About: Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration

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About: Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration Goto Sponge NotDistinct Permalink

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scientific article published on 01 June 2002

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 2002 (uk) im Juni 2002 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunu de 2002 (ast) scientific article published on 01 June 2002 (en)
publication date	wds:Q74084385-97F865C6-7A3B-4924-95DE-E1435A6B7772
publication date	2002-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q74084385-8B67F71C-774F-4B8E-8E77-8237A1F1CF67
language of work or name	English
cites work	wds:Q74084385-069F0CFB-27E8-4031-B5BB-4595EEB19183 wds:Q74084385-298346F1-A393-4B80-919F-DD48F42014F5 wds:Q74084385-2F177107-BA4B-47BB-A529-FEFD99BBC4EF wds:Q74084385-3AFB1A0C-574A-4202-B94F-D1E3E545E629 wds:Q74084385-454AE825-8577-4734-A5BF-3DD6D930A4DE wds:Q74084385-4EA468E3-6DD6-4D38-9441-E4F8FF453526 wds:Q74084385-54B4EC59-419F-486A-918E-692F75A635F9 wds:Q74084385-608185F5-602D-4E73-89B7-AF10BAD53C0E wds:Q74084385-6E8BF7A3-5D73-4B0B-B45A-13F013084B11 wds:Q74084385-794B8616-A75A-4876-8F3D-350F3F6DF97F wds:Q74084385-83AB66F1-83AB-4FDF-B57C-4C54F2E925BA wds:Q74084385-852D94D9-7D75-48FA-801A-52BE69B779A6 wds:Q74084385-8E32061C-A385-4D90-93E2-021C7F7B9C00 wds:Q74084385-8F6C483C-092E-4DFB-8062-C3FD41C6DC80 wds:Q74084385-90732F9C-7672-4D1A-9D27-BD61FD088E36 wds:Q74084385-9571925B-C184-46E0-8324-7191C4A76687 wds:Q74084385-A4646F00-1411-47BC-8B56-3121FED4BDCC wds:Q74084385-B0630784-A8F0-46C7-9E35-65283A9050C5 wds:Q74084385-B57ABD8B-E8E0-4ED2-A4CF-935A05DBAA3B wds:Q74084385-BCC04CD2-FB6A-40FC-AE6B-A499C3538AFD wds:Q74084385-EDB60962-2D1F-4F75-8475-1FE4BBEBF260 wds:Q74084385-F0CBD153-391D-4B2E-9EF7-015CDB6DB619
cites work	Structure-activity relationship of truncated and substituted analogues of the intracellular delivery vector Penetratin Getting hydrophilic compounds into cells: lessons from homeopeptides Evidence for an amphipathicity independent cellular uptake of amphipathic cell-penetrating peptides Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. Antimicrobial peptides of multicellular organisms Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra The position of the cell penetrating peptide penetratin in SDS micelles determined by NMR. Membrane thinning caused by magainin 2. Translocation of the pAntp peptide and its amphipathic analogue AP-2AL. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation Physico-chemical requirements for cellular uptake of pAntp peptide. Role of lipid-binding affinity Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments Cell-penetrating peptides. The antennapedia peptide penetratin translocates across lipid bilayers - the first direct observation. Homeodomain-derived peptides. In and out of the cells Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles Induction of secondary structure in the peptide hormone motilin by interaction with phospholipid vesicles Effect of salts on conformational change of basic amphipathic peptides from beta-structure to alpha-helix in the presence of phospholipid liposomes and their channel-forming ability Interaction of the third helix of Antennapedia homeodomain and a phospholipid monolayer, studied by ellipsometry and PM-IRRAS at the air-water interface
author name string	wds:Q74084385-E5CEBEA3-CED7-4657-9B3E-BC46227349D3 wds:Q74084385-F8121EFC-7B46-43CD-9234-389E98D93A53
author name string	Mazin Magzoub L E Göran Eriksson
rdfs:label	Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (en) Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (nl)
skos:prefLabel	Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (en) Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (nl)
name	Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (en) Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (nl)
author	wds:Q74084385-64FBEB37-778A-4DCA-ABAC-A7363C38C6EA
author	Astrid Gräslund
title	wds:Q74084385-59656631-836F-4591-BA4E-35B40FDC17A6
title	Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration (en)
page(s)	wds:Q74084385-68529133-6D0A-469C-A7C1-F373DA37D602
page(s)	53-63
instance of	wds:Q74084385-759B6674-F7A1-4525-9F46-16A8A676262B
instance of	scholarly article
PubMed ID	wds:Q74084385-9B7A0151-01C0-4919-A580-E619F5EA5521
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12007625
PubMed ID	12007625
published in	wds:Q74084385-BD68655C-6371-49E7-B8D0-B76C8D80A2BE
published in	Biochimica et Biophysica Acta
issue	wds:Q74084385-75FBD7F6-872A-4B04-BC65-594E55913365
volume	wds:Q74084385-5F5F2D96-A13E-44F1-985F-D7DECDAB79F7
issue	1-2
volume	1563
DOI	wds:Q74084385-446BFF52-AB7D-44C2-9C04-A07CEB41EA76
DOI	http://dx.doi.org/10.1016/S0005-2736(02)00373-5
DOI	10.1016/S0005-2736(02)00373-5
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q74084385
is cites work of	Cell-penetrating peptides and antimicrobial peptides: how different are they? A critical reassessment of penetratin translocation across lipid membranes On the mechanisms of the internalization of S4(13)-PV cell-penetrating peptide Investigation of Homeodomain Membrane Translocation Properties: Insights from the Structure Determination of Engrailed-2 Homeodomain in Aqueous and Membrane-Mimetic Environments Determination of penetratin secondary structure in live cells with Raman microscopy Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Surfactant Assemblies and their Various Possible Roles for the Origin(S) of Life Design strategies to improve soluble macromolecular delivery constructs Cell membrane translocation of the N-terminal (1-28) part of the prion protein A common landscape for membrane-active peptides Molecular dynamics studies of transportan 10 (tp10) interacting with a POPC lipid bilayer Membrane-mediated peptide conformation change from alpha-monomers to beta-aggregates Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles Small-molecule mimics of an alpha-helix for efficient transport of proteins into cells

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