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Recombination genes and proteins

Current Opinion in Genetics & Development, 1994
The recombination of DNA takes place by a multistep process involving numerous gene products. In the past year, studies using bacterial proteins have led to a number of significant advances in our understanding of the enzymes of recombination and of the reactions that they catalyze.
Stephen C. West, Hazel J. Dunderdale
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Recombination Proteins in Yeast

Annual Review of Genetics, 2004
▪ Abstract  The process of homologous recombination promotes error-free repair of double-strand breaks and is essential for meiosis. Central to the process of homologous recombination are the RAD52 group genes (RAD50, RAD51, RAD52, RAD54, RDH54/TID1, RAD55, RAD57, RAD59, MRE11, and XRS2), most of which were identified by their requirement for the ...
Berit Olsen Krogh, Lorraine S. Symington
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Recombinant proteins for therapy

Trends in Pharmacological Sciences, 1996
Recombinant therapeutic proteins have become increasingly important over the past ten years. Numerous products derived from 20 different proteins are already on the market. In this review Peter Buckel discusses the issues surrounding the use of recombinant proteins as therapeutic agents.
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Recombinant Protein Production in Yeasts

Molecular Biotechnology, 2005
Recombinant DNA (rDNA) technologies (genetic, protein, and metabolic engineering) allow the production of a wide range of peptides, proteins, and biochemicals from naturally nonproducing cells. These technologies, now approx 25 yr old, have become one of the most important technologies developed in the twentieth century.
PORRO, DANILO   +3 more
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Recombinant Protein Techniques [PDF]

open access: possible, 1996
The isolation and characterization of proteins parallels the major technical advances in protein chemistry. The first proteins that were characterized were those that could be isolated in large quantities. With the availability of more sensitive techniques, smaller and smaller quantities were required to produce detailed structural information.
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[28] Characterization of recombinant proteins

1990
Publisher Summary This chapter discusses characterization of recombinant proteins. The therapeutic utility of a recombinant protein is profoundly influenced by its macromolecular structure. The structural features that influence biological response may vary widely depending on the cell type used as the host expression system and the conditions under ...
Hubert A. Scoble, Stephen A. Martin
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Refolding of recombinant proteins

Current Opinion in Biotechnology, 1998
Expression of recombinant proteins as inclusion bodies in bacteria is one of the most efficient ways to produce cloned proteins, as long as the inclusion body protein can be successfully refolded. Aggregation is the leading cause of decreased refolding yields.
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Insights on the Formulation of Recombinant Proteins

2019
Recombinant proteins are large and complex molecules, whose therapeutic activity highly depends on their structure. Formulation of biopharmaceuticals aims at stabilizing protein conformation, promoting its efficacy, and preventing safety concerns, such as immunogenicity. Currently, the rational design of formulations is possible due to the availability
Ribeiro, Rita   +4 more
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Recombinant Protein Production in Yeasts

2011
Recombinant protein production is a multibillion-dollar market. The development of a new product begins with the choice of a production host. While one single perfect host for every protein does not exist, several expression systems ranging from bacterial hosts to mammalian cells have been established.
Mattanovich, D   +5 more
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Overview of the Characterization of Recombinant Proteins

Current Protocols in Protein Science, 1995
AbstractThis overview provides guidelines for the characterization of recombinantly expressed proteins (e.g., verifying primary structure and appropriate post‐translational modifications), along with methodologies for characterizing the proteins according to size, X‐ray structure, absorbance, biological activity, and subunit structure.
Keith Rose   +2 more
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