Biomolecular NMR Assignments
Article . 2014 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
1H, 15N and 13C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex
ANR| RNPASSEMBLY
Authors: Xavier, Manival; Clémence, Jacquemin; Bruno, Charpentier; Marc, Quinternet;
pmid: 24493341
1H, 15N and 13C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex
Abstract
We report the nearly complete (1)H, (15)N and (13)C resonance assignment of the complex formed by the C-terminal domains of Pih1 and Tah1 from S. cerevisiae and evidence the folding ability of Tah1 under complex formation.
Related Organizations
Keywords
Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Nuclear Proteins, Amino Acid Sequence, Saccharomyces cerevisiae, Nuclear Magnetic Resonance, Biomolecular, Molecular Chaperones, Protein Structure, Tertiary
Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Nuclear Proteins, Amino Acid Sequence, Saccharomyces cerevisiae, Nuclear Magnetic Resonance, Biomolecular, Molecular Chaperones, Protein Structure, Tertiary
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citations
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This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
popularity
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This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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