About: Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡

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About: Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	article (en) ലേഖനം (ml) wetenschappelijk artikel (nl) наукова стаття, опублікована в лютому 1997 (uk) article scientifique publié en 1997 (fr) im Februar 1997 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q56501840-A711CE87-A067-4C94-97D0-4BA0901A5377
publication date	1997-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56501840-CF508CA1-B5E5-40DE-860D-6F6D1A3688ED
language of work or name	English
author name string	wds:Q56501840-514B8973-B96F-411E-9DA8-9E25045FDF8D wds:Q56501840-A47C6B37-7013-454D-A739-3DBC94BB9C6A
author name string	Robert I. Lehrer Angelika Latal
rdfs:label	Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (en) Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (nl)
skos:prefLabel	Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (en) Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (nl)
name	Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (en) Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (nl)
author	wds:Q56501840-942F156A-00DE-45CA-8AA2-F9E5C9CB02B1 wds:Q56501840-B5D5DABC-1646-49A2-AF5C-603BB5D53BEB
author	Tomas Ganz Karl Lohner
title	wds:Q56501840-3BF634AA-9B07-4128-941F-A397B68DE704
title	Differential Scanning Microcalorimetry Indicates That Human Defensin, HNP-2, Interacts Specifically with Biomembrane Mimetic Systems†,‡ (en)
page(s)	wds:Q56501840-018197D8-971D-4BB7-926E-64DF5441EA13
page(s)	1525-1531
instance of	wds:Q56501840-E7B33BFB-E78F-4806-A8B2-00DCD795A503
instance of	scholarly article
PubMed ID	wds:Q56501840-8B48B16B-6835-4E0A-A9B5-883942650E59
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9063901
PubMed ID	9063901
published in	wds:Q56501840-D99729CB-7F8E-4566-87F7-AF8645E98032
published in	Biochemistry
issue	wds:Q56501840-4770A53F-C214-4B1E-8FC9-881E21E96794
volume	wds:Q56501840-CAAC8D2C-240B-4693-B87A-B31D8DF46F66
issue	6
volume	36
DOI	wds:Q56501840-291417A4-68DF-4265-886F-B2A8D36239B4
DOI	http://dx.doi.org/10.1021/BI961300P
DOI	10.1021/BI961300P
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56501840
is cites work of	Human defensins Mammalian defensins in the antimicrobial immune response Antibiotic peptides from higher eukaryotes: biology and applications Interaction of antimicrobial peptide protegrin with biomembranes Defensins: antimicrobial peptides of innate immunity Mechanism of the lamellar/inverse hexagonal phase transition examined by high resolution x-ray diffraction Membrane-active host defense peptides--challenges and perspectives for the development of novel anticancer drugs Salivary histatin 5 and human neutrophil defensin 1 kill Candida albicans via shared pathways. Resonance Assignment and Three-Dimensional Structure Determination of a Human α-Defensin, HNP-1, by Solid-State NMR A 3.1-kb genomic fragment of Bacillus subtilis encodes the protein inhibiting growth of Xanthomonas oryzae pv. oryzae Antimicrobial Peptides Targeting Gram-Positive Bacteria Antimicrobial peptides as mediators of epithelial host defense Antimicrobial peptides of vertebrates Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: determination and biological specificity Antimicrobial defensin peptides of the human ocular surface Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems Human beta-defensin 2 induces a vigorous cytokine response in peripheral blood mononuclear cells Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells Ideally amphipathic β-sheeted peptides at interfaces: structure, orientation, affinities for lipids and hemolytic activity of (KL)mK peptides Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids. In search of a novel target - phosphatidylserine exposed by non-apoptotic tumor cells and metastases of malignancies with poor treatment efficacy Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin Antimicrobial Activity of Novel Synthetic Peptides Derived from Indolicidin and Ranalexin against Streptococcus pneumoniae Mechanisms of renal damage owing to infection Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C. Differential scanning calorimetry: An invaluable tool for a detailed thermodynamic characterization of macromolecules and their interactions Diffusion as a probe of peptide-induced membrane domain formation Morphological changes induced by the action of antimicrobial peptides on supported lipid bilayers Packing characteristics of a model system mimicking cytoplasmic bacterial membranes Variations in the interaction of human defensins with Escherichia coli: Possible implications in bacterial killing Biomembrane model interaction and percutaneous absorption of papaverine through rat skin: effects of cyclodextrins as penetration enhancers Packing behaviour of two predominant anionic phospholipids of bacterial cytoplasmic membranes [Effector molecules of the innate immune system for treatment of wound infections] Studies on the Interaction of Alyteserin 1c Peptide and Its Cationic Analogue with Model Membranes Imitating Mammalian and Bacterial Membranes Biophysical approaches for exploring lipopeptide-lipid interactions Chapter Five Liposome-Based Biomembrane Mimetic Systems: Implications for Lipid–Peptide Interactions
is cites work of	wds:Q33666041-7AB5A66D-7BED-497A-A4F1-71E6E56C32F6 wds:Q27659134-2F9F21A5-06EC-45F4-A7BB-5DFF5C389C73 wds:Q33789711-C3A243FA-2ADD-4D59-A4F3-9F05C738DA48 wds:Q33789733-D0064446-D2C0-4BFA-8E4B-001C090BB44E wds:Q41729805-C739B61F-B669-44AB-9C2D-A68FEE5CEE0D wds:Q40232091-5CA37B79-D23F-433A-8604-B3DF1C250F70 wds:Q42702451-1B76D7A3-AF68-4267-AEFF-564B514007B7 wds:Q57362685-E15E2301-E721-4CD9-AFF9-EF4DD1FA15A9 wds:Q24669631-33FD505D-BC1C-4945-BECC-ADB8B8F1D3CD wds:Q28204453-2A1778E8-0DE0-40FB-B45B-BCB07EDF9B94 wds:Q30814666-7D1562CB-47AB-4B30-A7DC-C67B63338D63 wds:Q33579842-FB68E688-CAE5-424F-9B94-415F7DDE4B14 wds:Q38258695-0E3A1562-14E0-4A82-805E-AB7742F19881 wds:Q40235803-FA81D271-56B9-4091-B8F4-B135E0C2127C wds:Q43841721-8CFE2690-3945-4235-AF9D-990BF6E88DE6 wds:Q34510378-EED17E55-356D-4551-9509-42C6DB874891 wds:Q40293709-35967BB6-9BE1-43EC-9107-BA2E81FF513F wds:Q46972340-36CA2BCE-9F08-4EC9-B6AA-98C495745F7B wds:Q80009719-6B801B3D-A76D-444E-B505-36870DDCBC4A

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