Arginine‐Rich Cell‐Penetrating Peptides Induce Lipid Rearrangements for Their Active Translocation across Laterally Heterogeneous Membranes
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
-
Englisch
- Bibliographic citation
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Arginine‐Rich Cell‐Penetrating Peptides Induce Lipid Rearrangements for Their Active Translocation across Laterally Heterogeneous Membranes ; day:26 ; month:06 ; year:2024 ; extent:11
Advanced science ; (26.06.2024) (gesamt 11)
- Creator
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Park, Sujin
Kim, Jinmin
Oh, Seung Soo
Choi, Siyoung Q.
- DOI
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10.1002/advs.202404563
- URN
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urn:nbn:de:101:1-2406271422073.024461167022
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 11:00 AM CEST
Data provider
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Associated
- Park, Sujin
- Kim, Jinmin
- Oh, Seung Soo
- Choi, Siyoung Q.
Other Objects (12)
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Polyhistidine facilitates direct membrane translocation of cell-penetrating peptides into cells
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Translocation of the cell-penetrating bacterial effector protein YopM in vitro and in vivo
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
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Secondary structures and cell-penetrating abilities of arginine-rich peptide foldamers
Polyhistidine facilitates direct membrane translocation of cell-penetrating peptides into cells
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Translocation of the cell-penetrating bacterial effector protein YopM in vitro and in vivo
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Collembola laterally move biochar particles
Secondary structures and cell-penetrating abilities of arginine-rich peptide foldamers
Polyhistidine facilitates direct membrane translocation of cell-penetrating peptides into cells
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Translocation of the cell-penetrating bacterial effector protein YopM in vitro and in vivo
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2