Journal articles on the topic 'Arrestin Proteins'
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JAHNS, Roland, Franck BORGESE, Sabine LINDENTHAL, Annette STRAUB, René MOTAIS, and Bruno FIÉVET. "Trout red blood cell arrestin (TRCarr), a novel member of the arrestin family: cloning, immunoprecipitation and expression of recombinant TRCarr." Biochemical Journal 316, no. 2 (June 1, 1996): 497–506. http://dx.doi.org/10.1042/bj3160497.
Full textBecuwe, Michel, Antonio Herrador, Rosine Haguenauer-Tsapis, Olivier Vincent, and Sébastien Léon. "Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family." Biochemistry Research International 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/242764.
Full textMorris, Gavin E., Carl P. Nelson, Paul J. Brighton, Nicholas B. Standen, R. A. John Challiss, and Jonathon M. Willets. "Arrestins 2 and 3 differentially regulate ETA and P2Y2 receptor-mediated cell signaling and migration in arterial smooth muscle." American Journal of Physiology-Cell Physiology 302, no. 5 (March 1, 2012): C723—C734. http://dx.doi.org/10.1152/ajpcell.00202.2011.
Full textSpillmann, Martin, Larissa Thurner, Nina Romantini, Mirjam Zimmermann, Benoit Meger, Martin Behe, Maria Waldhoer, Gebhard F. X. Schertler, and Philipp Berger. "New Insights into Arrestin Recruitment to GPCRs." International Journal of Molecular Sciences 21, no. 14 (July 13, 2020): 4949. http://dx.doi.org/10.3390/ijms21144949.
Full textWess, Jürgen. "The Two β-Arrestins Regulate Distinct Metabolic Processes: Studies with Novel Mutant Mouse Models." International Journal of Molecular Sciences 23, no. 1 (January 2, 2022): 495. http://dx.doi.org/10.3390/ijms23010495.
Full textGurevich, Vsevolod V., and Eugenia V. Gurevich. "Solo vs Chorus: Monomers and Oligomers of Arrestin Proteins." International Journal of Molecular Sciences 23, no. 13 (June 29, 2022): 7253. http://dx.doi.org/10.3390/ijms23137253.
Full textVishnivetskiy, Sergey A., Luis E. Gimenez, Derek J. Francis, Susan M. Hanson, Wayne L. Hubbell, Candice S. Klug, and Vsevolod V. Gurevich. "Few Residues within an Extensive Binding Interface Drive Receptor Interaction and Determine the Specificity of Arrestin Proteins." Journal of Biological Chemistry 286, no. 27 (April 6, 2011): 24288–99. http://dx.doi.org/10.1074/jbc.m110.213835.
Full textZbieralski, Kacper, and Donata Wawrzycka. "α-Arrestins and Their Functions: From Yeast to Human Health." International Journal of Molecular Sciences 23, no. 9 (April 30, 2022): 4988. http://dx.doi.org/10.3390/ijms23094988.
Full textSeyedabadi, Mohammad, Mehdi Gharghabi, Eugenia V. Gurevich, and Vsevolod V. Gurevich. "Receptor-Arrestin Interactions: The GPCR Perspective." Biomolecules 11, no. 2 (February 4, 2021): 218. http://dx.doi.org/10.3390/biom11020218.
Full textCao, Yubo, Sahil Kumar, Yoon Namkung, Laurence Gagnon, Aaron Cho, and Stéphane A. Laporte. "Angiotensin II type 1 receptor variants alter endosomal receptor–β-arrestin complex stability and MAPK activation." Journal of Biological Chemistry 295, no. 38 (July 23, 2020): 13169–80. http://dx.doi.org/10.1074/jbc.ra120.014330.
Full textBorshchevskiy, Valentin, and Georg Büldt. "Active arrestin proteins crystallized." Nature 497, no. 7447 (April 24, 2013): 45–46. http://dx.doi.org/10.1038/nature12096.
Full textQu, Changxiu, Ji Young Park, Min Woo Yun, Qing-tao He, Fan Yang, Kiae Kim, Donghee Ham, et al. "Scaffolding mechanism of arrestin-2 in the cRaf/MEK1/ERK signaling cascade." Proceedings of the National Academy of Sciences 118, no. 37 (September 10, 2021): e2026491118. http://dx.doi.org/10.1073/pnas.2026491118.
Full textZarca, Aurélien, Claudia Perez, Jelle van den Bor, Jan Paul Bebelman, Joyce Heuninck, Rianna J. F. de Jonker, Thierry Durroux, Henry F. Vischer, Marco Siderius, and Martine J. Smit. "Differential Involvement of ACKR3 C-Tail in β-Arrestin Recruitment, Trafficking and Internalization." Cells 10, no. 3 (March 11, 2021): 618. http://dx.doi.org/10.3390/cells10030618.
Full textMorales, Paula, Marta Bruix, and M. Angeles Jiménez. "Structural Insights into β-arrestin/CB1 Receptor Interaction: NMR and CD Studies on Model Peptides." International Journal of Molecular Sciences 21, no. 21 (October 30, 2020): 8111. http://dx.doi.org/10.3390/ijms21218111.
Full textKarnam, Preethi C., Sergey A. Vishnivetskiy, and Vsevolod V. Gurevich. "Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors." International Journal of Molecular Sciences 22, no. 22 (November 19, 2021): 12481. http://dx.doi.org/10.3390/ijms222212481.
Full textKleist, Andrew B., Shawn Jenjak, Andrija Sente, Lauren J. Laskowski, Martyna Szpakowska, Maggie M. Calkins, Emilie I. Anderson, et al. "Conformational selection guides β-arrestin recruitment at a biased G protein–coupled receptor." Science 377, no. 6602 (July 8, 2022): 222–28. http://dx.doi.org/10.1126/science.abj4922.
Full textStaus, Dean P., Laura M. Wingler, Minjung Choi, Biswaranjan Pani, Aashish Manglik, Andrew C. Kruse, and Robert J. Lefkowitz. "Sortase ligation enables homogeneous GPCR phosphorylation to reveal diversity in β-arrestin coupling." Proceedings of the National Academy of Sciences 115, no. 15 (March 26, 2018): 3834–39. http://dx.doi.org/10.1073/pnas.1722336115.
Full textPydi, Sai P., Luiz F. Barella, Lu Zhu, Jaroslawna Meister, Mario Rossi, and Jürgen Wess. "β-Arrestins as Important Regulators of Glucose and Energy Homeostasis." Annual Review of Physiology 84, no. 1 (February 10, 2022): 17–40. http://dx.doi.org/10.1146/annurev-physiol-060721-092948.
Full textWang, Yandao, Jieli Huang, Xi Liu, Yangyang Niu, Liqin Zhao, Ying Yu, Li Zhou, Limin Lu, and Chen Yu. "β-Arrestin-biased AT1R stimulation promotes extracellular matrix synthesis in renal fibrosis." American Journal of Physiology-Renal Physiology 313, no. 1 (July 1, 2017): F1—F8. http://dx.doi.org/10.1152/ajprenal.00588.2016.
Full textGolan, Moran, Gabriel Schreiber, and Sofia Avissar. "Antidepressant-induced differential ubiquitination of β-arrestins 1 and 2 in mononuclear leucocytes of patients with depression." International Journal of Neuropsychopharmacology 16, no. 8 (September 1, 2013): 1745–54. http://dx.doi.org/10.1017/s1461145713000291.
Full textChompunud Na Ayudhya, Chalatip, Aetas Amponnawarat, and Hydar Ali. "Substance P Serves as a Balanced Agonist for MRGPRX2 and a Single Tyrosine Residue Is Required for β-Arrestin Recruitment and Receptor Internalization." International Journal of Molecular Sciences 22, no. 10 (May 18, 2021): 5318. http://dx.doi.org/10.3390/ijms22105318.
Full textGomez-Raja, Jonathan, and Dana A. Davis. "The β-Arrestin-Like Protein Rim8 Is Hyperphosphorylated and Complexes with Rim21 and Rim101 To Promote Adaptation to Neutral-Alkaline pH." Eukaryotic Cell 11, no. 5 (March 16, 2012): 683–93. http://dx.doi.org/10.1128/ec.05211-11.
Full textZaccor, Nicholas W., Charlotte J. Sumner, and Solomon H. Snyder. "The nonselective cation channel TRPV4 inhibits angiotensin II receptors." Journal of Biological Chemistry 295, no. 29 (June 3, 2020): 9986–97. http://dx.doi.org/10.1074/jbc.ra120.014325.
Full textMiranda, Connie Jaqueline, Nicole Fernandez, Nader Kamel, Daniel Turner, Del Benzenhafer, Susan N. Bolch, Jacob T. Andring, Robert McKenna, and W. Clay Smith. "An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1." Journal of Biological Chemistry 295, no. 19 (April 1, 2020): 6498–508. http://dx.doi.org/10.1074/jbc.ra120.013043.
Full textHolliday, Nicholas D., Birgitte Holst, Elena A. Rodionova, Thue W. Schwartz, and Helen M. Cox. "Importance of Constitutive Activity and Arrestin-Independent Mechanisms for Intracellular Trafficking of the Ghrelin Receptor." Molecular Endocrinology 21, no. 12 (December 1, 2007): 3100–3112. http://dx.doi.org/10.1210/me.2007-0254.
Full textWillets, Jonathon M., Craig A. Nash, Richard D. Rainbow, Carl P. Nelson, and R. A. John Challiss. "Defining the roles of arrestin2 and arrestin3 in vasoconstrictor receptor desensitization in hypertension." American Journal of Physiology-Cell Physiology 309, no. 3 (August 1, 2015): C179—C189. http://dx.doi.org/10.1152/ajpcell.00079.2015.
Full textLuttrell, Louis M., and Robert J. Lefkowitz. "The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals." Journal of Cell Science 115, no. 3 (February 1, 2002): 455–65. http://dx.doi.org/10.1242/jcs.115.3.455.
Full textParameswaran, Narayanan, Babu Gonipeta, Sitaram Parvataneni, Nandakumar Packiriswamy, and Deepika Sharma. "β-arrestin-1 negatively regulates inflammatory response to polymicrobial sepsis in mice (110.11)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 110.11. http://dx.doi.org/10.4049/jimmunol.186.supp.110.11.
Full textNeill, Jimmy D., L. Wayne Duck, Lois C. Musgrove, and Jeffrey C. Sellers. "Potential Regulatory Roles for G Protein-Coupled Receptor Kinases and β-Arrestins in Gonadotropin-Releasing Hormone Receptor Signaling*." Endocrinology 139, no. 4 (April 1, 1998): 1781–88. http://dx.doi.org/10.1210/endo.139.4.5868.
Full textXu, H. Eric. "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C567. http://dx.doi.org/10.1107/s2053273314094327.
Full textFerguson, SSG, J. Zhang, LS Barak, and MG Caron. "Pleiotropic Role for GRKs and b-Arrestins in Receptor Regulation." Physiology 12, no. 4 (August 1, 1997): 145–52. http://dx.doi.org/10.1152/physiologyonline.1997.12.4.145.
Full textXiong, Xinyu, Nour Nazo, Ritika Revoori, Sudarshan Rajagopal, and Matthew A. Sparks. "G protein- and β-arrestin Signaling Profiles of Endothelin Derivatives at the Type A Endothelin Receptor." Kidney360 2, no. 7 (May 17, 2021): 1124–31. http://dx.doi.org/10.34067/kid.0005462020.
Full textCraft, C. M., and D. H. Whitmore. "Arrestin (S-antigen) proteins constitute a multigene family of regulatory proteins." Experimental Eye Research 55 (September 1992): 58. http://dx.doi.org/10.1016/0014-4835(92)90419-s.
Full textBowman, Ray W., Eric M. Jordahl, Sydnie Davis, Stefanie Hedayati, Hannah Barsouk, Nejla Ozbaki-Yagan, Annette Chiang, Yang Li, and Allyson F. O’Donnell. "TORC1 Signaling Controls the Stability and Function of α-Arrestins Aly1 and Aly2." Biomolecules 12, no. 4 (March 31, 2022): 533. http://dx.doi.org/10.3390/biom12040533.
Full textMancini, Arturo D., Gyslaine Bertrand, Kevin Vivot, Éric Carpentier, Caroline Tremblay, Julien Ghislain, Michel Bouvier, and Vincent Poitout. "β-Arrestin Recruitment and Biased Agonism at Free Fatty Acid Receptor 1." Journal of Biological Chemistry 290, no. 34 (July 8, 2015): 21131–40. http://dx.doi.org/10.1074/jbc.m115.644450.
Full textHerranz, S., J. M. Rodriguez, H. J. Bussink, J. C. Sanchez-Ferrero, H. N. Arst, M. A. Penalva, and O. Vincent. "Arrestin-related proteins mediate pH signaling in fungi." Proceedings of the National Academy of Sciences 102, no. 34 (August 11, 2005): 12141–46. http://dx.doi.org/10.1073/pnas.0504776102.
Full textGurevich, Vsevolod V., and Eugenia V. Gurevich. "Arrestins and G proteins in cellular signaling: The coin has two sides." Science Signaling 11, no. 549 (September 25, 2018): eaav1646. http://dx.doi.org/10.1126/scisignal.aav1646.
Full textKaya, Ali I., Nicole A. Perry, Vsevolod V. Gurevich, and T. M. Iverson. "Phosphorylation barcode-dependent signal bias of the dopamine D1 receptor." Proceedings of the National Academy of Sciences 117, no. 25 (June 5, 2020): 14139–49. http://dx.doi.org/10.1073/pnas.1918736117.
Full textBenovic, Jeffrey L. "Historical Perspective of the G Protein-Coupled Receptor Kinase Family." Cells 10, no. 3 (March 4, 2021): 555. http://dx.doi.org/10.3390/cells10030555.
Full textKimura, Tohru, Patrick B. Allen, Angus C. Nairn, and Michael J. Caplan. "Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase." Molecular Biology of the Cell 18, no. 11 (November 2007): 4508–18. http://dx.doi.org/10.1091/mbc.e06-08-0711.
Full textShenoy, S. K., and R. J. Lefkowitz. "Angiotensin II-Stimulated Signaling Through G Proteins and -Arrestin." Science Signaling 2005, no. 311 (November 15, 2005): cm14. http://dx.doi.org/10.1126/stke.3112005cm14.
Full textBolger, Graeme B., George S. Baillie, Xiang Li, Martin J. Lynch, Pawel Herzyk, Ahmed Mohamed, Lisa High Mitchell, et al. "Scanning peptide array analyses identify overlapping binding sites for the signalling scaffold proteins, β-arrestin and RACK1, in cAMP-specific phosphodiesterase PDE4D5." Biochemical Journal 398, no. 1 (July 27, 2006): 23–36. http://dx.doi.org/10.1042/bj20060423.
Full textKang, Dong Soo, Xufan Tian, and Jeffrey L. Benovic. "Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking." Current Opinion in Cell Biology 27 (April 2014): 63–71. http://dx.doi.org/10.1016/j.ceb.2013.11.005.
Full textNogueras-Ortiz, Carlos, Cristina Roman-Vendrell, Gabriel E. Mateo-Semidey, Yu-Hsien Liao, Debra A. Kendall, and Guillermo A. Yudowski. "Retromer stops beta-arrestin 1–mediated signaling from internalized cannabinoid 2 receptors." Molecular Biology of the Cell 28, no. 24 (November 15, 2017): 3554–61. http://dx.doi.org/10.1091/mbc.e17-03-0198.
Full textKim, Jihee, Chad A. Grotegut, James W. Wisler, Lan Mao, Paul B. Rosenberg, Howard A. Rockman, and Robert J. Lefkowitz. "The β-arrestin-biased β-adrenergic receptor blocker carvedilol enhances skeletal muscle contractility." Proceedings of the National Academy of Sciences 117, no. 22 (May 15, 2020): 12435–43. http://dx.doi.org/10.1073/pnas.1920310117.
Full textPeterson, Sean M., Thomas F. Pack, Angela D. Wilkins, Nikhil M. Urs, Daniel J. Urban, Caroline E. Bass, Olivier Lichtarge, and Marc G. Caron. "Elucidation of G-protein and β-arrestin functional selectivity at the dopamine D2 receptor." Proceedings of the National Academy of Sciences 112, no. 22 (May 11, 2015): 7097–102. http://dx.doi.org/10.1073/pnas.1502742112.
Full textKendall, Ryan T., Erik G. Strungs, Saleh M. Rachidi, Mi-Hye Lee, Hesham M. El-Shewy, Deirdre K. Luttrell, Michael G. Janech, and Louis M. Luttrell. "The β-Arrestin Pathway-selective Type 1A Angiotensin Receptor (AT1A) Agonist [Sar1,Ile4,Ile8]Angiotensin II Regulates a Robust G Protein-independent Signaling Network." Journal of Biological Chemistry 286, no. 22 (April 18, 2011): 19880–91. http://dx.doi.org/10.1074/jbc.m111.233080.
Full textLabasque, Marilyne, Eric Reiter, Carine Becamel, Joël Bockaert, and Philippe Marin. "Physical Interaction of Calmodulin with the 5-Hydroxytryptamine2C Receptor C-Terminus Is Essential for G Protein-independent, Arrestin-dependent Receptor Signaling." Molecular Biology of the Cell 19, no. 11 (November 2008): 4640–50. http://dx.doi.org/10.1091/mbc.e08-04-0422.
Full textEishingdrelo, Haifeng, Wei Sun, Hua Li, Li Wang, Alex Eishingdrelo, Sheng Dai, John C. McKew, and Wei Zheng. "ERK and β-Arrestin Interaction." Journal of Biomolecular Screening 20, no. 3 (October 31, 2014): 341–49. http://dx.doi.org/10.1177/1087057114557233.
Full textPerry, Nicole A., Tamer S. Kaoud, Oscar O. Ortega, Ali I. Kaya, David J. Marcus, John M. Pleinis, Sandra Berndt, et al. "Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification." Proceedings of the National Academy of Sciences 116, no. 3 (December 27, 2018): 810–15. http://dx.doi.org/10.1073/pnas.1819230116.
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