BTT1/YDR252W Literature Guide Help

Other names published for BTT1: YDR252W

BTT1 - Additional Literature (14)

ReferenceOther Genes Addressed
Seresht AK, et al.  (2013) Long-term adaptation of Saccharomyces cerevisiae to the burden of recombinant insulin production. Biotechnol Bioeng ()
Jacobson T, et al.  (2012) Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125(Pt 21):5073-83
Venters BJ, et al.  (2011) A comprehensive genomic binding map of gene and chromatin regulatory proteins in Saccharomyces. Mol Cell 41(4):480-92
Pech M, et al.  (2010) Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome. J Biol Chem 285(25):19679-87
Zanders S, et al.  (2010) Detection of heterozygous mutations in the genome of mismatch repair defective diploid yeast using a bayesian approach. Genetics 186(2):493-503
Takahashi T, et al.  (2009) Dysfunctional nascent polypeptide-associated complex (NAC) activity in ribosomes enhances adriamycin toxicity in budding yeast. J Toxicol Sci 34(6):703-8
Dalley JA, et al.  (2008) Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation. Mol Biol Cell 19(7):2876-84
Grallath S, et al.  (2007) L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep 8(11):1086
Grallath S, et al.  (2006) L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep 7(1):78-84
Panasenko O, et al.  (2006) The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex. J Biol Chem 281(42):31389-98
Spreter T, et al.  (2005) The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain. J Biol Chem 280(16):15849-54
George R, et al.  (2002) The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo. FEBS Lett 516(1-3):213-6
Potashkin J, et al.  (1996) BTF3 is evolutionarily conserved in fission yeast. Biochim Biophys Acta 1308(3):182-4
Kellems RE and Butow RA  (1974) Cytoplasmic type 80 S ribosomes associated with yeast mitochondria. 3. Changes in the amount of bound ribosomes in response to changes in metabolic state. J Biol Chem 249(10):3304-10