Corrigendum to: Bio-orthogonal Fluorescent Labelling of Biopolymers through Inverse-Electron-Demand Diels–Alder Reactions (ChemBioChem, (2017), 18, (486-501), 10.1002/cbic.201600607)

Eszter Kozma, Orsolya Demeter, P. Kele

Research output: Contribution to journalComment/debate

Abstract

In Section 5, in the discussion of the work of Doll et al. (ref. [73]) we mistakenly used Ac4ManCCyc rather than Ac4GlcCCyc twice. The paragraph should read: “Recently, Doll et al. used Ac4GlcCCyc to study the glycosylation states of specific intracellular proteins [O-GlcNAc transferase (OGT), transcription factor Foxo1, tumor suppressor p53, serine/threonine kinas Akt1, actin-binding protein vinculin and calcium/calmodulin-dependent protein kinase CAMK4] in live cells. The target proteins were tagged with GFP and overexpressed in HEK293T cells incubated in Ac4GlcCCyc containing medium. FRET between GFP and TAMRA-3 tagged glycan was detected by fluorescence lifetime imaging microscopy (FLIM). This approach revealed nuclear localization and regulation of Akt1 by O-GlcNAcylation. This was the first demonstration of studying protein glycosylation states within living cells, stressing the power of bio-orthogonal chemistry.” The authors apologise for this error.

Original languageEnglish
Pages (from-to)570
Number of pages1
JournalChemBioChem
Volume18
Issue number6
DOIs
Publication statusPublished - Mar 16 2017

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Biopolymers
Labeling
Glycosylation
Electrons
Vinculin
Microfilament Proteins
Calcium-Calmodulin-Dependent Protein Kinases
Proteins
Optical Imaging
Threonine
Serine
Polysaccharides
Tumors
Microscopy
Microscopic examination
Transcription Factors
Demonstrations
Fluorescence
Cells
Imaging techniques

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Cite this

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title = "Corrigendum to: Bio-orthogonal Fluorescent Labelling of Biopolymers through Inverse-Electron-Demand Diels–Alder Reactions (ChemBioChem, (2017), 18, (486-501), 10.1002/cbic.201600607)",
abstract = "In Section 5, in the discussion of the work of Doll et al. (ref. [73]) we mistakenly used Ac4ManCCyc rather than Ac4GlcCCyc twice. The paragraph should read: “Recently, Doll et al. used Ac4GlcCCyc to study the glycosylation states of specific intracellular proteins [O-GlcNAc transferase (OGT), transcription factor Foxo1, tumor suppressor p53, serine/threonine kinas Akt1, actin-binding protein vinculin and calcium/calmodulin-dependent protein kinase CAMK4] in live cells. The target proteins were tagged with GFP and overexpressed in HEK293T cells incubated in Ac4GlcCCyc containing medium. FRET between GFP and TAMRA-3 tagged glycan was detected by fluorescence lifetime imaging microscopy (FLIM). This approach revealed nuclear localization and regulation of Akt1 by O-GlcNAcylation. This was the first demonstration of studying protein glycosylation states within living cells, stressing the power of bio-orthogonal chemistry.” The authors apologise for this error.",
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AU - Kozma, Eszter

AU - Demeter, Orsolya

AU - Kele, P.

PY - 2017/3/16

Y1 - 2017/3/16

N2 - In Section 5, in the discussion of the work of Doll et al. (ref. [73]) we mistakenly used Ac4ManCCyc rather than Ac4GlcCCyc twice. The paragraph should read: “Recently, Doll et al. used Ac4GlcCCyc to study the glycosylation states of specific intracellular proteins [O-GlcNAc transferase (OGT), transcription factor Foxo1, tumor suppressor p53, serine/threonine kinas Akt1, actin-binding protein vinculin and calcium/calmodulin-dependent protein kinase CAMK4] in live cells. The target proteins were tagged with GFP and overexpressed in HEK293T cells incubated in Ac4GlcCCyc containing medium. FRET between GFP and TAMRA-3 tagged glycan was detected by fluorescence lifetime imaging microscopy (FLIM). This approach revealed nuclear localization and regulation of Akt1 by O-GlcNAcylation. This was the first demonstration of studying protein glycosylation states within living cells, stressing the power of bio-orthogonal chemistry.” The authors apologise for this error.

AB - In Section 5, in the discussion of the work of Doll et al. (ref. [73]) we mistakenly used Ac4ManCCyc rather than Ac4GlcCCyc twice. The paragraph should read: “Recently, Doll et al. used Ac4GlcCCyc to study the glycosylation states of specific intracellular proteins [O-GlcNAc transferase (OGT), transcription factor Foxo1, tumor suppressor p53, serine/threonine kinas Akt1, actin-binding protein vinculin and calcium/calmodulin-dependent protein kinase CAMK4] in live cells. The target proteins were tagged with GFP and overexpressed in HEK293T cells incubated in Ac4GlcCCyc containing medium. FRET between GFP and TAMRA-3 tagged glycan was detected by fluorescence lifetime imaging microscopy (FLIM). This approach revealed nuclear localization and regulation of Akt1 by O-GlcNAcylation. This was the first demonstration of studying protein glycosylation states within living cells, stressing the power of bio-orthogonal chemistry.” The authors apologise for this error.

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