Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate Cathelicidins - Wikidata - wikimedia - TriplyDB

Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate Cathelicidins

Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate Cathelicidins

http://www.wikidata.org/entity/Q27676333

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Antiviral potential of cathelicidins High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments.The Role of Antimicrobial Peptides in Influenza Virus Infection and Their Potential as Antiviral and Immunomodulatory Therapy Antiviral Activity of the Human Cathelicidin, LL-37, and Derived Peptides on Seasonal and Pandemic Influenza A Viruses.PAGAL - Properties and corresponding graphics of alpha helical structures in proteins.Human antimicrobial peptides and proteins Identifying the Critical Domain of LL-37 Involved in Mediating Neutrophil Activation in the Presence of Influenza Virus: Functional and Structural Analysis Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300.Natural antimicrobial peptides as promising anti-HIV candidates.ATP synthase: a molecular therapeutic drug target for antimicrobial and antitumor peptides Database-Guided Discovery of Potent Peptides to Combat HIV-1 or Superbugs Membrane-Active Epithelial Keratin 6A Fragments (KAMPs) Are Unique Human Antimicrobial Peptides with a Non-αβ Structure Solution NMR studies of peptide-lipid interactions in model membranes.Human cathelicidin LL-37 prevents bacterial biofilm formation.Effects of arginine and leucine substitutions on anti-endotoxic activities and mechanisms of action of cationic and amphipathic antimicrobial octadecapeptide from rice α-amylase.The Naturally Occurring Host Defense Peptide, LL-37, and Its Truncated Mimetics KE-18 and KR-12 Have Selected Biocidal and Antibiofilm Activities Against Candida albicans, Staphylococcus aureus, and Escherichia coli In vitro.Design and surface immobilization of short anti-biofilm peptides.Structural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37.Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding.Transformation of human cathelicidin LL-37 into selective, stable, and potent antimicrobial compounds.Effect of substituting arginine and lysine with alanine on antimicrobial activity and the mechanism of action of a cationic dodecapeptide (CL(14-25)), a partial sequence of cyanate lyase from rice.Effect of alanine, leucine, and arginine substitution on antimicrobial activity against Candida albicans and action mechanism of a cationic octadecapeptide derived from α-amylase of rice.

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Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate Cathelicidins

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Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin

Solution structure of the N-terminal amphitropic domain ofEscherichia coliglucose-specific enzyme IIA in membrane-mimetic micelles

Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles

Decoding the Functional Roles of Cationic Side Chains of the Major Antimicrobial Region of Human Cathelicidin LL-37

Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions

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