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Sam-Yong Park

Researcher at Yokohama City University

Publications -  176
Citations -  7187

Sam-Yong Park is an academic researcher from Yokohama City University. The author has contributed to research in topics: Heme & Cytochrome. The author has an hindex of 43, co-authored 167 publications receiving 6437 citations. Previous affiliations of Sam-Yong Park include Gakushuin University & Japan Atomic Energy Agency.

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Crystal structure of the human centromeric nucleosome containing CENP-A

TL;DR: The structure provides the first atomic-resolution picture of the centromere-specific nucleosome, and it is revealed that CENP-A contains two extra amino acid residues in the loop 1 region, which is completely exposed to the solvent.
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1.25 a resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms.

TL;DR: Improved accuracy of the models clarifies the disagreement between NMR and X-ray studies of oxyHb, and reveals a hydrogen bond in both subunit types, but with subtly different geometry which may explain the very different behaviour when this residue is mutated to glycine in alpha or beta globin.
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Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125

TL;DR: The ternary complex structure of pepJIP1‐bound JNK1 complexed with SP600125, an ATP‐competitive inhibitor of JNK, is determined, providing the basis for the JNK specificity of the compound.
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Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules

TL;DR: The three-dimensional structures of the catalytic domain of human PDE5 complexed with the three drug molecules sildenafil, tadalafil (Cialis) and vardenafils (Levitra) are presented to provide opportunities to design potent and selective PDE inhibitors with improved pharmacological profiles.
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The structural basis for an essential subunit interaction in influenza virus RNA polymerase

TL;DR: It is demonstrated the importance to viral replication of a subunit interface in the viral RNA polymerase, thereby providing a new set of potential drug binding sites entirely independent of surface antigen type.