D
David S. King
Researcher at University of California, Berkeley
Publications - 139
Citations - 17186
David S. King is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Excited state & Peptide sequence. The author has an hindex of 62, co-authored 139 publications receiving 15405 citations. Previous affiliations of David S. King include University of California, Los Angeles & Scripps Research Institute.
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Journal ArticleDOI
Phase transitions in the assembly of multivalent signalling proteins
Pilong Li,Sudeep Banjade,Hui-Chun Cheng,Soyeon Kim,Baoyu Chen,Liang Guo,Marc C. Llaguno,Javoris Hollingsworth,David S. King,Salman F. Banani,Paul S. Russo,Qiu-Xing Jiang,B. Tracy Nixon,Michael K. Rosen +13 more
TL;DR: Interactions between diverse synthetic, multivalent macromolecules (including multi-domain proteins and RNA) produce sharp liquid–liquid-demixing phase separations, generating micrometre-sized liquid droplets in aqueous solution.
Journal ArticleDOI
Phase separation of signaling molecules promotes T cell receptor signal transduction
Xiaolei Su,Xiaolei Su,Jonathon A. Ditlev,Jonathon A. Ditlev,Enfu Hui,Enfu Hui,Wenmin Xing,Wenmin Xing,Sudeep Banjade,Sudeep Banjade,Julia Okrut,Julia Okrut,David S. King,Jack Taunton,Jack Taunton,Michael K. Rosen,Michael K. Rosen,Ronald D. Vale,Ronald D. Vale +18 more
TL;DR: It is demonstrated that protein phase separation can create a distinct physical and biochemical compartment that facilitates signaling and promote signaling outputs both in vitro and in human Jurkat T cells.
Journal ArticleDOI
Structure and Function of a Human TAFII250 Double Bromodomain Module
TL;DR: In this article, it was shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides.
Journal ArticleDOI
Addition of p-Azido-l-phenylalanine to the Genetic Code of Escherichia coli
TL;DR: The selection of a new orthogonal aminoacyl tRNA synthetase/tRNA pair for the in vivo incorporation of a photocrosslinker, p-azido-l-phenylalanine, into proteins in response to the amber codon, TAG, is reported.
Journal ArticleDOI
Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
TL;DR: An orthogonal aminoacyl-tRNA synthetase/tRNA pair is evolved that makes possible the in vivo incorporation of p-benzoyl-l-phenylalanine into proteins in Escherichia coli in response to the amber codon, TAG.