Consequences of alteration in leucine zipper sequence of melittin in its neutralization of lipopolysaccharide-induced proinflammatory response in macrophage cells and interaction with lipopolysaccharide.
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Identification of GXXXXG motif in Chrysophsin-1 and its implication in the design of analogs with cell-selective antimicrobial and anti-endotoxin activities.Melittin-glutathione S-transferase fusion protein exhibits anti-inflammatory properties and minimal toxicity.NMR structure of temporin-1 ta in lipopolysaccharide micelles: mechanistic insight into inactivation by outer membrane.Usefulness of ELISA Methods for Assessing LPS Interactions with Proteins and Peptides.Single Amino Acid Substitutions at Specific Positions of the Heptad Repeat Sequence of Piscidin-1 Yielded Novel Analogs That Show Low Cytotoxicity and In Vitro and In Vivo Antiendotoxin ActivityIntroduction of a lysine residue promotes aggregation of temporin L in lipopolysaccharides and augmentation of its antiendotoxin property.Piscidin-1-analogs with double L- and D-lysine residues exhibited different conformations in lipopolysaccharide but comparable anti-endotoxin activitiesMolecular Dynamics Simulations of the Host Defense Peptide Temporin L and Its Q3K Derivative: An Atomic Level View from Aggregation in Water to Bilayer Perturbation.Anti-inflammatory and anti-endotoxin properties of peptides derived from the carboxy-terminal region of a defensin from the tick Ornithodoros savignyi.Melittin suppresses tumor progression by regulating tumor-associated macrophages in a Lewis lung carcinoma mouse modelEffect of Bee Venom and Its Fractions on the Release of Pro-Inflammatory Cytokines in PMA-Differentiated U937 Cells Co-Stimulated with LPS.An MD2-derived peptide promotes LPS aggregation, facilitates its internalization in THP-1 cells, and inhibits LPS-induced pro-inflammatory responses.Membrane Active Peptides and Their Biophysical CharacterizationA Synthetic Peptide AWRK6 Alleviates Lipopolysaccharide-Induced Liver Injury
P2860
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P2860
Consequences of alteration in leucine zipper sequence of melittin in its neutralization of lipopolysaccharide-induced proinflammatory response in macrophage cells and interaction with lipopolysaccharide.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Consequences of alteration in ...... ction with lipopolysaccharide.
@ast
Consequences of alteration in ...... ction with lipopolysaccharide.
@en
type
label
Consequences of alteration in ...... ction with lipopolysaccharide.
@ast
Consequences of alteration in ...... ction with lipopolysaccharide.
@en
prefLabel
Consequences of alteration in ...... ction with lipopolysaccharide.
@ast
Consequences of alteration in ...... ction with lipopolysaccharide.
@en
P2093
P2860
P356
P1476
Consequences of alteration in ...... ction with lipopolysaccharide.
@en
P2093
Jimut Kanti Ghosh
Manish Singh
Raghvendra M Srivastava
Saurabh Srivastava
Virendra Kumar Bajpai
P2860
P304
P356
10.1074/JBC.M111.302893
P407
P577
2011-11-29T00:00:00Z