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関連文献

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“Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone”. Biochem. Soc. Trans. 32 (Pt 5):  728-30. (2005). doi:10.1042/BST0320728. PMID 15493999.
“Genetics of Paget's disease of bone”. Joint Bone Spine 73 (3):  243-8. (2006). doi:10.1016/j.jbspin.2005.05.009. PMID 16574459.
“Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region”. Proc. Natl. Acad. Sci. U.S.A. 92 (26):  12338-42. (1996). doi:10.1073/pnas.92.26.12338. PMC 40352. PMID 8618896. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC40352/.
“Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein”. Biochemistry 35 (7):  2157-67. (1996). doi:10.1021/bi9524124. PMID 8652557.
“p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins”. J. Biol. Chem. 271 (34):  20235-7. (1996). doi:10.1074/jbc.271.34.20235. PMID 8702753.
“A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor”. J. Biol. Chem. 271 (44):  27197-200. (1996). doi:10.1074/jbc.271.44.27197. PMID 8910285.
“The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase”. J. Biol. Chem. 272 (18):  12158-63. (1997). doi:10.1074/jbc.272.18.12158. PMID 9115287.
“Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62”. Mol. Cell. Biol. 18 (5):  3069-80. (1998). doi:10.1128/mcb.18.5.3069. PMC 110686. PMID 9566925. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110686/.
“Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein”. FEBS Lett. 435 (2-3):  138-42. (1998). doi:10.1016/S0014-5793(98)01021-7. PMID 9762895.
“The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation”. EMBO J. 18 (11):  3044-53. (1999). doi:10.1093/emboj/18.11.3044. PMC 1171386. PMID 10356400. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171386/.
“Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent”. Am. J. Pathol. 154 (6):  1701-10. (1999). doi:10.1016/S0002-9440(10)65426-0. PMC 1866621. PMID 10362795. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1866621/.
“p62 functions as a p38 MAP kinase regulator”. Biochem. Biophys. Res. Commun. 269 (2):  521-5. (2000). doi:10.1006/bbrc.2000.2333. PMID 10708586.
“The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway”. EMBO J. 19 (7):  1576-86. (2000). doi:10.1093/emboj/19.7.1576. PMC 310227. PMID 10747026. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC310227/.
“The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor”. J. Biol. Chem. 276 (11):  7709-12. (2001). doi:10.1074/jbc.C000869200. PMID 11244088.
“Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies”. NeuroReport 12 (10):  2085-90. (2001). doi:10.1097/00001756-200107200-00009. PMID 11447312.
“Paget disease of bone: mapping of two loci at 5q35-qter and 5q31”. Am. J. Hum. Genet. 69 (3):  528-43. (2001). doi:10.1086/322975. PMC 1235483. PMID 11473345. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1235483/.
“p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition”. FEBS Lett. 510 (1-2):  57-61. (2002). doi:10.1016/S0014-5793(01)03224-0. PMID 11755531.
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  1q02: NMR structure of the UBA domain of p62 (SQSTM1)