Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

MyNCBI Filters
Results by year

Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1983 2
1984 1
1986 23
1987 93
1988 123
1989 138
1990 198
1991 255
1992 365
1993 673
1994 1044
1995 1329
1996 972
1997 1080
1998 851
1999 716
2000 544
2001 369
2002 301
2003 335
2004 340
2005 352
2006 339
2007 249
2008 265
2009 301
2010 275
2011 311
2012 306
2013 309
2014 265
2015 218
2016 178
2017 162
2018 95
2019 34
2020 0
Text availability
Article attribute
Article type
Publication date

Search Results

12,961 results
Results by year
Filters applied: . Clear all
Page 1
Overview of Fusion Tags for Recombinant Proteins.
Kosobokova EN, et al. Biochemistry (Mosc) 2016 - Review. PMID 27262188
Virtually all recombinant proteins are now prepared using fusion domains also known as "tags". The use of tags helps to solve some serious problems: to simplify procedures of protein isolation, to increase expression and solubility of the desired protein, to simplify protein refolding and increase its efficiency, and to prevent proteolysis. In this review, advantages and disadvantages of such fusion tags are analyzed and data on both well-known and new tags are generalized. ...
Virtually all recombinant proteins are now prepared using fusion domains also known as "tags". The use of tags helps to …
Single-step affinity and cost-effective purification of recombinant proteins using the Sepharose-binding lectin-tag from the mushroom Laetiporus sulphureus as fusion partner.
Li XJ, et al. Protein Expr Purif 2016. PMID 26616099
Fusion proteins of LSL-tag and porcine circovirus capsid protein, designated LSL-Cap was recovered with purity of 90 ± 4%, and yield of 87 ± 3% from crude extract of recombinant Escherichia coli. ...The LSL affinity purification method enables rapid and inexpensive purification of LSL-tagged fusion proteins and scale-up production of native proteins....
Fusion proteins of LSL-tag and porcine circovirus capsid protein, designated LSL-Cap was recovered with purity of 90 ± 4%, and
The Use of Affinity Tags to Overcome Obstacles in Recombinant Protein Expression and Purification.
Amarasinghe C and Jin JP. Protein Pept Lett 2015 - Review. PMID 26216265
Research and industrial demands for recombinant proteins continue to increase over time for their broad applications in structural and functional studies and as therapeutic agents. ...This focused review compares and contrasts various strategies that employ affinity tags to improve bacterial expression and to facilitate purification of recombinant proteins. ...
Research and industrial demands for recombinant proteins continue to increase over time for their broad applications in struct …
Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications.
Young CL, et al. Biotechnol J 2012 - Review. PMID 22442034
Protein fusion tags are indispensible tools used to improve recombinant protein expression yields, enable protein purification, and accelerate the characterization of protein structure and function. ...This review serves as an excellent literature reference for those working on protein fusion tags....
Protein fusion tags are indispensible tools used to improve recombinant protein expression yields, enable protein purification …
HaloTag technology for specific and covalent labeling of fusion proteins.
Benink HA and Urh M. Methods Mol Biol 2015. PMID 25560071
Appending proteins of interest to fluorescent protein tags such as GFP has revolutionized how proteins are studied in the cellular environment. ...In this way a single genetically encoded protein fusion can easily be given functional diversity and adaptability as supplied by synthetic chemistry. ...
Appending proteins of interest to fluorescent protein tags such as GFP has revolutionized how proteins are studied in the cell …
Construction of Lasso Peptide Fusion Proteins.
Zong C, et al. ACS Chem Biol 2016. PMID 26492187 Free PMC article.
Here, we demonstrate fusion of two model proteins, the artificial leucine zipper A1 and the superfolder variant of GFP, to the C-terminus of the lasso peptide astexin-1. Successful lasso cyclization of the N-terminus of these fusion proteins requires a flexible linker in between the C-terminus of the lasso peptide and the N-terminus of the protein of interest. ...
Here, we demonstrate fusion of two model proteins, the artificial leucine zipper A1 and the superfolder variant of GFP, to the …
Production, Purification, and Characterization of Antibody-TNF Superfamily Ligand Fusion Proteins.
Siegemund M, et al. Methods Mol Biol 2018. PMID 30196506
Antibody-fusion proteins with ligands, e.g., of the TNF superfamily (TNFSF) can be adequately produced in mammalian expression systems. ...In addition, characterization of the purified proteins by size exclusion chromatography is described....
Antibody-fusion proteins with ligands, e.g., of the TNF superfamily (TNFSF) can be adequately produced in mammalian expression …
Enhancement of soluble protein expression through the use of fusion tags.
Esposito D and Chatterjee DK. Curr Opin Biotechnol 2006 - Review. PMID 16781139
The soluble expression of heterologous proteins in Escherichia coli remains a serious bottleneck in protein production. Although alteration of expression conditions can sometimes solve the problem, the best available tools to date have been fusion tags that enhance the solubility of expressed proteins. ...This data should allow us to better predict the effectiveness of tags currently in use, and might also provide the information needed to identify new fusion tags....
The soluble expression of heterologous proteins in Escherichia coli remains a serious bottleneck in protein production. Although alte …
Expression and purification of soluble monomeric streptavidin in Escherichia coli
Demonte D, et al. Appl Microbiol Biotechnol 2014. PMID 24691867
The fusion proteins can be expressed solubly in E. coli and increase the yield by more than 20-fold. Unmodified mSA can be obtained by proteolytically removing the fusion tag. ...Together, expressing mSA as a fusion with a solubilization tag vastly simplifies its preparation and increases its usability in biotechnology....
The fusion proteins can be expressed solubly in E. coli and increase the yield by more than 20-fold. Unmodified mSA can be obt …
Strategies for achieving high-level expression of genes in Escherichia coli
Makrides SC. Microbiol Rev 1996 - Review. PMID 8840785 Free PMC article.
The remarkable increase in the availability of fusion partners offers a wide range of tools for improved protein folding, solubility, protection from proteases, yield, and secretion into the culture medium, as well as for detection and purification of recombinant proteins. ...Finally, the elucidation of specific determinants of protein degradation, a plethora of protease-deficient host strains, and methods to stabilize proteins afford new strategies to minimize proteolytic susceptibility of recombinant proteins in E. coli....
The remarkable increase in the availability of fusion partners offers a wide range of tools for improved protein folding, solubility, …
12,961 results
Jump to page
Feedback