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

Year Number of Results
1945 1
1946 1
1948 1
1951 2
1952 1
1954 1
1955 2
1956 2
1957 3
1958 2
1959 2
1960 2
1961 4
1962 2
1963 4
1964 3
1971 1
1977 1
1978 1
1981 2
1982 39
1983 6
1984 10
1985 247
1986 1045
1987 1884
1988 2602
1989 3673
1990 5253
1991 6333
1992 7635
1993 9276
1994 10513
1995 12491
1996 12921
1997 12657
1998 13090
1999 13542
2000 14161
2001 13401
2002 13681
2003 14116
2004 14036
2005 13258
2006 13379
2007 12879
2008 12439
2009 12678
2010 12428
2011 12331
2012 11910
2013 11328
2014 10556
2015 10401
2016 9200
2017 9003
2018 7274
2019 3233
2020 44
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322,855 results
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Page 1
Overview of the purification of recombinant proteins.
Wingfield PT. Curr Protoc Protein Sci 2015 - Review. PMID 25829302 Free PMC article.
When the first version of this unit was written in 1995, protein purification of recombinant proteins was based on a variety of standard chromatographic methods and approaches, many of which were described and mentioned throughout Current Protocols in Protein Science. ...This may not be the case for biotechnology manufacture where affinity tags can complicate producing proteins under regulatory conditions. ...
When the first version of this unit was written in 1995, protein purification of recombinant proteins was based on a variety o …
General introduction: recombinant protein production and purification of insoluble proteins.
Ferrer-Miralles N, et al. Methods Mol Biol 2015 - Review. PMID 25447856
The production of soluble and functional recombinant proteins is among the main goals in the biotechnological field. In this context, it is important to point out that under stress conditions, protein folding machinery is saturated and this promotes protein misfolding and, consequently, protein aggregation. ...Escherichia coli is the most popular recombinant protein expression system despite the great development achieved so far by eukaryotic expression systems. ...
The production of soluble and functional recombinant proteins is among the main goals in the biotechnological field. In this c …
Guidelines to reach high-quality purified recombinant proteins.
Oliveira C and Domingues L. Appl Microbiol Biotechnol 2018 - Review. PMID 29151158
Therefore, this review aims at providing succinct information on the rational purification design of recombinant proteins produced in Escherichia coli, specifically the tagging purification, as well as on accessible tools for evaluating and optimizing protein quality. ...The guidelines compiled herein will aid preparing pure, soluble and homogeneous functional recombinant proteins from the very beginning of the molecular cloning design....
Therefore, this review aims at providing succinct information on the rational purification design of recombinant proteins prod …
Production of recombinant proteins from Plasmodium falciparum in Escherichia coli.
Guerra ÁP, et al. Biomedica 2016. PMID 27622630 Free article.
INTRODUCTION: The production of recombinant proteins is essential for the characterization and functional study of proteins from Plasmodium falciparum. However, the proteins of P. falciparum are among the most challenging to express, and when expression is achieved, the recombinant proteins usually fold incorrectly and lead to the formation of inclusion bodies.  ...
INTRODUCTION: The production of recombinant proteins is essential for the characterization and functional study of proteins
Production of prone-to-aggregate proteins.
Lebendiker M and Danieli T. FEBS Lett 2014 - Review. PMID 24211444 Free article.
Expression of recombinant proteins in Escherichia coli (E. coli) remains the most popular and cost-effective method for producing proteins in basic research and for pharmaceutical applications. Despite accumulating experience and methodologies developed over the years, production of recombinant proteins prone to aggregate in E. coli-based systems poses a major challenge in most research applications. ...
Expression of recombinant proteins in Escherichia coli (E. coli) remains the most popular and cost-effective method for produc …
Optimization of protein purification and characterization using Thermofluor screens
Boivin S, et al. Protein Expr Purif 2013 - Review. PMID 23948764
The efficient large scale production of recombinant proteins depends on the careful conditioning of the protein as it is isolated and purified to homogeneity. ...The second screen contains small molecules that can affect the folding, aggregation state and solubility of the protein construct and also includes small molecules that specifically bind and stabilize proteins. ...
The efficient large scale production of recombinant proteins depends on the careful conditioning of the protein as it is isola …
Quality Screening of Incorrectly Folded Soluble Aggregates from Functional Recombinant Proteins.
Kwon SB, et al. Int J Mol Sci 2019. PMID 30791505 Free PMC article.
Solubility is the prime criterion for determining the quality of recombinant proteins, yet it often fails to represent functional activity due to the involvement of non-functional, misfolded, soluble aggregates, which compromise the quality of recombinant proteins. ...Using the aggregation-prone enhanced green-fluorescent protein (EGFP) folding reporter system, we evaluated the folding status of recombinant proteins by employing the commonly used sonication and mild lysis of recombinant host cells. ...
Solubility is the prime criterion for determining the quality of recombinant proteins, yet it often fails to represent functio …
Optimization of Protein Expression in Mammalian Cells
Hunter M, et al. Curr Protoc Protein Sci 2019 - Review. PMID 30265450
In both the industrial and academic environments, the use of recombinant proteins varies widely and, with it, the method of production. ...Here, we elaborate on the various obstacles encountered when planning high-yield experiments to produce the recombinant proteins of interest. © 2018 by John Wiley & Sons, Inc....
In both the industrial and academic environments, the use of recombinant proteins varies widely and, with it, the method of pr …
Production of recombinant dengue non-structural 1 (NS1) proteins from clinical virus isolates.
Yohan B, et al. Protein Expr Purif 2017. PMID 27650871
Recombinant NS1 proteins were successfully purified and their antigenicities were assessed. Immunization of mice with recombinant proteins observed the immunogenicity of the NS1 protein. The generated recombinant proteins can be potentially used in the development of NS1 diagnostic test. With minimal modifications, this method can be used for producing NS1 recombinant proteins from isolates obtained from other geographical regions....
Recombinant NS1 proteins were successfully purified and their antigenicities were assessed. Immunization of mice with recom
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