Pages that link to "Q33723268"

The following pages link to The Membrane-Bound Structure and Topology of a Human α-Defensin Indicate a Dimer Pore Mechanism for Membrane Disruption (Q33723268):

Displaying 31 items.

• Sometimes it takes two to tango: contributions of dimerization to functions of human α-defensin HNP1 peptide (Q24613395) (← links)
• Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR (Q26830018) (← links)
• An intrinsically disordered region of the adenovirus capsid is implicated in neutralization by human alpha defensin 5 (Q27324472) (← links)
• NMR Solution Structure and Condition-Dependent Oligomerization of the Antimicrobial Peptide Human Defensin 5 (Q27675169) (← links)
• Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity (Q27678587) (← links)
• Antibacterial membrane attack by a pore-forming intestinal C-type lectin (Q27680655) (← links)
• Thermodynamic instability of viral proteins is a pathogen-associated molecular pattern targeted by human defensins (Q28828268) (← links)
• Human Defensin 5 Disulfide Array Mutants: Disulfide Bond Deletion Attenuates Antibacterial Activity against Staphylococcus aureus (Q30032656) (← links)
• Molecular evolution of the primate α-/θ-defensin multigene family (Q31161057) (← links)
• Variations in the interaction of human defensins with Escherichia coli: Possible implications in bacterial killing (Q33579842) (← links)
• Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR. (Q33827462) (← links)
• Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance. (Q34709011) (← links)
• Human defensins facilitate local unfolding of thermodynamically unstable regions of bacterial protein toxins (Q34727874) (← links)
• Human β-defensin 4 with non-native disulfide bridges exhibit antimicrobial activity (Q35580348) (← links)
• High Fidelity Processing and Activation of the Human α-Defensin HNP1 Precursor by Neutrophil Elastase and Proteinase 3 (Q35842408) (← links)
• Molecular basis for membrane pore formation by Bax protein carboxyl terminus (Q35955513) (← links)
• Structural perspectives on antimicrobial chemokines (Q36492362) (← links)
• Cellular response to Trypanosoma cruzi infection induces secretion of defensin α-1, which damages the flagellum, neutralizes trypanosome motility, and inhibits infection. (Q37264811) (← links)
• A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes (Q37337990) (← links)
• The Interplay between Defensins and Microbiota in Crohn's Disease (Q37633135) (← links)
• ProHNPs are specific markers of normal myelopoiesis. (Q37679269) (← links)
• α-Defensins in human innate immunity (Q37968296) (← links)
• Defensins: antifungal lessons from eukaryotes (Q38201011) (← links)
• Guardians of the Gut: Enteric Defensins (Q39281980) (← links)
• Probing Oligomerized Conformations of Defensin in the Membrane. (Q46643064) (← links)
• In situ production of human β defensin-3 in lager yeasts provides bactericidal activity against beer-spoiling bacteria under fermentation conditions. (Q46976807) (← links)
• Oral Administration of Probiotics Increases Paneth Cells and Intestinal Antimicrobial Activity. (Q55038841) (← links)
• Analysis of the antimicrobial mechanism of porcine beta defensin 2 against E. coli by electron microscopy and differentially expressed genes (Q57050221) (← links)
• Application of Antimicrobial Peptides of the Innate Immune System in Combination With Conventional Antibiotics-A Novel Way to Combat Antibiotic Resistance? (Q64078565) (← links)
• Human neutrophil alpha‐defensins induce formation of fibrinogen and thrombospondin‐1 amyloid‐like structures and activate platelets via glycoprotein IIb/IIIa (Q83304826) (← links)
• Integrated solid-state NMR and molecular dynamics modeling determines membrane insertion of human β-defensin analog (Q91178592) (← links)