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 - Nature.com
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 - Nature.com
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 - Nature.com
Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex ... - Nature.com
Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex ... - Nature.com
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Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex ...
Nature.com
Solid-state NMR and fluorescence spectroscopy data show that ssDNA binds PLN's cytoplasmic domain specifically, but does not affect SERCA in the absence of the regulatory protein. In particular, NMR spectra show that ssDNA shifts the conformational ...
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NMR reveals novel mechanisms of protein activity regulation.
NMR reveals novel mechanisms of protein activity regulation.
NMR reveals novel mechanisms of protein activity regulation.
Protein Sci. 2011 Mar 14;
Authors: Kalodimos CG
NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide site-resolved information about the conformation entropy of binding, as well as about energetically excited...
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03-16-2011 04:15 PM
[NMR paper] The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of co
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.
Related Articles 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 Apr;7(4):329-35
Authors: Varani L, Gunderson SI, Mattaj IW, Kay LE, Neuhaus D, Varani G
The status of the poly(A) tail at the 3'-end of mRNAs controls the expression of numerous genes in response to...
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 - Nature.com
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