Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure. - Wikidata - wikimedia - TriplyDB

Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure.

Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure.

http://www.wikidata.org/entity/Q44394283

about

The Human Cathelicidin Antimicrobial Peptide LL-37 and Mimics are Potential Anticancer Drugs Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5 Putative bioactive motif of tritrpticin revealed by an antibody with biological receptor-like properties Antimicrobial activity of novel dendrimeric peptides obtained by phage display selection and rational modification.Cell selectivity and interaction with model membranes of Val/Arg-rich peptides.Guanidino groups greatly enhance the action of antimicrobial peptidomimetics against bacterial cytoplasmic membranes A small peptide with therapeutic potential for inflammatory acne vulgaris HemoPred: a web server for predicting the hemolytic activity of peptides.Effect of repetitive lysine-tryptophan motifs on the bactericidal activity of antimicrobial peptides The single transmembrane segment determines the modulatory function of the BK channel auxiliary γ subunit.From antimicrobial to anticancer peptides. A review.Road to clinical efficacy: challenges and novel strategies for antimicrobial peptide development.Antimicrobial peptides: modes of mechanism, modulation of defense responses.Probing the disparate effects of arginine and lysine residues on antimicrobial peptide/bilayer association.Archetypal tryptophan-rich antimicrobial peptides: properties and applications.Enhancement of the anti-inflammatory activity of temporin-1Tl-derived antimicrobial peptides by tryptophan, arginine and lysine substitutions.Linear bactenecin analogs with cell selectivity and anti-endotoxic activity.Synthesis of anticancer heptapeptides containing a unique lipophilic β(2,2) -amino acid building block.Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7.Cathelicidin-trypsin inhibitor loop conjugate represents a promising antibiotic candidate with protease stability Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures.Significance of the cyclic structure and of arginine residues for the antibacterial activity of arenicin-1 and its interaction with phospholipid and lipopolysaccharide model membranes.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.Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units.Ion channel-like activity of the antimicrobial peptide tritrpticin in planar lipid bilayers.Rational design of cationic antimicrobial peptides by the tandem of leucine-rich repeat.The C-terminal sequences of porcine thrombin are active as antimicrobial peptides.Characterization and production of multifunctional cationic peptides derived from rice proteins.Antimicrobial activity and mechanism of action of a novel cationic α-helical octadecapeptide derived from α-amylase of 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.Rationale for the design of shortened derivatives of the NK-lysin-derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens.Interaction mode of a symmetric Trp-rich undeca peptide PST11-RK with lipid bilayers.Antimicrobial peptide modification of biomaterials using supramolecular additives Wine Spoilage Yeasts: Control Strategy

P2860

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P2860

Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure.

http://www.wikidata.org/entity/Q44394283

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

@zh-hant

name

Selective cytotoxicity followi ...... ue amphipathic turn structure.

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Selective cytotoxicity followi ...... ue amphipathic turn structure.

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type

label

Selective cytotoxicity followi ...... ue amphipathic turn structure.

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Selective cytotoxicity followi ...... ue amphipathic turn structure.

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Selective cytotoxicity followi ...... ue amphipathic turn structure.

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Selective cytotoxicity followi ...... ue amphipathic turn structure.

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Selective cytotoxicity followi ...... ue amphipathic turn structure.

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Chul Won Lee

http://www.w3.org/2001/XMLSchema#string

Jae Il Kim

http://www.w3.org/2001/XMLSchema#string

Kyung-Soo Hahm

http://www.w3.org/2001/XMLSchema#string

Song Yub Shin

http://www.w3.org/2001/XMLSchema#string

Sung-Tae Yang

http://www.w3.org/2001/XMLSchema#string

Yong-Chul Kim

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold

Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures

Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles

Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin.

Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems.

Antibiotic peptides as mediators of innate immunity.

Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides.

Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides.

Peptide antibiotics and their role in innate immunity.

Structure-activity studies on magainins and other host defense peptides.

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