Michael Thirman to Peptide Elongation Factors
This is a "connection" page, showing publications Michael Thirman has written about Peptide Elongation Factors.
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0.993
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ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. Mol Biol Cell. 2003 Apr; 14(4):1517-28.
Score: 0.194
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The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesis. Mol Cell Biol. 2001 Aug; 21(16):5678-87.
Score: 0.173
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EAF1, a novel ELL-associated factor that is delocalized by expression of the MLL-ELL fusion protein. Blood. 2001 Jul 01; 98(1):201-9.
Score: 0.172
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Retrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice. Proc Natl Acad Sci U S A. 2000 Sep 26; 97(20):10984-9.
Score: 0.163
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Developmental analysis and subcellular localization of the murine homologue of ELL. Proc Natl Acad Sci U S A. 1997 Feb 18; 94(4):1408-13.
Score: 0.127
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Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute myeloid leukemia. Proc Natl Acad Sci U S A. 1994 Dec 06; 91(25):12110-4.
Score: 0.109
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The elongation factor ELL (eleven-nineteen lysine-rich leukemia) is a selective coregulator for steroid receptor functions. Mol Endocrinol. 2005 May; 19(5):1158-69.
Score: 0.055