- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Context‐Dependence of the Reactivity of Cysteine and Lysine Residues ; day:01 ; month:06 ; year:2022 ; extent:1
ChemBioChem ; (01.06.2022) (gesamt 1)
- Creator
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Boll, Linus B.
Raines, Ronald T.
- DOI
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10.1002/cbic.202200258
- URN
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urn:nbn:de:101:1-2022060215132004812888
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:20 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Boll, Linus B.
- Raines, Ronald T.
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Reactivity‐Tunable Fluorescent Platform for Selective and Biocompatible Modification of Cysteine or Lysine
LSD1: more than demethylation of histone lysine residues
Sequence‐Dependent Acylation of Peptide Lysine Residues by DNAzymes
Metal Binding Ability of Small Peptides Containing Cysteine Residues
Traceless cysteine-linchpin enables precision engineering of lysine in native proteins
Nε-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms
Arsenic 3 methyltransferase (AS3MT) automethylates on cysteine residues in vitro
Lysine residues control the conformational dynamics of beta 2-glycoprotein I
Redox modifications of cysteine residues regulate the cytokine activity of HMGB1
Nucleotide-binding sites can enhance N-acylation of nearby protein lysine residues
The role of histone H3.3 lysine 4 and lysine 36 residues in mouse embryonic stem cells and neuronal development
Substrate dependence of graphene reactivity towards hydrogenation
Reactivity‐Tunable Fluorescent Platform for Selective and Biocompatible Modification of Cysteine or Lysine
LSD1: more than demethylation of histone lysine residues
Sequence‐Dependent Acylation of Peptide Lysine Residues by DNAzymes
Metal Binding Ability of Small Peptides Containing Cysteine Residues
Traceless cysteine-linchpin enables precision engineering of lysine in native proteins
Nε-Carboxymethyl Modification of Lysine Residues in Pathogenic Prion Isoforms
Arsenic 3 methyltransferase (AS3MT) automethylates on cysteine residues in vitro
Lysine residues control the conformational dynamics of beta 2-glycoprotein I
Redox modifications of cysteine residues regulate the cytokine activity of HMGB1
Nucleotide-binding sites can enhance N-acylation of nearby protein lysine residues
The role of histone H3.3 lysine 4 and lysine 36 residues in mouse embryonic stem cells and neuronal development