor Bound Arrestin Attracts New Partners Structure. 11: 1037-1042. PMID 12962621 DOI: 10.1016/S0969-2126(03)00184-9 |
0.461 |
|
| 2003 |
Shi M, Bennett TA, Cimino DF, Maestas DC, Foutz TD, Gurevich VV, Sklar LA, Prossnitz ER. Functional capabilities of an N-formyl peptide receptor-G(alpha)(i)(2) fusion protein: assemblies with G proteins and arrestins. Biochemistry. 42: 7283-93. PMID 12809484 DOI: 10.1021/Bi0341657 |
0.499 |
|
| 2003 |
Gray JA, Bhatnagar A, Gurevich VV, Roth BL. The interaction of a constitutively active arrestin with the arrestin-insensitive 5-HT(2A) receptor induces agonist-independent internalization. Molecular Pharmacology. 63: 961-72. PMID 12695524 DOI: 10.1124/Mol.63.5.961 |
0.385 |
|
| 2003 |
Raman D, Osawa S, Gurevich VV, Weiss ER. The interaction with the cytoplasmic loops of rhodopsin plays a crucial role in arrestin activation and binding. Journal of Neurochemistry. 84: 1040-1050. PMID 12603828 DOI: 10.1046/J.1471-4159.2003.01598.X |
0.455 |
|
| 2003 |
Pan L, Gurevich EV, Gurevich VV. The nature of the arrestin-receptor complex determines the ultimate fate of the internalized receptor Journal of Biological Chemistry. 278: 11623-11632. PMID 12525498 DOI: 10.1074/Jbc.M209532200 |
0.516 |
|
| 2003 |
Key TA, Foutz TD, Gurevich VV, Sklar LA, Prossnitz ER. N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity. The Journal of Biological Chemistry. 278: 4041-7. PMID 12424254 DOI: 10.1074/Jbc.M204687200 |
0.555 |
|
| 2002 |
Vishnivetskiy SA, Hirsch JA, Velez MG, Gurevich YV, Gurevich VV. Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge. The Journal of Biological Chemistry. 277: 43961-7. PMID 12215448 DOI: 10.1074/Jbc.M206951200 |
0.52 |
|
| 2002 |
DeGraff JL, Gurevich VV, Benovic JL. The third intracellular loop of alpha 2-adrenergic receptors determines subtype specificity of arrestin interaction. The Journal of Biological Chemistry. 277: 43247-52. PMID 12205092 DOI: 10.1074/Jbc.M207495200 |
0.361 |
|
| 2002 |
Hunzicker-Dunn M, Gurevich VV, Casanova JE, Mukherjee S. ARF6: a newly appreciated player in G protein-coupled receptor desensitization. Febs Letters. 521: 3-8. PMID 12067715 DOI: 10.1016/S0014-5793(02)02822-3 |
0.488 |
|
| 2002 |
Mukherjee S, Gurevich VV, Preninger A, Hamm HE, Bader MF, Fazleabas AT, Birnbaumer L, Hunzicker-Dunn M. Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2. The Journal of Biological Chemistry. 277: 17916-27. PMID 11867621 DOI: 10.1074/Jbc.M110479200 |
0.482 |
|
| 2002 |
Lowe JD, Celver JP, Gurevich VV, Chavkin C. mu-Opioid receptors desensitize less rapidly than delta-opioid receptors due to less efficient activation of arrestin. The Journal of Biological Chemistry. 277: 15729-35. PMID 11861651 DOI: 10.1074/Jbc.M200612200 |
0.451 |
|
| 2002 |
Gurevich EV, Benovic JL, Gurevich VV. Arrestin2 and arrestin3 are differentially expressed in the rat brain during postnatal development Neuroscience. 109: 421-436. PMID 11823056 DOI: 10.1016/S0306-4522(01)00511-5 |
0.423 |
|
| 2002 |
Celver J, Vishnivetskiy SA, Chavkin C, Gurevich VV. Conservation of the phosphate-sensitive elements in the arrestin family of proteins. The Journal of Biological Chemistry. 277: 9043-8. PMID 11782458 DOI: 10.1074/Jbc.M107400200 |
0.548 |
|
| 2002 |
Potter RM, Key TA, Gurevich VV, Sklar LA, Prossnitz ER. Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus. The Journal of Biological Chemistry. 277: 8970-8. PMID 11777932 DOI: 10.1074/Jbc.M111086200 |
0.527 |
|
| 2002 |
Prossnitz ER, Key TA, Potter RM, Gurevich VV, Slkar LA. S2L5 Mechanisms of arrestin interactions with G protein-coupled receptors Seibutsu Butsuri. 42: S12. DOI: 10.2142/Biophys.42.S12_1 |
0.34 |
|
| 2001 |
Bennett TA, Foutz TD, Gurevich VV, Sklar LA, Prossnitz ER. Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding. The Journal of Biological Chemistry. 276: 49195-203. PMID 11602585 DOI: 10.1074/Jbc.M106414200 |
0.55 |
|
| 2001 |
Key TA, Bennett TA, Foutz TD, Gurevich VV, Sklar LA, Prossnitz ER. Regulation of formyl peptide receptor agonist affinity by reconstitution with arrestins and heterotrimeric G proteins. The Journal of Biological Chemistry. 276: 49204-12. PMID 11598142 DOI: 10.1074/Jbc.M109475200 |
0.53 |
|
| 2001 |
Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. Structure (London, England : 1993). 9: 869-80. PMID 11566136 DOI: 10.1016/S0969-2126(01)00644-X |
0.466 |
|
| 2001 |
Bennett TA, Key TA, Gurevich VV, Neubig R, Prossnitz ER, Sklar LA. Real-time analysis of G protein-coupled receptor reconstitution in a solubilized system. The Journal of Biological Chemistry. 276: 22453-60. PMID 11309376 DOI: 10.1074/Jbc.M009679200 |
0.495 |
|
| 2001 |
Celver JP, Lowe J, Kovoor A, Gurevich VV, Chavkin C. Threonine 180 is required for G-protein-coupled receptor kinase 3- and beta-arrestin 2-mediated desensitization of the mu-opioid receptor in Xenopus oocytes. The Journal of Biological Chemistry. 276: 4894-900. PMID 11060299 DOI: 10.1074/Jbc.M007437200 |
0.511 |
|
| 2001 |
Vishnivetskiy SA, Schubert C, Climaco GC, Gurevich YV, Velez MG, Gurevich VV. An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation. The Journal of Biological Chemistry. 275: 41049-57. PMID 11024026 DOI: 10.1074/Jbc.M007159200 |
0.52 |
|
| 2000 |
Mushegian AR, Vishnivetskiy SA, Gurevich VV. Conserved phosphoprotein interaction motif is functionally interchangeable between ataxin-7 and arrestins Biochemistry. 39: 6809-6813. PMID 10841760 DOI: 10.1021/Bi992694Y |
0.451 |
|
| 2000 |
Mukherjee S, Gurevich VV, Jones JCR, Casanova JE, Frank SR, Maizels ET, Bader MF, Kahn RA, Palczewski K, Aktories K, Hunzicker-Dunn M. The ADP ribosylation factor nucleotide exchange factor ARNO promotes β- arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization Proceedings of the National Academy of Sciences of the United States of America. 97: 5901-5906. PMID 10811902 DOI: 10.1073/Pnas.100127097 |
0.484 |
|
| 2000 |
Lee KB, Ptasienski JA, Pals-Rylaarsdam R, Gurevich VV, Hosey MM. Arrestin binding to the M2 muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor Journal of Biological Chemistry. 275: 9284-9289. PMID 10734068 DOI: 10.1074/Jbc.275.13.9284 |
0.513 |
|
| 1999 |
Schubert C, Hirsch JA, Gurevich VV, Engelman DM, Sigler PB, Fleming KG. Visual arrestin activity may be regulated by self-association. The Journal of Biological Chemistry. 274: 21186-90. PMID 10409673 DOI: 10.1074/Jbc.274.30.21186 |
0.465 |
|
| 1999 |
Mukherjee S, Palczewski K, Gurevich VV, Hunzicker-Dunn M. beta-arrestin-dependent desensitization of luteinizing hormone/choriogonadotropin receptor is prevented by a synthetic peptide corresponding to the third intracellular loop of the receptor. The Journal of Biological Chemistry. 274: 12984-9. PMID 10224047 DOI: 10.1074/Jbc.274.19.12984 |
0.417 |
|
| 1999 |
Hirsch JA, Schubert C, Gurevich VV, Sigler PB. The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell. 97: 257-69. PMID 10219246 DOI: 10.1016/S0092-8674(00)80735-7 |
0.512 |
|
| 1999 |
Gelber EI, Kroeze WK, Willins DL, Gray JA, Sinar CA, Hyde EG, Gurevich V, Benovic J, Roth BL. Structure and function of the third intracellular loop of the 5-hydroxytryptamine2A receptor: the third intracellular loop is alpha-helical and binds purified arrestins. Journal of Neurochemistry. 72: 2206-14. PMID 10217304 DOI: 10.1046/J.1471-4159.1999.0722206.X |
0.488 |
|
| 1999 |
Vishnivetskiy SA, Paz CL, Schubert C, Hirsch JA, Sigler PB, Gurevich VV. How does arrestin respond to the phosphorylated state of rhodopsin? The Journal of Biological Chemistry. 274: 11451-4. PMID 10206946 DOI: 10.1074/Jbc.274.17.11451 |
0.532 |
|
| 1999 |
Hosey MM, Pals-Rylaarsdam R, Lee KB, Roseberry AG, Benovic JL, Gurevich VV, Bünemann M. Molecular events associated with the regulation of signaling by M2 muscarinic receptors. Life Sciences. 64: 363-8. PMID 10069497 DOI: 10.1016/S0024-3205(98)00575-X |
0.494 |
|
| 1999 |
Kovoor A, Celver J, Abdryashitov RI, Chavkin C, Gurevich VV. Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells. The Journal of Biological Chemistry. 274: 6831-4. PMID 10066734 DOI: 10.1074/Jbc.274.11.6831 |
0.485 |
|
| 1999 |
Mukherjee S, Palczewski K, Gurevich V, Benovic JL, Banga JP, Hunzicker-Dunn M. A direct role for arrestins in desensitization of the luteinizing hormone/choriogonadotropin receptor in porcine ovarian follicular membranes. Proceedings of the National Academy of Sciences of the United States of America. 96: 493-8. PMID 9892661 DOI: 10.1073/Pnas.96.2.493 |
0.342 |
|
| 1998 |
Gurevich VV. The Selectivity of Visual Arrestin for Light-activated Phosphorhodopsin Is Controlled by Multiple Nonredundant Mechanisms* Journal of Biological Chemistry. 273: 15501-15506. PMID 9624137 DOI: 10.1074/Jbc.273.25.15501 |
0.451 |
|
| 1997 |
Gurevich VV, Pals-Rylaarsdam R, Benovic JL, Hosey MM, Onorato JJ. Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity Journal of Biological Chemistry. 272: 28849-28852. PMID 9360951 DOI: 10.1074/Jbc.272.46.28849 |
0.517 |
|
| 1997 |
Goodman OB, Krupnick JG, Santini F, Gurevich VV, Penn RB, Gagnon AW, Keen JH, Benovic JL. Role of arrestins in G-protein-coupled receptor endocytosis. Advances in Pharmacology (San Diego, Calif.). 42: 429-33. PMID 9327931 DOI: 10.1016/S1054-3589(08)60780-2 |
0.547 |
|
| 1997 |
Pals-Rylaarsdam R, Gurevich VV, Lee KB, Ptasienski JA, Benovic JL, Hosey MM. Internalization of the m2 muscarinic acetylcholine receptor. Arrestin- independent and -dependent pathways Journal of Biological Chemistry. 272: 23682-23689. PMID 9295310 DOI: 10.1074/Jbc.272.38.23682 |
0.469 |
|
| 1997 |
Krupnick JG, Gurevich VV, Benovic JL. Mechanism of quenching of phototransduction: Binding competition between arrestin and transducin for phosphorhodopsin Journal of Biological Chemistry. 272: 18125-18131. PMID 9218446 DOI: 10.1074/Jbc.272.29.18125 |
0.489 |
|
| 1997 |
Gray-Keller MP, Detwiler PB, Benovic JL, Gurevich VV. Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion. Biochemistry. 36: 7058-63. PMID 9188704 DOI: 10.1021/Bi963110K |
0.508 |
|
| 1997 |
Goodman OB, Krupnick JG, Gurevich VV, Benovic JL, Keen JH. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. The Journal of Biological Chemistry. 272: 15017-22. PMID 9169477 DOI: 10.1074/Jbc.272.23.15017 |
0.425 |
|
| 1997 |
Gurevich VV, Benovic JL. Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state Molecular Pharmacology. 51: 161-169. PMID 9016359 DOI: 10.1124/Mol.51.1.161 |
0.473 |
|
| 1996 |
Goodman OB, Krupnick JG, Santini F, Gurevich VV, Penn RB, Gagnon AW, Keen JH, Benovic JL. Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature. 383: 447-50. PMID 8837779 DOI: 10.1038/383447A0 |
0.423 |
|
| 1995 |
Gurevich VV, Benovic JL. Visual arrestin binding to rhodopsin: Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin Journal of Biological Chemistry. 270: 6010-6016. PMID 7890732 DOI: 10.1074/Jbc.270.11.6010 |
0.468 |
|
| 1995 |
Gurevich VV, Dion SB, Onorato JJ, Ptasienski J, Kim CM, Sterne-Marr R, Hosey MM, Benovic JL. Arrestin interactions with G protein-coupled receptors: Direct binding studies of wild type and mutant arrestins with rhodopsin, β2-adrenergic, and m2 muscarinic cholinergic receptors Journal of Biological Chemistry. 270: 720-731. PMID 7822302 DOI: 10.1074/Jbc.270.2.720 |
0.546 |
|
| 1990 |
Zozulya SA, Gurevich VV, Zvyaga TA, Shirokova EP, Dumler IL, Garnovskaya MN, Natochin MY, Shmukler BE, Badalov PR. Functional expression in vitro of bovine visual rhodopsin. Protein Engineering. 3: 453-458. PMID 2140896 DOI: 10.1093/Protein/3.5.453 |
0.351 |
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