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Chao Zhang

Researcher at Beihang University

Publications -  4347
Citations -  118320

Chao Zhang is an academic researcher from Beihang University. The author has contributed to research in topics: Medicine & Computer science. The author has an hindex of 127, co-authored 3119 publications receiving 84711 citations. Previous affiliations of Chao Zhang include West Virginia University & University of Oklahoma.

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Protein Kinase Cδ Regulates Ethanol Intoxication and Enhancement of GABA-Stimulated Tonic Current

TL;DR: In this article, the authors investigated whether PKCδ also regulates behavioral responses to ethanol and found that PKC−/− mice showed reduced intoxication when administered ethanol and reduced ataxia when administered the nonselective GABAA receptor agonists pentobarbital and pregnanolone.
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Protein engineering of protein kinase A catalytic subunits results in the acquisition of novel inhibitor sensitivity.

TL;DR: This method is used to create protein kinase A (PKA) catalytic subunits with modifications that confer sensitivity to novel ATP analog inhibitors and should allow analysis of the specific roles of PKA isoforms in cell culture and in vivo.
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Constraints from experimental melting of amphibolite on the depth of formation of garnet-rich restites, and implications for models of Early Archean crustal growth

TL;DR: In this paper, the authors present results of amphibolite dehydration-melting experiments at pressures of 5-15kbar and provide constraints on melting reactions of a hydrated metabasalt with SiO2 of 47.5% and Al2O3 of 16.4%.
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Surface Plasmon Resonance in Bimetallic Core–Shell Nanoparticles

TL;DR: In this paper, the Mie theory was used to investigate the surface plasmon resonance (SPR) properties of bimetallic core-shell nanoparticles having a spherical shape and consisting of Drude metals.
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A Viral Deamidase Targets the Helicase Domain of RIG-I to Block RNA-Induced Activation

TL;DR: It is reported here that UL37 of herpes simplex virus 1 (HSV-1) is a protein deamidase that targets RIG-I to block RNA-induced activation and restrict viral replication.