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Sung-Hou Kim

Researcher at University of California, Berkeley

Publications -  374
Citations -  35180

Sung-Hou Kim is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Protein structure & Structural genomics. The author has an hindex of 93, co-authored 371 publications receiving 34091 citations. Previous affiliations of Sung-Hou Kim include Plexxikon & Korea Institute of Science and Technology.

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Sparse matrix sampling: a screening method for crystallization of proteins

TL;DR: A set of screening conditions for initial experiments in protein crystallization has been developed, tested, and is herein presented as discussed by the authors, which are empirically derived based on known or published crystallization conditions of various proteins in the past, so as to sample as large a range of buffer, pH, additive and precipitant variables as possible, using small amounts of proteins.
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Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity

TL;DR: PLX4720, a 7-azaindole derivative that inhibits B-RafV600E with an IC50 of 13 nM, defines a class of kinase inhibitor with marked selectivity in both biochemical and cellular assays and represents the entire discovery process from initial identification through structural and biological studies in animal models to a promising therapeutic for testing in cancer patients bearing B- RafV 600E-driven tumors.
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Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins

TL;DR: A comparison of eight three-dimensional structures of ras proteins in four different crystal lattices reveals that the "on" and "off" states of the switch are distinguished by conformational differences that span a length of more than 40 A, and are induced by the gamma-phosphate.
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Electron transfer by domain movement in cytochrome bc1.

TL;DR: X-ray crystal structures of the cytochrome bc1 complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron–sulphur protein.
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Crystal structure of cyclin-dependent kinase 2.

TL;DR: The crystal structures of the human CDK2 apoenzyme and its Mg2+ATP complex have been determined to 2.4Å resolution and the structure is bi-lobate, like that of the cyclic AMP-dependent protein kinase, but contains a unique helix—loop segment that interferes with ATP and protein substrate binding.