Arrestin (Indonesian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Arrestin" in Indonesian language version.

refsWebsite

Global rank Indonesian rank

17nih.gov

4^th place

13^th place

12doi.org

2^nd place

4^th place

1rcsb.org

8,838^th place

low place

doi.org (Global: 2^nd place; Indonesian: 4^th place)

PDB: 1CF1; Hirsch JA, Schubert C, Gurevich VV, Sigler PB (April 1999). "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation". Cell. 97 (2): 257–69. doi:10.1016/S0092-8674(00)80735-7. PMID 10219246.
"Regulation of receptor trafficking by GRKs and arrestins". Annual Review of Physiology. 69: 451–82. 2007. doi:10.1146/annurev.physiol.69.022405.154712. PMID 17037978.
"Transduction of receptor signals by beta-arrestins". Science. 308 (5721): 512–7. April 2005. doi:10.1126/science.1109237. PMID 15845844.
"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. March 1986. doi:10.1073/pnas.83.5.1174. PMC 323037. PMID 3006038.
"beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science. 248 (4962): 1547–50. June 1990. doi:10.1126/science.2163110. PMID 2163110.
"The structural basis of arrestin-mediated regulation of G-protein-coupled receptors". Pharmacology & Therapeutics. 110 (3): 465–502. June 2006. doi:10.1016/j.pharmthera.2005.09.008. PMC 2562282. PMID 16460808.
"Biased signalling: from simple switches to allosteric microprocessors". Nature Reviews. Drug Discovery. January 2018. doi:10.1038/nrd.2017.229. PMID 29302067.
"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. February 2017. doi:10.1073/pnas.1701529114. PMC 5347553. PMID 28223524.
"Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications. 7: 13416. November 2016. doi:10.1038/ncomms13416. PMC 5105198. PMID 27827372.
"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. April 2017. doi:10.1091/mbc.E16-12-0818. PMC 5391177. PMID 28228552.
"The molecular acrobatics of arrestin activation". Trends in Pharmacological Sciences. 25 (2): 105–11. February 2004. doi:10.1016/j.tips.2003.12.008. PMID 15102497.
Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C (September 2001). "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation". Structure. 9 (9): 869–80. doi:10.1016/S0969-2126(01)00644-X. PMID 11566136.

nih.gov (Global: 4^th place; Indonesian: 13^th place)

pubmed.ncbi.nlm.nih.gov

PDB: 1CF1; Hirsch JA, Schubert C, Gurevich VV, Sigler PB (April 1999). "The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation". Cell. 97 (2): 257–69. doi:10.1016/S0092-8674(00)80735-7. PMID 10219246.
"Regulation of receptor trafficking by GRKs and arrestins". Annual Review of Physiology. 69: 451–82. 2007. doi:10.1146/annurev.physiol.69.022405.154712. PMID 17037978.
"Transduction of receptor signals by beta-arrestins". Science. 308 (5721): 512–7. April 2005. doi:10.1126/science.1109237. PMID 15845844.
"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. March 1986. doi:10.1073/pnas.83.5.1174. PMC 323037. PMID 3006038.
"beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science. 248 (4962): 1547–50. June 1990. doi:10.1126/science.2163110. PMID 2163110.
"The structural basis of arrestin-mediated regulation of G-protein-coupled receptors". Pharmacology & Therapeutics. 110 (3): 465–502. June 2006. doi:10.1016/j.pharmthera.2005.09.008. PMC 2562282. PMID 16460808.
"Biased signalling: from simple switches to allosteric microprocessors". Nature Reviews. Drug Discovery. January 2018. doi:10.1038/nrd.2017.229. PMID 29302067.
"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. February 2017. doi:10.1073/pnas.1701529114. PMC 5347553. PMID 28223524.
"Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications. 7: 13416. November 2016. doi:10.1038/ncomms13416. PMC 5105198. PMID 27827372.
"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. April 2017. doi:10.1091/mbc.E16-12-0818. PMC 5391177. PMID 28228552.
"The molecular acrobatics of arrestin activation". Trends in Pharmacological Sciences. 25 (2): 105–11. February 2004. doi:10.1016/j.tips.2003.12.008. PMID 15102497.
Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C (September 2001). "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation". Structure. 9 (9): 869–80. doi:10.1016/S0969-2126(01)00644-X. PMID 11566136.

ncbi.nlm.nih.gov

"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. March 1986. doi:10.1073/pnas.83.5.1174. PMC 323037. PMID 3006038.
"The structural basis of arrestin-mediated regulation of G-protein-coupled receptors". Pharmacology & Therapeutics. 110 (3): 465–502. June 2006. doi:10.1016/j.pharmthera.2005.09.008. PMC 2562282. PMID 16460808.
"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. February 2017. doi:10.1073/pnas.1701529114. PMC 5347553. PMID 28223524.
"Functional competence of a partially engaged GPCR-β-arrestin complex". Nature Communications. 7: 13416. November 2016. doi:10.1038/ncomms13416. PMC 5105198. PMID 27827372.
"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. April 2017. doi:10.1091/mbc.E16-12-0818. PMC 5391177. PMID 28228552.

rcsb.org (Global: 8,838^th place; Indonesian: low place)

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

Arrestin (Indonesian Wikipedia)

doi.org (Global: 2nd place; Indonesian: 4th place)

nih.gov (Global: 4th place; Indonesian: 13th place)

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

rcsb.org (Global: 8,838th place; Indonesian: low place)

doi.org (Global: 2^nd place; Indonesian: 4^th place)

nih.gov (Global: 4^th place; Indonesian: 13^th place)

rcsb.org (Global: 8,838^th place; Indonesian: low place)