Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides.

Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides.

Item
http://www.wikidata.org/entity/Q39301392
The Cyclic Cystine Ladder in  -Defensins Is Important for Structure and Stability, but Not Antibacterial ActivityCombined systems approaches reveal highly plastic responses to antimicrobial peptide challenge in Escherichia coli.Investigation of cationicity and structure of pseudin-2 analogues for enhanced bacterial selectivity and anti-inflammatory activity.Antibacterial and detoxifying activity of NZ17074 analogues with multi-layers of selective antimicrobial actions against Escherichia coli and Salmonella enteritidis.Activity determinants of helical antimicrobial peptides: a large-scale computational studyHuman β-defensin 4 with non-native disulfide bridges exhibit antimicrobial activity.Anti-proliferative effect on a colon adenocarcinoma cell line exerted by a membrane disrupting antimicrobial peptide KL15.Proline facilitates membrane insertion of the antimicrobial peptide maculatin 1.1 via surface indentation and subsequent lipid disorderingAntimicrobial Peptide Potency is Facilitated by Greater Conformational Flexibility when Binding to Gram-negative Bacterial Inner Membranes.Simultaneous Analysis of Secondary Structure and Light Scattering from Circular Dichroism Titrations: Application to Vectofusin-1.The importance of being kinked: role of Pro residues in the selectivity of the helical antimicrobial peptide P5.Host Antimicrobial Peptides: The Promise of New Treatment Strategies against Tuberculosis.Dissection of the antimicrobial and hemolytic activity of Cap18: Generation of Cap18 derivatives with enhanced specificity.Rifampin- or Capreomycin-Induced Remodeling of the Mycolic Acid Layer Is Mitigated in Synergistic Combinations with Cationic Antimicrobial Peptides
P2860

Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic α-helical peptides.

Item
http://www.wikidata.org/entity/Q39301392
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Conformational flexibility det ...... f cationic α-helical peptides.
@en
Conformational flexibility det ...... f cationic α-helical peptides.
@nl
type
label
Conformational flexibility det ...... f cationic α-helical peptides.
@en
Conformational flexibility det ...... f cationic α-helical peptides.
@nl
prefLabel
Conformational flexibility det ...... f cationic α-helical peptides.
@en
Conformational flexibility det ...... f cationic α-helical peptides.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932
P356
P1433
P1476
Conformational flexibility det ...... of cationic α-helical peptides
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932