Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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online resource.
- Erschienen in
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Modulating the poly-l-lysine structure through the control of the protonation–deprotonation state of l-lysine ; volume:12 ; number:1 ; day:16 ; month:11 ; year:2022 ; pages:1-13 ; date:12.2022
Scientific reports ; 12, Heft 1 (16.11.2022), 1-13, 12.2022
- Urheber
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Stagi, Luigi
Sini, Martina
Carboni, Davide
Anedda, Roberto
Siligardi, Giuliano
Gianga, Tiberiu-Marius
Hussain, Rohanah
Innocenzi, Plinio
- Beteiligte Personen und Organisationen
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SpringerLink (Online service)
- DOI
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10.1038/s41598-022-24109-5
- URN
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urn:nbn:de:101:1-2023012909050323218994
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:37 MESZ
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Beteiligte
- Stagi, Luigi
- Sini, Martina
- Carboni, Davide
- Anedda, Roberto
- Siligardi, Giuliano
- Gianga, Tiberiu-Marius
- Hussain, Rohanah
- Innocenzi, Plinio
- SpringerLink (Online service)
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Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases
The antimicrobial effects and mechanism of ε-poly-lysine against Staphylococcus aureus
The High Potential of ε‐Poly‐ l ‐Lysine for the Development of Antimicrobial Biomaterials
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The functional diversity of protein lysine methylation
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Solid state NMR investigations of 15N labeled poly L-lysine
Properties of Cross‐Linked Poly‐ l ‐lysine Hydrogels across the Random Coil–Helix Transition
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Direct addition of poly-lysine or poly-ethylenimine to the medium: A simple alternative to plate pre-coating
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Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases
The antimicrobial effects and mechanism of ε-poly-lysine against Staphylococcus aureus
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Properties of Cross‐Linked Poly‐ l ‐lysine Hydrogels across the Random Coil–Helix Transition
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