WWドメイン (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "WWドメイン" in Japanese language version.

refsWebsite

Global rank Japanese rank

60nih.gov

4^th place

24^th place

34doi.org

2^nd place

6^th place

10harvard.edu

18^th place

107^th place

1rcsb.org

8,838^th place

low place

1ebi.ac.uk

5,849^th place

7,098^th place

doi.org

PDB: 1PIN; “Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent”. Cell 89 (6): 875–86. (June 1997). doi:10.1016/S0092-8674(00)80273-1. PMID 9200606.
“The WW domain: a signalling site in dystrophin?”. Trends in Biochemical Sciences 19 (12): 531–3. (December 1994). doi:10.1016/0968-0004(94)90053-1. PMID 7846762.
“The rsp5-domain is shared by proteins of diverse functions”. FEBS Letters 358 (2): 153–7. (January 1995). doi:10.1016/0014-5793(94)01415-W. PMID 7828727.
“WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65”. Biochemical and Biophysical Research Communications 205 (2): 1201–5. (December 1994). doi:10.1006/bbrc.1994.2793. PMID 7802651.
“Characterization of a novel protein-binding module--the WW domain”. FEBS Letters 369 (1): 67–71. (August 1995). doi:10.1016/0014-5793(95)00550-S. PMID 7641887.
“The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules”. Proceedings of the National Academy of Sciences of the United States of America 92 (17): 7819–23. (August 1995). Bibcode: 1995PNAS...92.7819C. doi:10.1073/pnas.92.17.7819. PMC 41237. PMID 7644498.
“Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide”. Nature 382 (6592): 646–9. (August 1996). Bibcode: 1996Natur.382..646M. doi:10.1038/382646a0. PMID 8757138.
“Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain”. The Journal of Biological Chemistry 270 (24): 14733–41. (June 1995). doi:10.1074/jbc.270.24.14733. PMID 7782338.
“Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways”. Structure 20 (10): 1726–36. (October 2012). doi:10.1016/j.str.2012.07.014. PMC 3472128. PMID 22921829.
“Regulation of Nedd4-2 self-ubiquitination and stability by a PY motif located within its HECT-domain”. The Biochemical Journal 415 (1): 155–63. (October 2008). doi:10.1042/BJ20071708. PMID 18498246.
“Function of WW domains as phosphoserine- or phosphothreonine-binding modules”. Science 283 (5406): 1325–8. (February 1999). Bibcode: 1999Sci...283.1325L. doi:10.1126/science.283.5406.1325. PMID 10037602.
“Structural basis for phosphoserine-proline recognition by group IV WW domains”. Nature Structural Biology 7 (8): 639–43. (August 2000). doi:10.1038/77929. PMID 10932246.
“A novel pro-Arg motif recognized by WW domains”. The Journal of Biological Chemistry 275 (14): 10359–69. (April 2000). doi:10.1074/jbc.275.14.10359. PMID 10744724.
“The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled”. The Journal of Biological Chemistry 272 (52): 32869–77. (December 1997). doi:10.1074/jbc.272.52.32869. PMID 9407065.
“Modularity in the Hippo signaling pathway”. Trends in Biochemical Sciences 35 (11): 627–33. (November 2010). doi:10.1016/j.tibs.2010.05.010. PMID 20598891.
“Golabi-Ito-Hall syndrome results from a missense mutation in the WW domain of the PQBP1 gene”. Journal of Medical Genetics 43 (6): e30. (June 2006). doi:10.1136/jmg.2005.037556. PMC 2564547. PMID 16740914.
“Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing”. The Journal of Biological Chemistry 285 (25): 19391–401. (June 2010). doi:10.1074/jbc.M109.084525. PMC 2885219. PMID 20410308.
“Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome”. The EMBO Journal 15 (10): 2381–7. (May 1996). doi:10.1002/j.1460-2075.1996.tb00594.x. PMC 450168. PMID 8665845.
“Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination”. The EMBO Journal 16 (21): 6325–36. (November 1997). doi:10.1093/emboj/16.21.6325. PMC 1170239. PMID 9351815.
“A map of WW domain family interactions”. Proteomics 4 (3): 643–55. (March 2004). doi:10.1002/pmic.200300632. PMID 14997488.
“Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1”. FEBS Letters 586 (17): 2795–9. (August 2012). doi:10.1016/j.febslet.2012.03.041. PMC 3413755. PMID 22710169.
“The Hippo signaling pathway coordinately regulates cell proliferation and apoptosis by inactivating Yorkie, the Drosophila Homolog of YAP”. Cell 122 (3): 421–34. (August 2005). doi:10.1016/j.cell.2005.06.007. PMID 16096061.
“Both TEAD-binding and WW domains are required for the growth stimulation and oncogenic transformation activity of yes-associated protein”. Cancer Research 69 (3): 1089–98. (February 2009). doi:10.1158/0008-5472.CAN-08-2997. PMID 19141641.
“Molecular mechanism of pancreatic tumor metastasis inhibition by Gd@C82(OH)22 and its implication for de novo design of nanomedicine”. Proceedings of the National Academy of Sciences of the United States of America 109 (38): 15431–6. (September 2012). Bibcode: 2012PNAS..10915431K. doi:10.1073/pnas.1204600109. PMC 3458392. PMID 22949663.
“Non-destructive inhibition of metallofullerenol Gd@C(82)(OH)(22) on WW domain: implication on signal transduction pathway”. Scientific Reports 2: 957. (2012). Bibcode: 2012NatSR...2E.957K. doi:10.1038/srep00957. PMC 3518810. PMID 23233876.
“Structures of YAP protein domains reveal promising targets for development of new cancer drugs”. Seminars in Cell & Developmental Biology 23 (7): 827–33. (September 2012). doi:10.1016/j.semcdb.2012.05.002. PMC 3427467. PMID 22609812.
“Evaluating beta-turn mimics as beta-sheet folding nucleators”. Proceedings of the National Academy of Sciences of the United States of America 106 (27): 11067–72. (July 2009). Bibcode: 2009PNAS..10611067F. doi:10.1073/pnas.0813012106. PMC 2708776. PMID 19541614.
“Understanding the mechanism of beta-sheet folding from a chemical and biological perspective”. Biopolymers 90 (6): 751–8. (2008). doi:10.1002/bip.21101. PMID 18844292.
“Structure-function-folding relationship in a WW domain”. Proceedings of the National Academy of Sciences of the United States of America 103 (28): 10648–53. (July 2006). Bibcode: 2006PNAS..10310648J. doi:10.1073/pnas.0600511103. PMC 1502286. PMID 16807295.
“Natural-like function in artificial WW domains”. Nature 437 (7058): 579–83. (September 2005). Bibcode: 2005Natur.437..579R. doi:10.1038/nature03990. PMID 16177795.
“Evolutionary information for specifying a protein fold”. Nature 437 (7058): 512–8. (September 2005). Bibcode: 2005Natur.437..512S. doi:10.1038/nature03991. PMID 16177782.
“Computational design and experimental testing of the fastest-folding β-sheet protein”. Journal of Molecular Biology 405 (1): 43–8. (January 2011). doi:10.1016/j.jmb.2010.10.023. PMID 20974152.
“Atomic-level characterization of the structural dynamics of proteins”. Science 330 (6002): 341–6. (October 2010). Bibcode: 2010Sci...330..341S. doi:10.1126/science.1187409. PMID 20947758.
“Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities” (英語). Accounts of Chemical Research 50 (8): 1875–1882. (August 2017). doi:10.1021/acs.accounts.7b00195. PMC 5584629. PMID 28723063.

ebi.ac.uk

“interpro7-client”. www.ebi.ac.uk. 2019年11月17日閲覧。

harvard.edu

ui.adsabs.harvard.edu

“The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules”. Proceedings of the National Academy of Sciences of the United States of America 92 (17): 7819–23. (August 1995). Bibcode: 1995PNAS...92.7819C. doi:10.1073/pnas.92.17.7819. PMC 41237. PMID 7644498.
“Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide”. Nature 382 (6592): 646–9. (August 1996). Bibcode: 1996Natur.382..646M. doi:10.1038/382646a0. PMID 8757138.
“Function of WW domains as phosphoserine- or phosphothreonine-binding modules”. Science 283 (5406): 1325–8. (February 1999). Bibcode: 1999Sci...283.1325L. doi:10.1126/science.283.5406.1325. PMID 10037602.
“Molecular mechanism of pancreatic tumor metastasis inhibition by Gd@C82(OH)22 and its implication for de novo design of nanomedicine”. Proceedings of the National Academy of Sciences of the United States of America 109 (38): 15431–6. (September 2012). Bibcode: 2012PNAS..10915431K. doi:10.1073/pnas.1204600109. PMC 3458392. PMID 22949663.
“Non-destructive inhibition of metallofullerenol Gd@C(82)(OH)(22) on WW domain: implication on signal transduction pathway”. Scientific Reports 2: 957. (2012). Bibcode: 2012NatSR...2E.957K. doi:10.1038/srep00957. PMC 3518810. PMID 23233876.
“Evaluating beta-turn mimics as beta-sheet folding nucleators”. Proceedings of the National Academy of Sciences of the United States of America 106 (27): 11067–72. (July 2009). Bibcode: 2009PNAS..10611067F. doi:10.1073/pnas.0813012106. PMC 2708776. PMID 19541614.
“Structure-function-folding relationship in a WW domain”. Proceedings of the National Academy of Sciences of the United States of America 103 (28): 10648–53. (July 2006). Bibcode: 2006PNAS..10310648J. doi:10.1073/pnas.0600511103. PMC 1502286. PMID 16807295.
“Natural-like function in artificial WW domains”. Nature 437 (7058): 579–83. (September 2005). Bibcode: 2005Natur.437..579R. doi:10.1038/nature03990. PMID 16177795.
“Evolutionary information for specifying a protein fold”. Nature 437 (7058): 512–8. (September 2005). Bibcode: 2005Natur.437..512S. doi:10.1038/nature03991. PMID 16177782.
“Atomic-level characterization of the structural dynamics of proteins”. Science 330 (6002): 341–6. (October 2010). Bibcode: 2010Sci...330..341S. doi:10.1126/science.1187409. PMID 20947758.

nih.gov

pubmed.ncbi.nlm.nih.gov

PDB: 1PIN; “Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent”. Cell 89 (6): 875–86. (June 1997). doi:10.1016/S0092-8674(00)80273-1. PMID 9200606.
“The WW domain: a signalling site in dystrophin?”. Trends in Biochemical Sciences 19 (12): 531–3. (December 1994). doi:10.1016/0968-0004(94)90053-1. PMID 7846762.
“The rsp5-domain is shared by proteins of diverse functions”. FEBS Letters 358 (2): 153–7. (January 1995). doi:10.1016/0014-5793(94)01415-W. PMID 7828727.
“WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65”. Biochemical and Biophysical Research Communications 205 (2): 1201–5. (December 1994). doi:10.1006/bbrc.1994.2793. PMID 7802651.
“Characterization of a novel protein-binding module--the WW domain”. FEBS Letters 369 (1): 67–71. (August 1995). doi:10.1016/0014-5793(95)00550-S. PMID 7641887.
“The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules”. Proceedings of the National Academy of Sciences of the United States of America 92 (17): 7819–23. (August 1995). Bibcode: 1995PNAS...92.7819C. doi:10.1073/pnas.92.17.7819. PMC 41237. PMID 7644498.
“Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide”. Nature 382 (6592): 646–9. (August 1996). Bibcode: 1996Natur.382..646M. doi:10.1038/382646a0. PMID 8757138.
“Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain”. The Journal of Biological Chemistry 270 (24): 14733–41. (June 1995). doi:10.1074/jbc.270.24.14733. PMID 7782338.
“Structural basis for the versatile interactions of Smad7 with regulator WW domains in TGF-β Pathways”. Structure 20 (10): 1726–36. (October 2012). doi:10.1016/j.str.2012.07.014. PMC 3472128. PMID 22921829.
“Regulation of Nedd4-2 self-ubiquitination and stability by a PY motif located within its HECT-domain”. The Biochemical Journal 415 (1): 155–63. (October 2008). doi:10.1042/BJ20071708. PMID 18498246.
“Function of WW domains as phosphoserine- or phosphothreonine-binding modules”. Science 283 (5406): 1325–8. (February 1999). Bibcode: 1999Sci...283.1325L. doi:10.1126/science.283.5406.1325. PMID 10037602.
“Structural basis for phosphoserine-proline recognition by group IV WW domains”. Nature Structural Biology 7 (8): 639–43. (August 2000). doi:10.1038/77929. PMID 10932246.
“A novel pro-Arg motif recognized by WW domains”. The Journal of Biological Chemistry 275 (14): 10359–69. (April 2000). doi:10.1074/jbc.275.14.10359. PMID 10744724.
“The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled”. The Journal of Biological Chemistry 272 (52): 32869–77. (December 1997). doi:10.1074/jbc.272.52.32869. PMID 9407065.
“Modularity in the Hippo signaling pathway”. Trends in Biochemical Sciences 35 (11): 627–33. (November 2010). doi:10.1016/j.tibs.2010.05.010. PMID 20598891.
“Golabi-Ito-Hall syndrome results from a missense mutation in the WW domain of the PQBP1 gene”. Journal of Medical Genetics 43 (6): e30. (June 2006). doi:10.1136/jmg.2005.037556. PMC 2564547. PMID 16740914.
“Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing”. The Journal of Biological Chemistry 285 (25): 19391–401. (June 2010). doi:10.1074/jbc.M109.084525. PMC 2885219. PMID 20410308.
“Identification of a PY motif in the epithelial Na channel subunits as a target sequence for mutations causing channel activation found in Liddle syndrome”. The EMBO Journal 15 (10): 2381–7. (May 1996). doi:10.1002/j.1460-2075.1996.tb00594.x. PMC 450168. PMID 8665845.
“Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination”. The EMBO Journal 16 (21): 6325–36. (November 1997). doi:10.1093/emboj/16.21.6325. PMC 1170239. PMID 9351815.
“A map of WW domain family interactions”. Proteomics 4 (3): 643–55. (March 2004). doi:10.1002/pmic.200300632. PMID 14997488.
“Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1”. FEBS Letters 586 (17): 2795–9. (August 2012). doi:10.1016/j.febslet.2012.03.041. PMC 3413755. PMID 22710169.
“The Hippo signaling pathway coordinately regulates cell proliferation and apoptosis by inactivating Yorkie, the Drosophila Homolog of YAP”. Cell 122 (3): 421–34. (August 2005). doi:10.1016/j.cell.2005.06.007. PMID 16096061.
“Both TEAD-binding and WW domains are required for the growth stimulation and oncogenic transformation activity of yes-associated protein”. Cancer Research 69 (3): 1089–98. (February 2009). doi:10.1158/0008-5472.CAN-08-2997. PMID 19141641.
“Molecular mechanism of pancreatic tumor metastasis inhibition by Gd@C82(OH)22 and its implication for de novo design of nanomedicine”. Proceedings of the National Academy of Sciences of the United States of America 109 (38): 15431–6. (September 2012). Bibcode: 2012PNAS..10915431K. doi:10.1073/pnas.1204600109. PMC 3458392. PMID 22949663.
“Non-destructive inhibition of metallofullerenol Gd@C(82)(OH)(22) on WW domain: implication on signal transduction pathway”. Scientific Reports 2: 957. (2012). Bibcode: 2012NatSR...2E.957K. doi:10.1038/srep00957. PMC 3518810. PMID 23233876.
“Structures of YAP protein domains reveal promising targets for development of new cancer drugs”. Seminars in Cell & Developmental Biology 23 (7): 827–33. (September 2012). doi:10.1016/j.semcdb.2012.05.002. PMC 3427467. PMID 22609812.
“Evaluating beta-turn mimics as beta-sheet folding nucleators”. Proceedings of the National Academy of Sciences of the United States of America 106 (27): 11067–72. (July 2009). Bibcode: 2009PNAS..10611067F. doi:10.1073/pnas.0813012106. PMC 2708776. PMID 19541614.
“Understanding the mechanism of beta-sheet folding from a chemical and biological perspective”. Biopolymers 90 (6): 751–8. (2008). doi:10.1002/bip.21101. PMID 18844292.
“Structure-function-folding relationship in a WW domain”. Proceedings of the National Academy of Sciences of the United States of America 103 (28): 10648–53. (July 2006). Bibcode: 2006PNAS..10310648J. doi:10.1073/pnas.0600511103. PMC 1502286. PMID 16807295.
“Natural-like function in artificial WW domains”. Nature 437 (7058): 579–83. (September 2005). Bibcode: 2005Natur.437..579R. doi:10.1038/nature03990. PMID 16177795.
“Evolutionary information for specifying a protein fold”. Nature 437 (7058): 512–8. (September 2005). Bibcode: 2005Natur.437..512S. doi:10.1038/nature03991. PMID 16177782.
“Computational design and experimental testing of the fastest-folding β-sheet protein”. Journal of Molecular Biology 405 (1): 43–8. (January 2011). doi:10.1016/j.jmb.2010.10.023. PMID 20974152.
“Atomic-level characterization of the structural dynamics of proteins”. Science 330 (6002): 341–6. (October 2010). Bibcode: 2010Sci...330..341S. doi:10.1126/science.1187409. PMID 20947758.
“Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities” (英語). Accounts of Chemical Research 50 (8): 1875–1882. (August 2017). doi:10.1021/acs.accounts.7b00195. PMC 5584629. PMID 28723063.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

rcsb.org

PDB: 1PIN; “Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent”. Cell 89 (6): 875–86. (June 1997). doi:10.1016/S0092-8674(00)80273-1. PMID 9200606.