ECM29/YHL030W Literature Guide Help

Other names published for ECM29: YHL030W

ECM29 - Primary Literature (11)

ReferenceOther Genes Addressed
Sukhai MA, et al.  (2013) Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors. J Clin Invest 123(1):315-28
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
Lee SY, et al.  (2011) Loss of Rpt5 protein interactions with the core particle and Nas2 protein causes the formation of faulty proteasomes that are inhibited by Ecm29 protein. J Biol Chem 286(42):36641-51
Panasenko OO and Collart MA  (2011) Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29. Mol Cell Biol 31(8):1610-23
Park S, et al.  (2011) Structural defects in the regulatory particle-core particle interface of the proteasome induce a novel proteasome stress response. J Biol Chem 286(42):36652-66
Lehmann A, et al.  (2010) Ecm29 fulfils quality control functions in proteasome assembly. Mol Cell 38(6):879-88
Wang X, et al.  (2010) Regulation of the 26S Proteasome Complex During Oxidative Stress. Sci Signal 3(151):ra88
Guerrero C, et al.  (2006) An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol Cell Proteomics 5(2):366-78
Schmidt M, et al.  (2005) The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat Struct Mol Biol 12(4):294-303
Leggett DS, et al.  (2002) Multiple associated proteins regulate proteasome structure and function. Mol Cell 10(3):495-507
Lussier M, et al.  (1997) Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics 147(2):435-50