Results 41 to 50 of about 188,935 (276)

Characterizing the role of cell-wall β-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37. [PDF]

open access: yesPLoS ONE, 2011
Candida albicans is the major fungal pathogen of humans. Its adhesion to host-cell surfaces is the first critical step during mucosal infection. Antimicrobial peptides play important roles in the first line of mucosal immunity against C.
Pei-Wen Tsai   +3 more
doaj   +1 more source

Microenvironmental hCAP-18/LL-37 promotes pancreatic ductal adenocarcinoma by activating its cancer stem cell compartment [PDF]

open access: yes, 2015
This is the peer reviewed version of the following article: Microenvironmental hCAP-18/LL-37 promotes pancreatic ductal adenocarcinoma by activating its cancer stem cell compartment.
Alcala, Sonia   +16 more
core   +2 more sources

Role of antimicrobial peptides in tuberculosis and respiratory tract infections : clinical and mechanistic studies [PDF]

open access: yes, 2015
Antimicrobial peptides (AMPs) are effector molecules of the innate immune system in multicellular organisms. They are mainly expressed in epithelial cells and immune cells, providing the first line of defense against a wide range of pathogens.
Rekha, Rokeya Sultana
core   +1 more source

Cathelicidin hCAP18/LL-37 promotes cell proliferation and suppresses antitumor activity of 1,25(OH)2D3 in hepatocellular carcinoma

open access: yesCell Death Discovery, 2022
Cathelicidin hCAP18/LL-37 can resist infection from various pathogens and is an essential component of the human immune system. Accumulating evidence has indicated that hCAP18/LL-37 plays a tissue-specific role in human cancer.
Huidan Zhang   +7 more
doaj   +1 more source

Antimicrobial peptides, disease severity and exacerbations in bronchiectasis [PDF]

open access: yes, 2019
Rationale: Recently a frequent exacerbator phenotype has been described in bronchiectasis, but the underlying biological mechanisms are unknown. Antimicrobial peptides (AMPs) are important in host defence against microbes but can be proinflammatory in ...
Aliberti, Stefano   +14 more
core   +2 more sources

Cationic Peptides Facilitate Iron-induced Mutagenesis in Bacteria [PDF]

open access: yes, 2015
Pseudomonas aeruginosa is the causative agent of chronic respiratory infections and is an important pathogen of cystic fibrosis patients. Adaptive mutations play an essential role for antimicrobial resistance and persistence.
Makarova, Olga   +3 more
core   +3 more sources

Structural and functional analysis of the pro-domain of human cathelicidin, LL-37 [PDF]

open access: yes, 2013
Cathelicidins form a family of small host defense peptides distinct from another class of cationic antimicrobial peptides, the defensins. They are expressed as large precursor molecules with a highly conserved pro-domain known as the cathelin-like domain
Beckley, Amy J.   +12 more
core   +1 more source

Human host-defense peptide LL-37 targets stealth siderophores

open access: yesBiochemical and Biophysical Research Communications, 2020
A growing number of evidence shows that human-associated microbiota is an important contributor in health and disease. However, much of the complexity of host-microbiota interaction remains to be elucidated both at cellular and molecular levels. Siderophores are chemically diverse, ferric-specific chelators synthesized and secreted by microbes to ...
Ferenc Zsila, Tamás Beke-Somfai
openaire   +2 more sources

Efficacy of sodium butyrate adjunct therapy in shigellosis: a randomized, double-blind, placebo-controlled clinical trial [PDF]

open access: yes, 2012
BACKGROUND: Treatment of shigellosis in rabbits with butyrate reduces clinical severity and counteracts the downregulation of cathelicidin (CAP-18) in the large intestinal epithelia.
Abu Saleh Mohammed Arifuzzaman   +9 more
core   +1 more source

Transmembrane Pores Formed by Human Antimicrobial Peptide LL-37 [PDF]

open access: yesBiophysical Journal, 2011
Human LL-37 is a multifunctional cathelicidin peptide that has shown a wide spectrum of antimicrobial activity by permeabilizing microbial membranes similar to other antimicrobial peptides; however, its molecular mechanism has not been clarified. Two independent experiments revealed LL-37 bound to membranes in the α-helical form with the axis lying in ...
Lee, Chang-Chun   +3 more
openaire   +2 more sources

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