オプシン (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "オプシン" in Japanese language version.

refsWebsite

Global rank Japanese rank

28nih.gov

4^th place

24^th place

21doi.org

2^nd place

6^th place

13harvard.edu

18^th place

107^th place

1kobe-u.ac.jp

low place

951^st place

1kotobank.jp

178^th place

12^th place

doi.org

“G protein involvement in receptor-effector coupling”. The Journal of Biological Chemistry 263 (6): 2577–2580. (February 1988). doi:10.1016/s0021-9258(18)69103-3. PMID 2830256.
“Fingerprinting G-protein-coupled receptors”. Protein Engineering 7 (2): 195–203. (February 1994). doi:10.1093/protein/7.2.195. PMID 8170923.
“Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin”. Nature 321 (6065): 75–79. (May 1986). Bibcode: 1986Natur.321...75D. doi:10.1038/321075a0. PMID 30101326
“Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core”. Nature 326 (6108): 73–77. (March 1987). Bibcode: 1987Natur.326...73D. doi:10.1038/326073a0. PMID 2881211.
“Carotenoids and the Vitamin A Cycle in Vision”. Nature 134 (3376): 65. (July 1934). Bibcode: 1934Natur.134...65W. doi:10.1038/134065a0.
“Hindered Cis Isomers of Vitamin a and Retinene: The Structure of the Neo-B Isomer”. Proceedings of the National Academy of Sciences of the United States of America 41 (7): 438–451. (July 1955). Bibcode: 1955PNAS...41..438W. doi:10.1073/pnas.41.7.438. PMC 528115. PMID 16589696.
“The neo-b isomer of vitamin A and retinene”. The Journal of Biological Chemistry 222 (2): 865–877. (October 1956). doi:10.1016/S0021-9258(20)89944-X. PMID 13367054.
“The Synthesis and Configuration of Neo-B Vitamin A and Neoretinine b”. Journal of the American Chemical Society 78 (11): 2651–2652. (June 1956). doi:10.1021/ja01592a095.
“HINDERED CIS ISOMERS OF VITAMIN A AND RETINENE: THE STRUCTURE OF THE NEO-b ISOMER”. Proceedings of the National Academy of Sciences of the United States of America 42 (9): 578–580. (September 1956). Bibcode: 1956PNAS...42..578O. doi:10.1073/pnas.42.9.578. PMC 534254. PMID 16589909.
“The structure of bovine rhodopsin”. Biophysics of Structure and Mechanism 9 (4): 235–244. (1983). doi:10.1007/BF00535659. PMID 63426916
“Crystal structure of rhodopsin: A G protein-coupled receptor”. Science 289 (5480): 739–745. (August 2000). Bibcode: 2000Sci...289..739P. doi:10.1126/science.289.5480.739. PMID 109265286
“Crystal structure of squid rhodopsin”. Nature 453 (7193): 363–367. (May 2008). Bibcode: 2008Natur.453..363M. doi:10.1038/nature06925. PMID 18480818.
“Site of attachment of retinal in rhodopsin”. Nature 216 (5121): 1178–1181. (December 1967). Bibcode: 1967Natur.216.1178B. doi:10.1038/2161178a0. PMID 4294735.
“Rhodopsin and indicator yellow”. Nature 171 (4350): 469–471. (March 1953). Bibcode: 1953Natur.171..469C. doi:10.1038/171469a0. PMID 13046517.
“Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue”. The Biochemical Journal 59 (1): 122–128. (January 1955). doi:10.1042/bj0590122. PMC 1216098. PMID 14351151.
“The Action of Light on Rhodopsin”. Proceedings of the National Academy of Sciences of the United States of America 44 (2): 130–139. (February 1958). Bibcode: 1958PNAS...44..130H. doi:10.1073/pnas.44.2.130. PMC 335377. PMID 16590155.
“The mechanism of bleaching rhodopsin”. Annals of the New York Academy of Sciences 74 (2): 266–280. (November 1959). Bibcode: 1959NYASA..74..266K. doi:10.1111/j.1749-6632.1958.tb39550.x. PMID 13627857.
“Crystal structure of metarhodopsin II”. Nature 471 (7340): 651–655. (March 2011). Bibcode: 2011Natur.471..651C. doi:10.1038/nature09789. PMID 213899886
“Molecular basis of visual excitation”. Science 162 (3850): 230–239. (October 1968). Bibcode: 1968Sci...162..230W. doi:10.1126/science.162.3850.230. PMID 4877437.
“Evolution and diversity of opsins”. Wiley Interdisciplinary Reviews: Membrane Transport and Signaling 1 (1): 104–111. (January 2012). doi:10.1002/wmts.6.
“Spectral tuning of deep red cone pigments”. Biochemistry 47 (16): 4614–4620. (April 2008). doi:10.1021/bi702069d. PMC 2492582. PMID 18370404.

harvard.edu

ui.adsabs.harvard.edu

“Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin”. Nature 321 (6065): 75–79. (May 1986). Bibcode: 1986Natur.321...75D. doi:10.1038/321075a0. PMID 30101326
“Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core”. Nature 326 (6108): 73–77. (March 1987). Bibcode: 1987Natur.326...73D. doi:10.1038/326073a0. PMID 2881211.
“Carotenoids and the Vitamin A Cycle in Vision”. Nature 134 (3376): 65. (July 1934). Bibcode: 1934Natur.134...65W. doi:10.1038/134065a0.
“Hindered Cis Isomers of Vitamin a and Retinene: The Structure of the Neo-B Isomer”. Proceedings of the National Academy of Sciences of the United States of America 41 (7): 438–451. (July 1955). Bibcode: 1955PNAS...41..438W. doi:10.1073/pnas.41.7.438. PMC 528115. PMID 16589696.
“HINDERED CIS ISOMERS OF VITAMIN A AND RETINENE: THE STRUCTURE OF THE NEO-b ISOMER”. Proceedings of the National Academy of Sciences of the United States of America 42 (9): 578–580. (September 1956). Bibcode: 1956PNAS...42..578O. doi:10.1073/pnas.42.9.578. PMC 534254. PMID 16589909.
“Crystal structure of rhodopsin: A G protein-coupled receptor”. Science 289 (5480): 739–745. (August 2000). Bibcode: 2000Sci...289..739P. doi:10.1126/science.289.5480.739. PMID 109265286
“Crystal structure of squid rhodopsin”. Nature 453 (7193): 363–367. (May 2008). Bibcode: 2008Natur.453..363M. doi:10.1038/nature06925. PMID 18480818.
“Site of attachment of retinal in rhodopsin”. Nature 216 (5121): 1178–1181. (December 1967). Bibcode: 1967Natur.216.1178B. doi:10.1038/2161178a0. PMID 4294735.
“Rhodopsin and indicator yellow”. Nature 171 (4350): 469–471. (March 1953). Bibcode: 1953Natur.171..469C. doi:10.1038/171469a0. PMID 13046517.
“The Action of Light on Rhodopsin”. Proceedings of the National Academy of Sciences of the United States of America 44 (2): 130–139. (February 1958). Bibcode: 1958PNAS...44..130H. doi:10.1073/pnas.44.2.130. PMC 335377. PMID 16590155.
“The mechanism of bleaching rhodopsin”. Annals of the New York Academy of Sciences 74 (2): 266–280. (November 1959). Bibcode: 1959NYASA..74..266K. doi:10.1111/j.1749-6632.1958.tb39550.x. PMID 13627857.
“Crystal structure of metarhodopsin II”. Nature 471 (7340): 651–655. (March 2011). Bibcode: 2011Natur.471..651C. doi:10.1038/nature09789. PMID 213899886
“Molecular basis of visual excitation”. Science 162 (3850): 230–239. (October 1968). Bibcode: 1968Sci...162..230W. doi:10.1126/science.162.3850.230. PMID 4877437.

kobe-u.ac.jp

“無脊椎動物由来の光受容タンパク質を利用した、特定の細胞応答を選択的に光でコントロールできる「精密バイアス光操作ツール」の開発”. 神戸大学. 2024年6月16日閲覧。

kotobank.jp

「オプシン」。

nih.gov

pubmed.ncbi.nlm.nih.gov

“G protein involvement in receptor-effector coupling”. The Journal of Biological Chemistry 263 (6): 2577–2580. (February 1988). doi:10.1016/s0021-9258(18)69103-3. PMID 2830256.
“Fingerprinting G-protein-coupled receptors”. Protein Engineering 7 (2): 195–203. (February 1994). doi:10.1093/protein/7.2.195. PMID 8170923.
“Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin”. Nature 321 (6065): 75–79. (May 1986). Bibcode: 1986Natur.321...75D. doi:10.1038/321075a0. PMID 30101326
“Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core”. Nature 326 (6108): 73–77. (March 1987). Bibcode: 1987Natur.326...73D. doi:10.1038/326073a0. PMID 2881211.
“Hindered Cis Isomers of Vitamin a and Retinene: The Structure of the Neo-B Isomer”. Proceedings of the National Academy of Sciences of the United States of America 41 (7): 438–451. (July 1955). Bibcode: 1955PNAS...41..438W. doi:10.1073/pnas.41.7.438. PMC 528115. PMID 16589696.
“The neo-b isomer of vitamin A and retinene”. The Journal of Biological Chemistry 222 (2): 865–877. (October 1956). doi:10.1016/S0021-9258(20)89944-X. PMID 13367054.
“HINDERED CIS ISOMERS OF VITAMIN A AND RETINENE: THE STRUCTURE OF THE NEO-b ISOMER”. Proceedings of the National Academy of Sciences of the United States of America 42 (9): 578–580. (September 1956). Bibcode: 1956PNAS...42..578O. doi:10.1073/pnas.42.9.578. PMC 534254. PMID 16589909.
“The structure of bovine rhodopsin”. Biophysics of Structure and Mechanism 9 (4): 235–244. (1983). doi:10.1007/BF00535659. PMID 63426916
“Crystal structure of rhodopsin: A G protein-coupled receptor”. Science 289 (5480): 739–745. (August 2000). Bibcode: 2000Sci...289..739P. doi:10.1126/science.289.5480.739. PMID 109265286
“Crystal structure of squid rhodopsin”. Nature 453 (7193): 363–367. (May 2008). Bibcode: 2008Natur.453..363M. doi:10.1038/nature06925. PMID 18480818.
“Site of attachment of retinal in rhodopsin”. Nature 216 (5121): 1178–1181. (December 1967). Bibcode: 1967Natur.216.1178B. doi:10.1038/2161178a0. PMID 4294735.
“Rhodopsin and indicator yellow”. Nature 171 (4350): 469–471. (March 1953). Bibcode: 1953Natur.171..469C. doi:10.1038/171469a0. PMID 13046517.
“Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue”. The Biochemical Journal 59 (1): 122–128. (January 1955). doi:10.1042/bj0590122. PMC 1216098. PMID 14351151.
“The Action of Light on Rhodopsin”. Proceedings of the National Academy of Sciences of the United States of America 44 (2): 130–139. (February 1958). Bibcode: 1958PNAS...44..130H. doi:10.1073/pnas.44.2.130. PMC 335377. PMID 16590155.
“The mechanism of bleaching rhodopsin”. Annals of the New York Academy of Sciences 74 (2): 266–280. (November 1959). Bibcode: 1959NYASA..74..266K. doi:10.1111/j.1749-6632.1958.tb39550.x. PMID 13627857.
“Crystal structure of metarhodopsin II”. Nature 471 (7340): 651–655. (March 2011). Bibcode: 2011Natur.471..651C. doi:10.1038/nature09789. PMID 213899886
“Molecular basis of visual excitation”. Science 162 (3850): 230–239. (October 1968). Bibcode: 1968Sci...162..230W. doi:10.1126/science.162.3850.230. PMID 4877437.
“Spectral tuning of deep red cone pigments”. Biochemistry 47 (16): 4614–4620. (April 2008). doi:10.1021/bi702069d. PMC 2492582. PMID 18370404.

ncbi.nlm.nih.gov

“Hindered Cis Isomers of Vitamin a and Retinene: The Structure of the Neo-B Isomer”. Proceedings of the National Academy of Sciences of the United States of America 41 (7): 438–451. (July 1955). Bibcode: 1955PNAS...41..438W. doi:10.1073/pnas.41.7.438. PMC 528115. PMID 16589696.
“HINDERED CIS ISOMERS OF VITAMIN A AND RETINENE: THE STRUCTURE OF THE NEO-b ISOMER”. Proceedings of the National Academy of Sciences of the United States of America 42 (9): 578–580. (September 1956). Bibcode: 1956PNAS...42..578O. doi:10.1073/pnas.42.9.578. PMC 534254. PMID 16589909.
“Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue”. The Biochemical Journal 59 (1): 122–128. (January 1955). doi:10.1042/bj0590122. PMC 1216098. PMID 14351151.
“The Action of Light on Rhodopsin”. Proceedings of the National Academy of Sciences of the United States of America 44 (2): 130–139. (February 1958). Bibcode: 1958PNAS...44..130H. doi:10.1073/pnas.44.2.130. PMC 335377. PMID 16590155.
“Spectral tuning of deep red cone pigments”. Biochemistry 47 (16): 4614–4620. (April 2008). doi:10.1021/bi702069d. PMC 2492582. PMID 18370404.

pmc.ncbi.nlm.nih.gov

“Hindered Cis Isomers of Vitamin a and Retinene: The Structure of the Neo-B Isomer”. Proceedings of the National Academy of Sciences of the United States of America 41 (7): 438–451. (July 1955). Bibcode: 1955PNAS...41..438W. doi:10.1073/pnas.41.7.438. PMC 528115. PMID 16589696.
“HINDERED CIS ISOMERS OF VITAMIN A AND RETINENE: THE STRUCTURE OF THE NEO-b ISOMER”. Proceedings of the National Academy of Sciences of the United States of America 42 (9): 578–580. (September 1956). Bibcode: 1956PNAS...42..578O. doi:10.1073/pnas.42.9.578. PMC 534254. PMID 16589909.
“Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue”. The Biochemical Journal 59 (1): 122–128. (January 1955). doi:10.1042/bj0590122. PMC 1216098. PMID 14351151.
“The Action of Light on Rhodopsin”. Proceedings of the National Academy of Sciences of the United States of America 44 (2): 130–139. (February 1958). Bibcode: 1958PNAS...44..130H. doi:10.1073/pnas.44.2.130. PMC 335377. PMID 16590155.
“Spectral tuning of deep red cone pigments”. Biochemistry 47 (16): 4614–4620. (April 2008). doi:10.1021/bi702069d. PMC 2492582. PMID 18370404.