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Joseph L. Kim

Researcher at Amgen

Publications -  71
Citations -  5790

Joseph L. Kim is an academic researcher from Amgen. The author has contributed to research in topics: Hepatitis C virus & Cancer. The author has an hindex of 28, co-authored 69 publications receiving 5586 citations. Previous affiliations of Joseph L. Kim include Howard Hughes Medical Institute & Vertex Pharmaceuticals.

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Co-crystal structure of TBP recognizing the minor groove of a TATA element

TL;DR: The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 Å resolution.
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X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex

TL;DR: The ternary complex described here represents the three-dimensional structure of a Ser/Thr protein phosphatase and provides a structural basis for understanding calcineurin inhibition by FKBP12-FK506.
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Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide.

TL;DR: The 2.5 angstrom resolution X-ray crystal structure of the NS3 protease domain complexed with a synthetic NS4A activator peptide is reported, which shows a chymotrypsin-like fold and features a tetrahedrally coordinated metal ion distal to the active site.
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Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

TL;DR: The structure of the HCV NS3 RNA helicase domain complexed with a single-stranded DNA oligonucleotide has been solved to 2.2 A resolution and is a member of a superfamily of helicases, termed superfamily II.
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TATA Element Recognition by the TATA Box-Binding Protein Has Been Conserved Throughout Evolution

TL;DR: It is concluded that the structure of the TBP-TATA box complex found at the heart of the polymerase II (pol II) transcription machinery has remained constant over the course of evolution, despite variations in TBP and its DNA targets.