scholarly journals Identification and validation of four novel promoters for gene engineering with broad suitability across species

2021 ◽  
Author(s):  
Cai-Yun Wang ◽  
Li-Cheng Liu ◽  
Ying-Cai Wu ◽  
Yi-Xuan Zhang
Keyword(s):  
Gene Engineering

Microbiology illuminated: gene engineering and bioluminescence

1991 ◽  
Vol 2 ◽  
pp. 7-10 ◽  
Author(s):  
Gordon S.A.B. Stewart ◽  
Stephen P. Denyer ◽  
Jay Lewington
Keyword(s):  
Gene Engineering

scholarly journals Safety and efficiency of therapy by gene-engineering-biological preparations of rheumatoid arthritis

2018 ◽  
Vol 9 (3) ◽  
pp. 44-49
Author(s):  
E. A. Strel’tsov
Keyword(s):  
Rheumatoid Arthritis ◽  
Literature Search ◽  
Randomized Trials ◽  
Web Of Science ◽  
Genetically Engineered ◽  
Systematic Literature Search ◽  
Efficacy And Safety ◽  
Review Of The Literature ◽  
Gene Engineering

In this review of the literature, questions of the efficacy and safety of therapy with genetically engineered biological preparations for rheumatoid arthritis are discussed. The results of randomized trials of recent years are described in detail. Systematic literature search was conducted on the databases Scopus, Web of Science, MedLine, elibrary and others.

ADJUSTMENT OF THE CONCEPTED APPARATUS IN THE FIELD OF GENE ENGINEERING FOR THE FORMATION OF PRODUCT-ORIENTED LEGISLATION

2020 ◽  
pp. 338-339
Keyword(s):  
Conceptual Framework ◽  
Legal Regulation ◽  
Innovative Development ◽  
Gene Engineering

The issues of legal regulation of GMOs in Russia are reviewed. It is shown that for transformation to innovative development, it is necessary to correct the conceptual framework and develop product-oriented legislation.

scholarly journals Versatile format of minichaperone-based protein fusion system

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Maria S. Yurkova ◽  
Olga A. Sharapova ◽  
Vladimir A. Zenin ◽  
Alexey N. Fedorov
Keyword(s):  
Recombinant Proteins ◽  
Inclusion Bodies ◽  
Target Protein ◽  
Fusion System ◽  
Protein Fusion ◽  
Gene Engineering ◽  
Apical Domain ◽  
Stable Forms ◽  
Protein Variants ◽  
Protein Moiety

Abstract Hydrophobic recombinant proteins often tend to aggregate upon expression into inclusion bodies and are difficult to refold. Producing them in soluble forms constitutes a common bottleneck problem. A fusion system for production of insoluble hydrophobic proteins in soluble stable forms with thermophilic minichaperone, GroEL apical domain (GrAD) as a carrier, has recently been developed. To provide the utmost flexibility of the system for interactions between the carrier and various target protein moieties a strategy of making permutated protein variants by gene engineering has been applied: the original N- and C-termini of the minichaperone were linked together by a polypeptide linker and new N- and C-termini were made at desired parts of the protein surface. Two permutated GrAD forms were created and analyzed. Constructs of GrAD and both of its permutated forms fused with the initially insoluble N-terminal fragment of hepatitis C virus’ E2 protein were tested. Expressed fusions formed inclusion bodies. After denaturation, all fusions were completely renatured in stable soluble forms. A variety of permutated GrAD variants can be created. The versatile format of the system provides opportunities for choosing an optimal pair between particular target protein moiety and the best-suited original or specific permutated carrier.

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