Site-specific mutagenesis of the N -(deoxyguanosin-8-yl)-2-amino-1-methyl-6-phenylimidazo[4,5- b ]pyridine DNA adduct in mammalian cells

1998 ◽  
Vol 207 (6) ◽  
pp. 459-463 ◽  
Author(s):  
S. Shibutani ◽  
Andrea Fernandes ◽  
Naomi Suzuki ◽  
L. Zhou ◽  
Francis Johnson ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Dna Adduct ◽  
Site Specific

Site-Specific Identification of Lysine Acetylation Stoichiometries in Mammalian Cells

2016 ◽  
Vol 15 (3) ◽  
pp. 1103-1113 ◽  
Author(s):  
Tong Zhou ◽  
Ying-hua Chung ◽  
Jianji Chen ◽  
Yue Chen
Keyword(s):  
Mammalian Cells ◽  
Lysine Acetylation ◽  
Site Specific ◽  
Specific Identification

Comparison of Integrases Identifies Bxb1-GA Mutant as the Most Efficient Site-Specific Integrase System in Mammalian Cells

2019 ◽  
Vol 8 (1) ◽  
pp. 16-24 ◽  
Author(s):  
Barbara Jusiak ◽  
Kalpana Jagtap ◽  
Leonid Gaidukov ◽  
Xavier Duportet ◽  
Kalpanie Bandara ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Site Specific

A diversity of serine phage integrases mediate site-specific recombination in mammalian cells

2006 ◽  
Vol 276 (2) ◽  
Author(s):  
Annahita Keravala ◽  
Amy C. Groth ◽  
Sohail Jarrahian ◽  
Bhaskar Thyagarajan ◽  
Jason J. Hoyt ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Site Specific ◽  
Site Specific Recombination ◽  
Phage Integrases

scholarly journals ‘Traceless’ tracing of proteins – high-affinity trans-splicing directed by a minimal interaction pair

2016 ◽  
Vol 7 (4) ◽  
pp. 2646-2652 ◽  
Author(s):  
M. Braner ◽  
A. Kollmannsperger ◽  
R. Wieneke ◽  
R. Tampé
Keyword(s):  
Mammalian Cells ◽  
Protein Labeling ◽  
Terminal Protein ◽  
Site Specific ◽  
High Affinity ◽  
Trans Splicing

Using a minimal lock-and-key element the affinity between the intein fragments for N-terminal protein trans-splicing was significantly increased, allowing for site-specific, ‘traceless’ covalent protein labeling in living mammalian cells at nanomolar probe concentrations.

scholarly journals Site-Specific Incorporation of Unnatural Amino Acids into Receptors Expressed in Mammalian Cells

2003 ◽  
Vol 10 (6) ◽  
pp. 573-580 ◽  
Author(s):  
Sarah L Monahan ◽  
Henry A Lester ◽  
Dennis A Dougherty
Keyword(s):  
Amino Acids ◽  
Unnatural Amino Acids ◽  
Mammalian Cells ◽  
Site Specific

scholarly journals High-Yield, Zero-Leakage Expression System with a Translational Switch Using Site-Specific Unnatural Amino Acid Incorporation

2013 ◽  
Vol 80 (5) ◽  
pp. 1718-1725 ◽  
Author(s):  
Masaomi Minaba ◽  
Yusuke Kato
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Unnatural Amino Acids ◽  
Mammalian Cells ◽  
Expression System ◽  
Trna Synthetase ◽  
Unnatural Amino Acid ◽  
Translational Efficiency ◽  
Site Specific ◽  
Content Type

ABSTRACTSynthetic biologists construct complex biological circuits by combinations of various genetic parts. Many genetic parts that are orthogonal to one another and are independent of existing cellular processes would be ideal for use in synthetic biology. However, our toolbox is still limited with respect to the bacteriumEscherichia coli, which is important for both research and industrial use. The site-specific incorporation of unnatural amino acids is a technique that incorporates unnatural amino acids into proteins using a modified exogenous aminoacyl-tRNA synthetase/tRNA pair that is orthogonal to any native pairs in a host and is independent from other cellular functions. Focusing on the orthogonality and independency that are suitable for the genetic parts, we designed novel AND gate and translational switches using the unnatural amino acid 3-iodo-l-tyrosine incorporation system inE. coli. A translational switch was turned on after addition of 3-iodo-l-tyrosine in the culture medium within minutes and allowed tuning of switchability and translational efficiency. As an application, we also constructed a gene expression system that produced large amounts of proteins under induction conditions and exhibited zero-leakage expression under repression conditions. Similar translational switches are expected to be applicable also for eukaryotes such as yeasts, nematodes, insects, mammalian cells, and plants.

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