Tobacco Etch Virus protease: A shortcut across biotechnologies.

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Title: Tobacco Etch Virus protease: A shortcut across biotechnologies.
Authors: Cesaratto, Francesca1, Burrone, Oscar R.1 burrone@icgeb.org, Petris, Gianluca2 gianluca.petris@unitn.it
Source: Journal of Biotechnology. Aug2016, Vol. 231, p239-249. 11p.
Subjects: Tobacco etch virus, Proteolytic enzymes, Endopeptidases, Protein engineering
Abstract: About thirty years ago, studies on the RNA genome of Tobacco Etch Virus revealed the presence of an efficient and specific protease, called Tobacco Etch Virus protease (TEVp), that was part of the Nuclear Inclusion a (NIa) enzyme. TEVp is an efficient and specific protease of 27 kDa that has become a valuable biotechnological tool. Nowadays TEVp is a unique endopeptidase largely exploited in biotechnology from industrial applications to in vitro and in vivo cellular studies. A number of TEVp mutants with different rate of cleavage, stability and specificity have been reported. Similarly, a panel of different target cleavage sites, derived from the canonical ENLYFQ-G/S site, has been established. In this review we describe these aspects of TEVp and some of its multiple applications. A particular focus is on the use and molecular biology of TEVp in living cells and organisms. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biotechnology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Tobacco Etch Virus protease: A shortcut across biotechnologies.
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  Data: <searchLink fieldCode="AR" term="%22Cesaratto%2C+Francesca%22">Cesaratto, Francesca</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Burrone%2C+Oscar+R%2E%22">Burrone, Oscar R.</searchLink><relatesTo>1</relatesTo><i> burrone@icgeb.org</i><br /><searchLink fieldCode="AR" term="%22Petris%2C+Gianluca%22">Petris, Gianluca</searchLink><relatesTo>2</relatesTo><i> gianluca.petris@unitn.it</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biotechnology%22">Journal of Biotechnology</searchLink>. Aug2016, Vol. 231, p239-249. 11p.
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  Data: <searchLink fieldCode="DE" term="%22Tobacco+etch+virus%22">Tobacco etch virus</searchLink><br /><searchLink fieldCode="DE" term="%22Proteolytic+enzymes%22">Proteolytic enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Endopeptidases%22">Endopeptidases</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+engineering%22">Protein engineering</searchLink>
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  Label: Abstract
  Group: Ab
  Data: About thirty years ago, studies on the RNA genome of Tobacco Etch Virus revealed the presence of an efficient and specific protease, called Tobacco Etch Virus protease (TEVp), that was part of the Nuclear Inclusion a (NIa) enzyme. TEVp is an efficient and specific protease of 27 kDa that has become a valuable biotechnological tool. Nowadays TEVp is a unique endopeptidase largely exploited in biotechnology from industrial applications to in vitro and in vivo cellular studies. A number of TEVp mutants with different rate of cleavage, stability and specificity have been reported. Similarly, a panel of different target cleavage sites, derived from the canonical ENLYFQ-G/S site, has been established. In this review we describe these aspects of TEVp and some of its multiple applications. A particular focus is on the use and molecular biology of TEVp in living cells and organisms. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Biotechnology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1016/j.jbiotec.2016.06.012
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      – Code: eng
        Text: English
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        PageCount: 11
        StartPage: 239
    Subjects:
      – SubjectFull: Tobacco etch virus
        Type: general
      – SubjectFull: Proteolytic enzymes
        Type: general
      – SubjectFull: Endopeptidases
        Type: general
      – SubjectFull: Protein engineering
        Type: general
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      – TitleFull: Tobacco Etch Virus protease: A shortcut across biotechnologies.
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              Text: Aug2016
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              Value: 231
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