Chemistry Reference
In-Depth Information
Meimaridou E, Gooljar SB, Chapple JP (2009) From hatching to dispatching: the multiple cellular
roles of the Hsp70 molecular chaperone machinery. J Mol Endocrinol 42:1-9
Morishima Y, Wang AM, Yu Z et al (2008) CHIP deletion reveals functional redundancy of E3
ligases in promoting degradation of both signaling proteins and expanded glutamine proteins.
Hum Mol Genet 17:3942-3952
Muller P, Hrstka R, Coomber D et al (2008) Chaperone-dependent stabilization and degradation of
p53 mutants. Oncogene 27:3371-3383
Muller P, Ruckova E, Halada P et al (2013) C-terminal phosphorylation of Hsp70 and Hsp90 regu-
lates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/
degradation balances. Oncogene 32:3101-3110
Murata S, Minami Y, Minami M et al (2001) CHIP is a chaperone-dependent E3 ligase that ubiq-
uitylates unfolded protein. EMBO Rep 2:1133-1138
Murata S, Chiba T, Tanaka K (2003) CHIP: a quality-control E3 ligase collaborating with molecu-
lar chaperones. Int J Biochem Cell Biol 35:572-578
Murata S, Yashiroda H, Tanaka K (2009) Molecular mechanisms of proteasome assembly. Nat Rev
Mol Cell Biol 10:104-115
Nillegoda NB, Theodoraki MA, Mandal AK et al (2010) Ubr1 and Ubr2 function in a quality
control pathway for degradation of unfolded cytosolic proteins. Mol Biol Cell 21:2102-2116
Odunuga OO, Hornby JA, Bies C et al (2003) Tetratricopeptide repeat motif-mediated Hsc70-
mSTI1 interaction. Molecular characterization of the critical contacts for successful binding
and specificity. J Biol Chem 278:6896-6904
Ohi MD, Vander Kooi CW, Rosenberg JA et al (2003) Structural insights into the U-box, a domain
associated with multi-ubiquitination. Nat Struct Biol 10:250-255
Olsen SK, Lima CD (2013) Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester
transfer. Mol Cell 49:884-896
Ortega J, Heymann JB, Kajava AV et al (2005) The axial channel of the 20S proteasome opens
upon binding of the PA200 activator. J Mol Biol 346:1221-1227
Panaretou B, Prodromou C, Roe SM et al (1998) ATP binding and hydrolysis are essential to the
function of the Hsp90 molecular chaperone in vivo . EMBO J 17:4829-4836
Paul I, Ahmed SF, Bhowmik A et al (2013) The ubiquitin ligase CHIP regulates c-Myc stability
and transcriptional activity. Oncogene 32:1284-1295
Peng HM, Morishima Y, Jenkins GJ et al (2004) Ubiquitylation of neuronal Nitric-oxide synthase
by CHIP, a chaperone-dependent E3 ligase. J Biol Chem 279:52970-52977
Petrucelli L, Dickson D, Kehoe K et al (2004) CHIP and Hsp70 regulate tau ubiquitination, degra-
dation and aggregation. Hum Mol Genet 13:703-714
Prodromou C, Roe SM, O'Brien R et al (1997) Identification and structural characterization of the
ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90:65-75
Prodromou C, Siligardi G, O'Brien R et al (1999) Regulation of Hsp90 ATPase activity by tetratri-
copeptide repeat (TPR)-domain co-chaperones. EMBO J 18:754-762
Prodromou C, Panaretou B, Chohan S et al (2000) The ATPase cycle of Hsp90 drives a molecular
'clamp' via transient dimerization of the N-terminal domains. EMBO J 19:4383-4392
Qian SB, McDonough H, Boellmann F et al (2006) CHIP-mediated stress recovery by sequential
ubiquitination of substrates and Hsp70. Nature 440:551-555
Raynes DA, Guerriero V Jr (1998) Inhibition of Hsp70 ATPase activity and protein renaturation by
a novel Hsp70-binding protein. J Biol Chem 273:32883-32888
Ronnebaum SM, Wu Y, McDonough H et al (2013) The ubiquitin ligase CHIP prevents SirT6
degradation through noncanonical ubiquitination. Mol Cell Biol 33:4461-4472
Roos-Mattjus P, Sistonen L (2004) The ubiquitin-proteasome pathway. Ann Med 36:285-295
Ruckova E, Muller P, Nenutil R et al (2012) Alterations of the Hsp70/Hsp90 chaperone and the
HOP/CHIP co-chaperone system in cancer. Cell Mol Biol Lett 17:446-458
Saeki Y, Kudo T, Sone T et al (2009) Lysine 63-linked polyubiquitin chain may serve as a targeting
signal for the 26S proteasome. EMBO J 28:359-371
Sahara N, Murayama M, Mizoroki T et al (2005) In vivo evidence of CHIP up-regulation attenuat-
ing tau aggregation. J Neurochem 94:1254-1263
Search WWH ::




Custom Search