C
C. Cheng Kao
Researcher at Indiana University
Publications - 184
Citations - 12124
C. Cheng Kao is an academic researcher from Indiana University. The author has contributed to research in topics: RNA & RNA-dependent RNA polymerase. The author has an hindex of 63, co-authored 183 publications receiving 11103 citations. Previous affiliations of C. Cheng Kao include Texas A&M University & University of California, Santa Barbara.
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Journal ArticleDOI
Cyclic GMP-AMP Synthase is Activated by Double-stranded DNA-Induced Oligomerization
Xin Li,Chang Shu,Guanghui Yi,Catherine T. Chaton,Catherine L. Shelton,Jiasheng Diao,Xiaobing Zuo,C. Cheng Kao,Andrew B. Herr,Pingwei Li +9 more
TL;DR: Results demonstrated that cGAS is activated by dsDNA-induced oligomerization and that site B plays a critical role in DNA binding.
Journal ArticleDOI
An oligomeric signaling platform formed by the Toll-like receptor signal transducers MyD88 and IRAK-4.
Precious G. Motshwene,Martin C. Moncrieffe,Jorg Gunter Grossmann,C. Cheng Kao,Murali Ayaluru,Alan M. Sandercock,Carol V. Robinson,Eicke Latz +7 more
TL;DR: These findings indicate that TLR activation causes the formation of a highly oligomeric signaling platform analogous to the death-inducing signaling complex of the Fas receptor pathway.
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Adenovirus E1A activation domain binds the basic repeat in the TATA box transcription factor
TL;DR: It is demonstrated that the activation domain of E1A (conserved region 3) binds to TFIID, the general polymerase II transcription factor that initiates assembly of transcription complexes.
Journal ArticleDOI
Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure.
Erin K. O'Reilly,C. Cheng Kao +1 more
TL;DR: Whether all RdRps will have structures similar to those found in the poliovirus polymerase structure is addressed and structural predictions are used to explain the phenotypes of a collection of mutations that exist in several RNA polymerases.
Journal ArticleDOI
Cloning of a transcriptionally active human TATA binding factor.
TL;DR: The human TFIID polypeptide has 339 amino acids and a molecular size of 37,745 daltons as mentioned in this paper, and the amino terminus contains an unusual repeat of 38 consecutive glutamine residues and an X-Thr-Pro repeat.