Literature DB >> 16305545

Incorporation of selenocysteine into proteins using peptide ligation.

Robert J Hondal1.   

Abstract

Expressed protein ligation has become a frequently used technique to insert non-standard amino acids into proteins. The technique has been adapted to insert selenocysteine residues in place of cysteine residue in proteins, taking advantage of the similarity in the chemistries of sulfur and selenium. This replacement can confer unique structural and catalytic properties to enzymes and proteins. The development of this technique also allows for naturally occurring selenoproteins to be produced semisynthetically.

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Year:  2005        PMID: 16305545      PMCID: PMC3683319          DOI: 10.2174/0929866054864319

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  51 in total

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Journal:  Science       Date:  1999-08-27       Impact factor: 47.728

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Authors:  M D Gieselman; L Xie; W A van Der Donk
Journal:  Org Lett       Date:  2001-05-03       Impact factor: 6.005

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Journal:  Annu Rev Biochem       Date:  1996       Impact factor: 23.643

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Authors:  T C Evans; J Benner; M Q Xu
Journal:  Protein Sci       Date:  1998-11       Impact factor: 6.725

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Journal:  J Pept Sci       Date:  1997 Nov-Dec       Impact factor: 1.905

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Journal:  Methods Enzymol       Date:  1987       Impact factor: 1.600

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Authors:  F Zinoni; A Birkmann; T C Stadtman; A Böck
Journal:  Proc Natl Acad Sci U S A       Date:  1986-07       Impact factor: 11.205

9.  Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity.

Authors:  S Bar-Noy; S N Gorlatov; T C Stadtman
Journal:  Free Radic Biol Med       Date:  2001-01-01       Impact factor: 7.376

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Authors:  D Theodoropoulos; I L Schwartz; R Walter
Journal:  Biochemistry       Date:  1967-12       Impact factor: 3.162

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  8 in total

1.  Expressed protein ligation for metalloprotein design and engineering.

Authors:  Kevin M Clark; Wilfred A van der Donk; Yi Lu
Journal:  Methods Enzymol       Date:  2009       Impact factor: 1.600

2.  Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations.

Authors:  Jun Liu; Qingqing Chen; Sharon Rozovsky
Journal:  J Am Chem Soc       Date:  2017-02-27       Impact factor: 15.419

3.  Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.

Authors:  Jun Liu; Qingqing Chen; Sharon Rozovsky
Journal:  Methods Mol Biol       Date:  2018

4.  Studies on deprotection of cysteine and selenocysteine side-chain protecting groups.

Authors:  Katharine M Harris; Stevenson Flemer; Robert J Hondal
Journal:  J Pept Sci       Date:  2007-02       Impact factor: 1.905

5.  Semisynthesis and characterization of mammalian thioredoxin reductase.

Authors:  Brian Eckenroth; Katharine Harris; Anton A Turanov; Vadim N Gladyshev; Ronald T Raines; Robert J Hondal
Journal:  Biochemistry       Date:  2006-04-25       Impact factor: 3.162

Review 6.  Using chemical approaches to study selenoproteins-focus on thioredoxin reductases.

Authors:  Robert J Hondal
Journal:  Biochim Biophys Acta       Date:  2009-05-04

Review 7.  Selenocysteine in thiol/disulfide-like exchange reactions.

Authors:  Robert J Hondal; Stefano M Marino; Vadim N Gladyshev
Journal:  Antioxid Redox Signal       Date:  2012-12-16       Impact factor: 8.401

8.  Application of dehydroalanine as a building block for the synthesis of selenocysteine-containing peptides.

Authors:  Kishorkumar M Reddy; Govindasamy Mugesh
Journal:  RSC Adv       Date:  2018-12-20       Impact factor: 3.361

  8 in total

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