相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。A delivery system targeting bone formation surfaces to facilitate RNAi-based anabolic therapy
Ge Zhang et al.
NATURE MEDICINE (2012)
Cdh1 Regulates Osteoblast Function through an APC/C-Independent Modulation of Smurf1
Lixin Wan et al.
MOLECULAR CELL (2011)
N-terminal PH domain and C-terminal auto-inhibitory region of CKIP-1 coordinate to determine its nucleus-plasma membrane shuttling
Shenli Xi et al.
FEBS LETTERS (2010)
Smad Ubiquitylation Regulatory Factor 1/2 (Smurf1/2) Promotes p53 Degradation by Stabilizing the E3 Ligase MDM2
Jing Nie et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2010)
ATP-Dependent Steps in the Binding of Ubiquitin Conjugates to the 26S Proteasome that Commit to Degradation
Andreas Peth et al.
MOLECULAR CELL (2010)
Monoubiquitination of RPN10 Regulates Substrate Recruitment to the Proteasome
Marta Isasa et al.
MOLECULAR CELL (2010)
Molecular mechanisms of proteasome assembly
Shigeo Murata et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2009)
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
Patrick Schreiner et al.
NATURE (2008)
Proteasome subunit Rpn13 is a novel ubiquitin receptor
Koraljka Husnjak et al.
NATURE (2008)
Targeting WW domains linker of HECT-type ubiquitin ligase Smurf1 for activation by CKIP-1
Kefeng Lu et al.
NATURE CELL BIOLOGY (2008)
UBL/UBA ubiquitin receptor proteins bind a common tetraubiquitin chain
Y Kang et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
Delivery of ubiquitinated substrates to protein-unfolding machines
S Elsasser et al.
NATURE CELL BIOLOGY (2005)
Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation
M Yamashita et al.
CELL (2005)
Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
I Kim et al.
MOLECULAR BIOLOGY OF THE CELL (2004)
Regulation of cell polarity and protrusion formation by targeting RhoA for degradation
HR Wang et al.
SCIENCE (2003)
Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein
PG Corn et al.
NATURE GENETICS (2003)