The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein. [Nat Struct Biol. 2000]
The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.
Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G. Nat Struct Biol. 2000 Apr; 7(4):329-35.
A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. [Cell. 2000]
A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.
Grosset C, Chen CY, Xu N, Sonenberg N, Jacquemin-Sablon H, Shyu AB. Cell. 2000 Sep 29; 103(1):29-40.
Poly(A) tail length-dependent stabilization of GAP-43 mRNA by the RNA-binding protein HuD. [J Biol Chem. 2002]
Poly(A) tail length-dependent stabilization of GAP-43 mRNA by the RNA-binding protein HuD.
Beckel-Mitchener AC, Miera A, Keller R, Perrone-Bizzozero NI. J Biol Chem. 2002 Aug 2; 277(31):27996-8002. Epub 2002 May 28.
Review Hypothetical double-helical poly(A) formation in a cell and its possible biological significance. [IUBMB Life. 1999]
Review Hypothetical double-helical poly(A) formation in a cell and its possible biological significance.
Zarudnaya MI, Hovorun DM. IUBMB Life. 1999 Dec; 48(6):581-4.
Review Cytoplasmic deadenylation: regulation of mRNA fate. [Biochem Soc Trans. 2010]
Review Cytoplasmic deadenylation: regulation of mRNA fate.
Wiederhold K, Passmore LA. Biochem Soc Trans. 2010 Dec; 38(6):1531-6.

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