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Global Hairpin Folding of Tau in Solution | Biochemistry
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Global Hairpin Folding of Tau in Solution | Biochemistry
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Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer - Neves - 2021 - The FEBS Journal - Wiley Online Library
7. Specific forms of stalactites and stalagmites formed under the... | Download Scientific Diagram
Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer - Neves - 2021 - The FEBS Journal - Wiley Online Library
Jakub Zytecki
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Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer - Neves - 2021 - The FEBS Journal - Wiley Online Library
Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer - Neves - 2021 - The FEBS Journal - Wiley Online Library
Global Hairpin Folding of Tau in Solution | Biochemistry
Water | Free Full-Text | Ionic Runoff as a Way to Determine the Degree of Karst Denudation (Case Study Jasov Plateau, Slovak Karst, Slovakia)
Global Hairpin Folding of Tau in Solution | Biochemistry
Phosphorylated full‐length Tau interacts with 14‐3‐3 proteins via two short phosphorylated sequences, each occupying a binding groove of 14‐3‐3 dimer - Neves - 2021 - The FEBS Journal - Wiley Online Library
Water | Free Full-Text | Ionic Runoff as a Way to Determine the Degree of Karst Denudation (Case Study Jasov Plateau, Slovak Karst, Slovakia)
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Frontiers | Contemporary biophysical approaches for studying 14-3-3 protein-protein interactions
Fossil freatic passages in the upper parts. Photo: J. Stankovič | Download Scientific Diagram