Synthesis of post-translationally modified proteins

被引：10
|
作者：
van Kasteren, Sander [1 ]
机构：
[1] Netherlands Canc Inst NKI, Div Cell Biol 2, Biol Chem Lab, NL-1066 CX Amsterdam, Netherlands
来源：
BIOCHEMICAL SOCIETY TRANSACTIONS | 2012年 / 40卷
基金：
英国惠康基金;
关键词：
amber codon suppression; expressed protein ligation (EPL); modiform; native chemical ligation (NCL); post-translational modification (PTM); semi-synthesis; SITE-SPECIFIC INCORPORATION; UNNATURAL AMINO-ACIDS; GENETIC-CODE; TYROSINE PHOSPHORYLATION; ESCHERICHIA-COLI; CHEMICAL BIOLOGY; IN-VIVO; GLYCOPROTEIN-SYNTHESIS; RECOMBINANT PROTEINS; FIREFLY LUCIFERASE;
D O I：
10.1042/BST20120144
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Post-translational modifications of proteins can have dramatic effect on the function of proteins. Significant research effort has gone into understanding the effect of particular modifications on protein parameters. In the present paper, I review some of the recently developed tools for the synthesis of proteins modified with single post-translational modifications at specific sites in the protein, such as amber codon suppression technologies, tag and modify, and native chemical ligation.
引用
收藏
页码：929 / 944
页数：16
相关论文
共 50 条
  • [31] CENTROSOMES, CENTRIOLES AND POST-TRANSLATIONALLY MODIFIED MICROTUBULES DURING FERTILIZATION
    SCHATTEN, H
    HOWARD, C
    COFFE, G
    SIMERLY, C
    SCHATTEN, G
    ZOOLOGICAL SCIENCE, 1988, 5 (03) : 585 - 601
  • [32] Post-translationally modified conopeptides: Biological activities and pharmacological applications
    Jimenez, Elsie C.
    PEPTIDES, 2021, 139
  • [33] Antibodies to post-translationally modified insulin in type 1 diabetes
    Strollo, Rocky
    Vinci, Chiara
    Arshad, Mayda H.
    Perrett, David
    Tiberti, Claudio
    Chiarelli, Francesco
    Napoli, Nicola
    Pozzilli, Paolo
    Nissim, Ahuva
    DIABETOLOGIA, 2015, 58 (12) : 2851 - 2860
  • [34] Antibodies to post-translationally modified insulin in type 1 diabetes
    Rocky Strollo
    Chiara Vinci
    Mayda H. Arshad
    David Perrett
    Claudio Tiberti
    Francesco Chiarelli
    Nicola Napoli
    Paolo Pozzilli
    Ahuva Nissim
    Diabetologia, 2015, 58 : 2851 - 2860
  • [35] Analysis of histones, histone variants, and their post-translationally modified forms
    Lindner, Herbert H.
    ELECTROPHORESIS, 2008, 29 (12) : 2516 - 2532
  • [36] MRP.py: A Parametrizer of Post-Translationally Modified Residues
    Sahrmann, Patrick G.
    Donnan, Patrick H.
    Merz, Kenneth M., Jr.
    Mansoorabadi, Steven O.
    Goodwin, Douglas C.
    JOURNAL OF CHEMICAL INFORMATION AND MODELING, 2020, 60 (10) : 4424 - 4428
  • [37] Post-translationally modified peptides - New targets in autoimmune disease?
    Purcell, A. W.
    Lau, K.
    Drummond, B.
    Williamson, N. A.
    Roberts, L. J.
    Mannering, S. I.
    Harrision, L. C.
    JOURNAL OF PEPTIDE SCIENCE, 2006, 12 : 95 - 95
  • [38] Targeted Proteomics Identification of Post-Translationally Modified KRAS Forms
    Chertov, Oleg
    Gillette, William
    Perkins, Shelley
    Esposito, Dominic
    Chertova, Elena
    Knotts, Joseph
    Colantonio, Simona
    Maciag, Anna
    Stephen, Andrew
    PROTEIN SCIENCE, 2017, 26 : 174 - +
  • [39] Localization of post-translationally modified α-tubulin and pseudocyst formation in tritrichomonads
    Andrea K. Boggild
    Christine A. Sundermann
    Barbara H. Estridge
    Parasitology Research, 2002, 88 : 468 - 474
  • [40] Low-molecular-weight post-translationally modified microcins
    Severinov, Konstantin
    Semenova, Ekaterina
    Kazakov, Alexey
    Kazakov, Teymur
    Gelfand, Mikhail S.
    MOLECULAR MICROBIOLOGY, 2007, 65 (06) : 1380 - 1394
12345