エメリン (タンパク質) (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "エメリン (タンパク質)" in Japanese language version.

refsWebsite

Global rank Japanese rank

30nih.gov

4^th place

24^th place

23doi.org

2^nd place

6^th place

2ensembl.org

1,626^th place

2,625^th place

2wikipedia.org

low place

1histmodbiomed.org

low place

1wikidata.org

43^rd place

1,892^nd place

1web.archive.org

1^st place

1heartproteome.org

low place

doi.org

“Identification of a novel X-linked gene responsible for Emery–Dreifuss muscular dystrophy”. Nature Genetics 8 (4): 323–7. (Dec 1994). doi:10.1038/ng1294-323. PMID 7894480.
“Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy”. Nature Genetics 12 (3): 254–9. (Mar 1996). doi:10.1038/ng0396-254. PMID 8589715.
“The Emery–Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein”. Human Molecular Genetics 5 (6): 801–8. (Jun 1996). doi:10.1093/hmg/5.6.801. PMID 8776595.
“Heart-specific localization of emerin: new insights into Emery–Dreifuss muscular dystrophy”. Human Molecular Genetics 6 (13): 2257–64. (Dec 1997). doi:10.1093/hmg/6.13.2257. PMID 9361031.
“Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation”. Cellular and Molecular Life Sciences 67 (5): 781–96. (Mar 2010). doi:10.1007/s00018-009-0219-8. PMID 19997769.
“Distribution of emerin and lamins in the heart and implications for Emery–Dreifuss muscular dystrophy”. Human Molecular Genetics 8 (2): 353–9. (Feb 1999). doi:10.1093/hmg/8.2.353. PMID 9949197.
Lammerding, J; Hsiao, J; Schulze, PC; Kozlov, S; Stewart, CL; Lee, RT (29 August 2005). “Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells.”. The Journal of Cell Biology 170 (5): 781–91. doi:10.1083/jcb.200502148. PMC 2171355. PMID 16115958.
Wheeler, MA; Warley, A; Roberts, RG; Ehler, E; Ellis, JA (March 2010). “Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation.”. Cellular and Molecular Life Sciences 67 (5): 781–96. doi:10.1007/s00018-009-0219-8. PMID 19997769.
“Emery–Dreifuss muscular dystrophy - a 40 year retrospective”. Neuromuscular Disorders 10 (4–5): 228–32. (Jun 2000). doi:10.1016/s0960-8966(00)00105-x. PMID 10838246.
“Emerin deletions occurring on both Xq28 inversion backgrounds”. Human Molecular Genetics 7 (1): 135–9. (Jan 1998). doi:10.1093/hmg/7.1.135. PMID 9384614.
“Virology: HIV goes nuclear”. Nature 441 (7093): 581–2. (Jun 2006). doi:10.1038/441581a. PMID 16738646.
“Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts”. Biochemical and Biophysical Research Communications 303 (3): 764–70. (Apr 2003). doi:10.1016/s0006-291x(03)00415-7. PMID 12670476.
“The molecular basis of emerin-emerin and emerin-BAF interactions”. Journal of Cell Science 127 (Pt 18): 3956–69. (Sep 2014). doi:10.1242/jcs.148247. PMC 4163644. PMID 25052089.
“Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro”. The Journal of Biological Chemistry 278 (9): 6969–75. (Feb 2003). doi:10.1074/jbc.M208811200. PMID 12493765.
“Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery–Dreifuss muscular dystrophy”. European Journal of Biochemistry / FEBS 271 (5): 1035–45. (Mar 2004). doi:10.1111/j.1432-1033.2004.04007.x. PMID 15009215.
“The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus”. The EMBO Journal 25 (14): 3275–85. (Jul 2006). doi:10.1038/sj.emboj.7601230. PMC 1523183. PMID 16858403.
“Emerin interacts in vitro with the splicing-associated factor, YT521-B”. European Journal of Biochemistry / FEBS 270 (11): 2459–66. (Jun 2003). doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.
“Interaction between emerin and nuclear lamins”. Journal of Biochemistry 129 (2): 321–7. (Feb 2001). doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
“Direct interaction between emerin and lamin A”. Biochemical and Biophysical Research Communications 267 (3): 709–14. (Jan 2000). doi:10.1006/bbrc.1999.2023. PMID 10673356.
“Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro”. FEBS Letters 525 (1–3): 135–40. (Aug 2002). doi:10.1016/s0014-5793(02)03105-8. PMID 12163176.
“Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy”. Experimental Cell Research 313 (13): 2845–57. (Aug 2007). doi:10.1016/j.yexcr.2007.03.025. PMID 17462627.
“Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle”. Journal of Cell Science 118 (Pt 4): 673–87. (Feb 2005). doi:10.1242/jcs.01642. PMID 15671068.
“LUMA interacts with emerin and influences its distribution at the inner nuclear membrane”. Journal of Cell Science 121 (Pt 4): 536–48. (Feb 2008). doi:10.1242/jcs.019281. PMID 18230648.

ensembl.org

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000102119 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000001964 - Ensembl, May 2017

heartproteome.org

“Protein sequence of human EMD (Uniprot ID: P50402)”. Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). 4 March 2016時点のオリジナルよりアーカイブ。16 September 2015閲覧。

histmodbiomed.org

Peter Harper; Lois Reynolds; Tilli Tansey, eds. (2010年), Clinical Genetics in Britain: Origins and development, Wellcome Witnesses to Contemporary Medicine, History of Modern Biomedicine Research Group, pp. 118-119, ISBN 978-0-85484-127-1 , Wikidata Q29581774

nih.gov

pubmed.ncbi.nlm.nih.gov

“Identification of a novel X-linked gene responsible for Emery–Dreifuss muscular dystrophy”. Nature Genetics 8 (4): 323–7. (Dec 1994). doi:10.1038/ng1294-323. PMID 7894480.
“Emerin deficiency at the nuclear membrane in patients with Emery–Dreifuss muscular dystrophy”. Nature Genetics 12 (3): 254–9. (Mar 1996). doi:10.1038/ng0396-254. PMID 8589715.
“The Emery–Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein”. Human Molecular Genetics 5 (6): 801–8. (Jun 1996). doi:10.1093/hmg/5.6.801. PMID 8776595.
“Heart-specific localization of emerin: new insights into Emery–Dreifuss muscular dystrophy”. Human Molecular Genetics 6 (13): 2257–64. (Dec 1997). doi:10.1093/hmg/6.13.2257. PMID 9361031.
“Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation”. Cellular and Molecular Life Sciences 67 (5): 781–96. (Mar 2010). doi:10.1007/s00018-009-0219-8. PMID 19997769.
“Distribution of emerin and lamins in the heart and implications for Emery–Dreifuss muscular dystrophy”. Human Molecular Genetics 8 (2): 353–9. (Feb 1999). doi:10.1093/hmg/8.2.353. PMID 9949197.
Lammerding, J; Hsiao, J; Schulze, PC; Kozlov, S; Stewart, CL; Lee, RT (29 August 2005). “Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells.”. The Journal of Cell Biology 170 (5): 781–91. doi:10.1083/jcb.200502148. PMC 2171355. PMID 16115958.
Wheeler, MA; Warley, A; Roberts, RG; Ehler, E; Ellis, JA (March 2010). “Identification of an emerin-beta-catenin complex in the heart important for intercalated disc architecture and beta-catenin localisation.”. Cellular and Molecular Life Sciences 67 (5): 781–96. doi:10.1007/s00018-009-0219-8. PMID 19997769.
“Emery–Dreifuss muscular dystrophy - a 40 year retrospective”. Neuromuscular Disorders 10 (4–5): 228–32. (Jun 2000). doi:10.1016/s0960-8966(00)00105-x. PMID 10838246.
“Emerin deletions occurring on both Xq28 inversion backgrounds”. Human Molecular Genetics 7 (1): 135–9. (Jan 1998). doi:10.1093/hmg/7.1.135. PMID 9384614.
“Virology: HIV goes nuclear”. Nature 441 (7093): 581–2. (Jun 2006). doi:10.1038/441581a. PMID 16738646.
“Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts”. Biochemical and Biophysical Research Communications 303 (3): 764–70. (Apr 2003). doi:10.1016/s0006-291x(03)00415-7. PMID 12670476.
“The molecular basis of emerin-emerin and emerin-BAF interactions”. Journal of Cell Science 127 (Pt 18): 3956–69. (Sep 2014). doi:10.1242/jcs.148247. PMC 4163644. PMID 25052089.
“Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro”. The Journal of Biological Chemistry 278 (9): 6969–75. (Feb 2003). doi:10.1074/jbc.M208811200. PMID 12493765.
“Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery–Dreifuss muscular dystrophy”. European Journal of Biochemistry / FEBS 271 (5): 1035–45. (Mar 2004). doi:10.1111/j.1432-1033.2004.04007.x. PMID 15009215.
“The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus”. The EMBO Journal 25 (14): 3275–85. (Jul 2006). doi:10.1038/sj.emboj.7601230. PMC 1523183. PMID 16858403.
“Emerin interacts in vitro with the splicing-associated factor, YT521-B”. European Journal of Biochemistry / FEBS 270 (11): 2459–66. (Jun 2003). doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.
“Interaction between emerin and nuclear lamins”. Journal of Biochemistry 129 (2): 321–7. (Feb 2001). doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
“Direct interaction between emerin and lamin A”. Biochemical and Biophysical Research Communications 267 (3): 709–14. (Jan 2000). doi:10.1006/bbrc.1999.2023. PMID 10673356.
“Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues”. Journal of Cell Science 114 (Pt 24): 4485–98. (Dec 2001). PMID 11792814.
“Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro”. FEBS Letters 525 (1–3): 135–40. (Aug 2002). doi:10.1016/s0014-5793(02)03105-8. PMID 12163176.
“Distinct functional domains in nesprin-1alpha and nesprin-2beta bind directly to emerin and both interactions are disrupted in X-linked Emery–Dreifuss muscular dystrophy”. Experimental Cell Research 313 (13): 2845–57. (Aug 2007). doi:10.1016/j.yexcr.2007.03.025. PMID 17462627.
“Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle”. Journal of Cell Science 118 (Pt 4): 673–87. (Feb 2005). doi:10.1242/jcs.01642. PMID 15671068.
“LUMA interacts with emerin and influences its distribution at the inner nuclear membrane”. Journal of Cell Science 121 (Pt 4): 536–48. (Feb 2008). doi:10.1242/jcs.019281. PMID 18230648.

ncbi.nlm.nih.gov

Human PubMed Reference:
Mouse PubMed Reference:
“Entrez Gene: EMD emerin (Emery–Dreifuss muscular dystrophy)”. 2019年11月24日閲覧。
Lammerding, J; Hsiao, J; Schulze, PC; Kozlov, S; Stewart, CL; Lee, RT (29 August 2005). “Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells.”. The Journal of Cell Biology 170 (5): 781–91. doi:10.1083/jcb.200502148. PMC 2171355. PMID 16115958.
“The molecular basis of emerin-emerin and emerin-BAF interactions”. Journal of Cell Science 127 (Pt 18): 3956–69. (Sep 2014). doi:10.1242/jcs.148247. PMC 4163644. PMID 25052089.
“The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus”. The EMBO Journal 25 (14): 3275–85. (Jul 2006). doi:10.1038/sj.emboj.7601230. PMC 1523183. PMID 16858403.

web.archive.org

“Protein sequence of human EMD (Uniprot ID: P50402)”. Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). 4 March 2016時点のオリジナルよりアーカイブ。16 September 2015閲覧。

wikidata.org

Peter Harper; Lois Reynolds; Tilli Tansey, eds. (2010年), Clinical Genetics in Britain: Origins and development, Wellcome Witnesses to Contemporary Medicine, History of Modern Biomedicine Research Group, pp. 118-119, ISBN 978-0-85484-127-1 , Wikidata Q29581774

wikipedia.org

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000102119 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000001964 - Ensembl, May 2017