about
The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesisShort N-terminal sequences package proteins into bacterial microcompartments.Exploring the substrate range of wild-type aminoacyl-tRNA synthetases.The N-terminal region of the medium subunit (PduD) packages adenosylcobalamin-dependent diol dehydratase (PduCDE) into the Pdu microcompartmentGenetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella.Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments.Rationally evolving tRNAPyl for efficient incorporation of noncanonical amino acidsEvolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids.Dual Genetic Encoding of Acetyl-lysine and Non-deacetylatable Thioacetyl-lysine Mediated by FlexizymeExpanding the genetic code of Salmonella with non-canonical amino acids.Expanding the genetic code of Escherichia coli with phosphotyrosine.Genetically encoding thioacetyl-lysine as a non-deacetylatable analog of lysine acetylation in Escherichia coli.Increasing the fidelity of noncanonical amino acid incorporation in cell-free protein synthesis.Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously.A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli.Continuous directed evolution of aminoacyl-tRNA synthetases.Biochemical Characterization of the Lysine Acetylation of Tyrosyl-tRNA Synthetase in Escherichia coli.Studying the Lysine Acetylation of Malate Dehydrogenase.Genome-Wide Quantification of the Effect of Gene Overexpression on GrowthCharacterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coliRecent Development of Genetic Code Expansion for Posttranslational Modification StudiesSite-Specifically Studying Lysine Acetylation of Aminoacyl-tRNA SynthetasesCharacterizing lysine acetylation of Escherichia coli type II citrate synthaseCatalytic Activity, Stability, and Loading Trends of Alcohol Dehydrogenase Enzyme Encapsulated in a Metal-Organic Framework
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Chenguang Fan
@ast
Chenguang Fan
@en
Chenguang Fan
@es
Chenguang Fan
@nl
Chenguang Fan
@sl
type
label
Chenguang Fan
@ast
Chenguang Fan
@en
Chenguang Fan
@es
Chenguang Fan
@nl
Chenguang Fan
@sl
prefLabel
Chenguang Fan
@ast
Chenguang Fan
@en
Chenguang Fan
@es
Chenguang Fan
@nl
Chenguang Fan
@sl
P106
P31
P496
0000-0003-0662-1185