Arrestina (Galician Wikipedia)

Analysis of information sources in references of the Wikipedia article "Arrestina" in Galician language version.

refsWebsite

Global rank Galician rank

16doi.org

2^nd place

7^th place

15nih.gov

4^th place

6^th place

6harvard.edu

18^th place

38^th place

1rcsb.org

8,838^th place

735^th place

doi.org

dx.doi.org

PDB 1CF1; Hirsch JA, Schubert C, Gurevich VV, Sigler PB (abril de 1999). "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation". Cell 97 (2): 257–69. PMID 10219246. doi:10.1016/S0092-8674(00)80735-7.
Moore CA, Milano SK, Benovic JL (2007). "Regulation of receptor trafficking by GRKs and arrestins". Annual Review of Physiology 69: 451–82. PMID 17037978. doi:10.1146/annurev.physiol.69.022405.154712.
Lefkowitz RJ, Shenoy SK (abril de 2005). "Transduction of receptor signals by beta-arrestins". Science 308 (5721): 512–7. Bibcode:2005Sci...308..512L. PMID 15845844. doi:10.1126/science.1109237.
Wilden U, Hall SW, Kühn H (marzo de 1986). "Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments". Proceedings of the National Academy of Sciences of the United States of America 83 (5): 1174–8. Bibcode:1986PNAS...83.1174W. PMC 323037. PMID 3006038. doi:10.1073/pnas.83.5.1174.
Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ (xuño de 1990). "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science 248 (4962): 1547–50. Bibcode:1990Sci...248.1547L. PMID 2163110. doi:10.1126/science.2163110.
Gurevich VV, Gurevich EV (xuño de 2006). "The structural basis of arrestin-mediated regulation of G-protein-coupled receptors". Pharmacology & Therapeutics 110 (3): 465–502. PMC 2562282. PMID 16460808. doi:10.1016/j.pharmthera.2005.09.008.
Smith JS, Lefkowitz RJ, Rajagopal S (xaneiro de 2018). "Biased signalling: from simple switches to allosteric microprocessors". Nature Reviews. Drug Discovery 17 (4): 243–260. PMC 5936084. PMID 29302067. doi:10.1038/nrd.2017.229.
Cahill TJ, Thomsen AR, Tarrasch JT, Plouffe B, Nguyen AH, Yang F, et al. (febreiro de 2017). "Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis". Proceedings of the National Academy of Sciences of the United States of America 114 (10): 2562–2567. Bibcode:2017PNAS..114.2562C. PMC 5347553. PMID 28223524. doi:10.1073/pnas.1701529114.
Kumari P, Srivastava A, Banerjee R, Ghosh E, Gupta P, Ranjan R, Chen X, Gupta B, Gupta C, Jaiman D, Shukla AK (November 2016). "Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications 7: 13416. Bibcode:2016NatCo...713416K. PMC 5105198. PMID 27827372. doi:10.1038/ncomms13416.
Kumari P, Srivastava A, Ghosh E, Ranjan R, Dogra S, Yadav PN, Shukla AK (April 2017). "Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation". Molecular Biology of the Cell 28 (8): 1003–10. PMC 5391177. PMID 28228552. doi:10.1091/mbc.E16-12-0818.
Gurevich VV, Gurevich EV (febreiro de 2004). "The molecular acrobatics of arrestin activation". Trends in Pharmacological Sciences 25 (2): 105–11. PMID 15102497. doi:10.1016/j.tips.2003.12.008.
Gurevich EV, Gurevich VV (2006). "Arrestins: ubiquitous regulators of cellular signaling pathways". Genome Biology 7 (9): 236. PMC 1794542. PMID 17020596. doi:10.1186/gb-2006-7-9-236.
Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, et al. (xullo de 2015). "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser". Nature 523 (7562): 561–7. Bibcode:2015Natur.523..561K. PMC 4521999. PMID 26200343. doi:10.1038/nature14656.
Smith JS, Pack TF, et al. (2021). "Noncanonical scaffolding of Gαi and β-arrestin by G protein–coupled receptors". Science 371 (Ahead of print): eaay1833. PMC 8005335. PMID 33479120. doi:10.1126/science.aay1833.
Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C (setembro de 2001). "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation". Structure 9 (9): 869–80. PMID 11566136. doi:10.1016/S0969-2126(01)00644-X.

doi.org

Roman, G., He, J., & Davis, R. L. (2000). kurtz, a novel nonvisual arrestin, is an essential neural gene in Drosophila. Genetics, 155(3), 1281–1295. https://doi.org/10.1093/genetics/155.3.1281

harvard.edu

adsabs.harvard.edu

Lefkowitz RJ, Shenoy SK (abril de 2005). "Transduction of receptor signals by beta-arrestins". Science 308 (5721): 512–7. Bibcode:2005Sci...308..512L. PMID 15845844. doi:10.1126/science.1109237.
Wilden U, Hall SW, Kühn H (marzo de 1986). "Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments". Proceedings of the National Academy of Sciences of the United States of America 83 (5): 1174–8. Bibcode:1986PNAS...83.1174W. PMC 323037. PMID 3006038. doi:10.1073/pnas.83.5.1174.
Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ (xuño de 1990). "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science 248 (4962): 1547–50. Bibcode:1990Sci...248.1547L. PMID 2163110. doi:10.1126/science.2163110.
Cahill TJ, Thomsen AR, Tarrasch JT, Plouffe B, Nguyen AH, Yang F, et al. (febreiro de 2017). "Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis". Proceedings of the National Academy of Sciences of the United States of America 114 (10): 2562–2567. Bibcode:2017PNAS..114.2562C. PMC 5347553. PMID 28223524. doi:10.1073/pnas.1701529114.
Kumari P, Srivastava A, Banerjee R, Ghosh E, Gupta P, Ranjan R, Chen X, Gupta B, Gupta C, Jaiman D, Shukla AK (November 2016). "Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications 7: 13416. Bibcode:2016NatCo...713416K. PMC 5105198. PMID 27827372. doi:10.1038/ncomms13416.
Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, et al. (xullo de 2015). "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser". Nature 523 (7562): 561–7. Bibcode:2015Natur.523..561K. PMC 4521999. PMID 26200343. doi:10.1038/nature14656.

nih.gov

ncbi.nlm.nih.gov

PDB 1CF1; Hirsch JA, Schubert C, Gurevich VV, Sigler PB (abril de 1999). "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation". Cell 97 (2): 257–69. PMID 10219246. doi:10.1016/S0092-8674(00)80735-7.
Moore CA, Milano SK, Benovic JL (2007). "Regulation of receptor trafficking by GRKs and arrestins". Annual Review of Physiology 69: 451–82. PMID 17037978. doi:10.1146/annurev.physiol.69.022405.154712.
Lefkowitz RJ, Shenoy SK (abril de 2005). "Transduction of receptor signals by beta-arrestins". Science 308 (5721): 512–7. Bibcode:2005Sci...308..512L. PMID 15845844. doi:10.1126/science.1109237.
Wilden U, Hall SW, Kühn H (marzo de 1986). "Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments". Proceedings of the National Academy of Sciences of the United States of America 83 (5): 1174–8. Bibcode:1986PNAS...83.1174W. PMC 323037. PMID 3006038. doi:10.1073/pnas.83.5.1174.
Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ (xuño de 1990). "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science 248 (4962): 1547–50. Bibcode:1990Sci...248.1547L. PMID 2163110. doi:10.1126/science.2163110.
Gurevich VV, Gurevich EV (xuño de 2006). "The structural basis of arrestin-mediated regulation of G-protein-coupled receptors". Pharmacology & Therapeutics 110 (3): 465–502. PMC 2562282. PMID 16460808. doi:10.1016/j.pharmthera.2005.09.008.
Smith JS, Lefkowitz RJ, Rajagopal S (xaneiro de 2018). "Biased signalling: from simple switches to allosteric microprocessors". Nature Reviews. Drug Discovery 17 (4): 243–260. PMC 5936084. PMID 29302067. doi:10.1038/nrd.2017.229.
Cahill TJ, Thomsen AR, Tarrasch JT, Plouffe B, Nguyen AH, Yang F, et al. (febreiro de 2017). "Distinct conformations of GPCR-β-arrestin complexes mediate desensitization, signaling, and endocytosis". Proceedings of the National Academy of Sciences of the United States of America 114 (10): 2562–2567. Bibcode:2017PNAS..114.2562C. PMC 5347553. PMID 28223524. doi:10.1073/pnas.1701529114.
Kumari P, Srivastava A, Banerjee R, Ghosh E, Gupta P, Ranjan R, Chen X, Gupta B, Gupta C, Jaiman D, Shukla AK (November 2016). "Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications 7: 13416. Bibcode:2016NatCo...713416K. PMC 5105198. PMID 27827372. doi:10.1038/ncomms13416.
Kumari P, Srivastava A, Ghosh E, Ranjan R, Dogra S, Yadav PN, Shukla AK (April 2017). "Core engagement with β-arrestin is dispensable for agonist-induced vasopressin receptor endocytosis and ERK activation". Molecular Biology of the Cell 28 (8): 1003–10. PMC 5391177. PMID 28228552. doi:10.1091/mbc.E16-12-0818.
Gurevich VV, Gurevich EV (febreiro de 2004). "The molecular acrobatics of arrestin activation". Trends in Pharmacological Sciences 25 (2): 105–11. PMID 15102497. doi:10.1016/j.tips.2003.12.008.
Gurevich EV, Gurevich VV (2006). "Arrestins: ubiquitous regulators of cellular signaling pathways". Genome Biology 7 (9): 236. PMC 1794542. PMID 17020596. doi:10.1186/gb-2006-7-9-236.
Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, et al. (xullo de 2015). "Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser". Nature 523 (7562): 561–7. Bibcode:2015Natur.523..561K. PMC 4521999. PMID 26200343. doi:10.1038/nature14656.
Smith JS, Pack TF, et al. (2021). "Noncanonical scaffolding of Gαi and β-arrestin by G protein–coupled receptors". Science 371 (Ahead of print): eaay1833. PMC 8005335. PMID 33479120. doi:10.1126/science.aay1833.
Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C (setembro de 2001). "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation". Structure 9 (9): 869–80. PMID 11566136. doi:10.1016/S0969-2126(01)00644-X.

rcsb.org

PDB 1CF1; Hirsch JA, Schubert C, Gurevich VV, Sigler PB (abril de 1999). "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation". Cell 97 (2): 257–69. PMID 10219246. doi:10.1016/S0092-8674(00)80735-7.