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Hatakeyama S, Yada M, Matsumoto M et al (2001) U box proteins as a new family of ubiquitin-
protein ligases. J Biol Chem 276:33111-33120
Hatakeyama S, Matsumoto M, Kamura T et al (2004a) U-box protein carboxyl terminus of Hsc70-
interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and
is involved in neurodegeneration of tauopathy. J Neurochem 91:299-307
Hatakeyama S, Matsumoto M, Yada M et al (2004b) Interaction of U-box-type ubiquitin-protein
ligases (E3s) with molecular chaperones. Genes Cells 9:533-548
Heinemeyer W, Ramos PC, Dohmen RJ (2004) The ultimate nanoscale mincer: assembly, structure
and active sites of the 20S proteasome core. Cell Mol Life Sci 61:1562-1578
Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425-479
Hiromura M, Yano M, Mori H et al (1998) Intrinsic ADP-ATP exchange activity is a novel func-
tion of the molecular chaperone, Hsp70. J Biol Chem 273:5435-5438
Hofmann RM, Pickart CM (1999) Noncanonical MMS2-encoded ubiquitin-conjugating enzyme
functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96:645-653
Hohfeld J (1998) Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the charac-
terization of the anti-apoptotic protein BAG-1 provides novel insights. Biol Chem 379:269-274
Hohfeld J, Cyr DM, Patterson C (2001) From the cradle to the grave: molecular chaperones that
may choose between folding and degradation. EMBO Rep 2:885-890
Hwang JR, Zhang C, Patterson C (2005) C-terminus of heat shock protein 70-interacting protein
facilitates degradation of apoptosis signal-regulating kinase 1 and inhibits apoptosis signal-
regulating kinase 1-dependent apoptosis. Cell Stress Chaperones 10:147-156
Imai J, Yashiroda H, Maruya M et al (2003) Proteasomes and molecular chaperones: cellular ma-
chinery responsible for folding and destruction of unfolded proteins. Cell Cycle 2:585-590
Jacobson AD, Zhang NY, Xu P et al (2009) The lysine 48 and lysine 63 ubiquitin conjugates are
processed differently by the 26 s proteasome. J Biol Chem 284:35485-35494
Jang KW, Lee JE, Kim SY et al (2011a) The C-terminus of Hsp70-interacting protein promotes
Met receptor degradation. J Thorac Oncol 6:679-687
Jang KW, Lee KH, Kim SH et al (2011b) Ubiquitin ligase CHIP induces TRAF2 proteasomal deg-
radation and NF-kappaB inactivation to regulate breast cancer cell invasion. J Cell Biochem
112:3612-3620
Jiang J, Ballinger CA, Wu Y et al (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identifi-
cation of Hsc70 as a target for ubiquitylation. J Biol Chem 276:42938-42944
Johnson ES, Bartel B, Seufert W et al (1992) Ubiquitin as a degradation signal. EMBO J 11:497-
505
Johnson ES, Ma PC, Ota IM et al (1995) A proteolytic pathway that recognizes ubiquitin as a
degradation signal. J Biol Chem 270:17442-17456
Kabani M, McLellan C, Raynes DA et al (2002) HspBP1, a homologue of the yeast Fes1 and Sls1
proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett 531:339-342
Kajiro M, Hirota R, Nakajima Y et al (2009) The ubiquitin ligase CHIP acts as an upstream regula-
tor of oncogenic pathways. Nat Cell Biol 11:312-319
Kalia LV, Kalia SK, Chau H et al (2011) Ubiquitinylation of alpha-synuclein by carboxyl termi-
nus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5).
PLoS One 6:e14695
Kastle M, Grune T (2012) Interactions of the proteasomal system with chaperones: protein triage
and protein quality control. Prog Mol Biol Transl Sci 109:113-160
Kettern N, Dreiseidler M, Tawo R et al (2010) Chaperone-assisted degradation: multiple paths to
destruction. Biol Chem 391:481-489
Knapp RT, Wong MJ, Kollmannsberger LK et al (2014) Hsp70 cochaperones HspBP1 and BAG-
1M differentially regulate steroid hormone receptor function. PLoS One 9:e85415
Ko HS, Bailey R, Smith WW et al (2009) CHIP regulates leucine-rich repeat kinase-2 ubiquitina-
tion, degradation, and toxicity. Proc Natl Acad Sci U S A 106:2897-2902
Ko HR, Kim CK, Lee SB et al (2014) P42 Ebp1 regulates the proteasomal degradation of the p85
regulatory subunit of PI3K by recruiting a chaperone-E3 ligase complex HSP70/CHIP. Cell
Death Dis 5:e1131
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