Results 261 to 270 of about 188,935 (276)

Human antimicrobial peptide LL-37 induces glial-mediated neuroinflammation

Biochemical Pharmacology, 2015
LL-37 is the sole cathelicidin-derived antimicrobial peptide found in humans. It becomes active upon C-terminal cleavage of its inactive precursor hCAP18. In addition to antimicrobial action, it also functions as an innate immune system stimulant in many tissues of the body.
Moonhee, Lee, Xiaolei, Shi, Annelise E, Barron, Edith, McGeer, Patrick L, McGeer   +4 more
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2013
LL-37 .
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Antimicrobial peptide LL-37 on surfaces presenting carboxylate anions

Biomaterials Science, 2015
Non-covalently immobilized antimicrobial peptide LL-37 attracts and rapidly kills bacteria upon contact.
G T, Qin, A, Lopez, C, Santos, A M, McDermott, C Z, Cai   +4 more
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Low serum levels of cathelicidin LL-37 in leprosy

Acta Tropica, 2011
The antimicrobial peptide cathelicidin LL-37 possesses antituberculous activity, its association with other mycobacterial diseases, such as leprosy, is unknown. We studied serum cathelicidin and 25OH-vitamin D3 levels in 29 leprosy patients and 19 healthy individuals from Yemen.
Michael, Matzner, Abdul Rahim, Al Samie, Heide-Maria, Winkler, Johannes, Nemeth, Andreas, Grasnek, Alexander, Indra, Christian, Bieglmayer, Stefan, Winkler   +7 more
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LL-37: Cathelicidin-related antimicrobial peptide with pleiotropic activity

Pharmacological Reports, 2016
Antimicrobial peptides (AMPs) is a large family of compounds serving as natural antibiotics, widely distributed across the organism, mainly in mucus layers. They are designed to prevent pathogens from colonization. Among them, defensins and cathelicidins could be found.
Adam, Fabisiak, Natalia, Murawska, Jakub, Fichna   +2 more
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The Antimicrobial Peptide LL-37 Inhibits HIV-1 Replication

Current HIV Research, 2007
The antimicrobial peptide LL-37 is the only cathelicidin that has been described in humans. LL-37 exerts chemotactic, immunomodulatory and angiogenic effects; activities that are mediated through binding to the formyl peptide receptor like (FPRL)-1 receptor.
Peter, Bergman, Lilian, Walter-Jallow, Kristina, Broliden, Birgitta, Agerberth, Johan, Söderlund   +4 more
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Structure-function relationship of the human antimicrobial peptide LL-37 and LL-37 fragments in the modulation of TLR responses

bchm, 2009
Abstract Cathelicidins are effector molecules of the innate host defense system that establish an antimicrobial barrier at epithelial interfaces. The human cathelicidin LL-37, in addition to its antimicrobial activity, also exhibits immunomodulatory effects, such as inhibition of pro-inflammatory responses to bacterial LPS in human ...
Molhoek, E.M., den Hertog, A.L., de Vries, A.M.B.C., Nazmi, K., Veerman, E.C.I., Hartgers, F.C., Yazdanbakhsh, M., Bikker, F.J., van der Kleij, D.   +8 more
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Preparation of LL-37-Grafted Titanium Surfaces with Bactericidal Activity

Bioconjugate Chemistry, 2006
Modification of material surfaces aimed at bestowing them with antimicrobial properties is a promising approach in the development of new biomaterials. Antimicrobial peptides (AMPs) are an attractive alternative to conventional antibiotics because of lack of toxicity, inherently high selectivity, and absence of immune response.
Gabriel, M.O., Nazmi, K., Veerman, E.C.I., van Nieuw Amerongen, A., Zentner, A.   +4 more
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Human cathelicidin LL-37 rapidly disrupted colonic epithelial integrity

Biochimica et Biophysica Acta (BBA) - Biomembranes
The intestinal barrier, held together by epithelial cells and intercellular tight junction (TJ) proteins, prevents the penetration of microbial pathogens. Concurrently, intestinal epithelial cells secrete antimicrobial peptides, including cathelicidin. Cathelicidin has direct antibacterial and immunomodulatory functions, although its role in intestinal
Geeta, Kilari, Jacquelyn, Tran, Graham A D, Blyth, Eduardo R, Cobo   +3 more
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Cathelicidin LL-37

Der Hautarzt, 2007
J. Schauber, T. Ruzicka, R.A. Rupec
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