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English
Design and characterization of anchoring amphiphilic peptides and their interactions with lipid vesicles
scientific article published on 01 November 1999
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scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
title
Design and characterization of anchoring amphiphilic peptides and their interactions with lipid vesicles
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
author name string
Percot A
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
Zhu XX
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
Lafleur M
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
publication date
1 November 1999
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
published in
Biopolymers
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
volume
50
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
issue
6
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
page(s)
647-655
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
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Polymer networks with grafted cell adhesion peptides for highly biospecific cell adhesive substrates.
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Physical properties of single phospholipid bilayers adsorbed to micro glass beads. A new vesicular model system studied by 2H-nuclear magnetic resonance
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Steric immobilization of liposomes in chromatographic gel beads and incorporation of integral membrane proteins into their lipid bilayers
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Activity of amphipathic poly(ethylene glycol) 5000 to prolong the circulation time of liposomes depends on the liposome size and is unfavorable for immunoliposome binding to target
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Combined influence of cholesterol and synthetic amphiphillic peptides upon bilayer thickness in model membranes
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Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 1. Studies of the conformation, intrabilayer orientation, and amide hydrogen exchangeability of Ac-K2-(LA)12-K2-amide
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Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans
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Design of membrane-inserting peptides: spectroscopic characterization with and without lipid bilayers
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Design and synthesis of amphiphilic alpha-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes
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Relative helix-forming tendencies of nonpolar amino acids
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Melittin-phospholipid interaction studied by employing the single tryptophan residue as an intrinsic fluorescent probe.
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Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesicles
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Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design
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On the transfer of integral proteins into membranes
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21 January 2018
Identifiers
DOI
10.1002/(SICI)1097-0282(199911)50:6<647::AID-BIP9>3.0.CO;2-T
0 references
PubMed ID
10508967
1 reference
stated in
Europe PubMed Central
PubMed ID
10508967
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10508967%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 October 2019
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