Littérature scientifique sur le sujet « Peptide LL-37 »
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Articles de revues sur le sujet "Peptide LL-37":
Nagant, C., B. Pitts, K. Nazmi, M. Vandenbranden, J. G. Bolscher, P. S. Stewart et J. P. Dehaye. « Identification of Peptides Derived from the Human Antimicrobial Peptide LL-37 Active against Biofilms Formed by Pseudomonas aeruginosa Using a Library of Truncated Fragments ». Antimicrobial Agents and Chemotherapy 56, no 11 (20 août 2012) : 5698–708. http://dx.doi.org/10.1128/aac.00918-12.
Sieprawska-Lupa, Magdalena, Piotr Mydel, Katarzyna Krawczyk, Kinga Wójcik, Magdalena Puklo, Boguslaw Lupa, Piotr Suder et al. « Degradation of Human Antimicrobial Peptide LL-37 by Staphylococcus aureus-Derived Proteinases ». Antimicrobial Agents and Chemotherapy 48, no 12 (décembre 2004) : 4673–79. http://dx.doi.org/10.1128/aac.48.12.4673-4679.2004.
Perez-Perez, David A., Teresa de J. Villanueva-Ramirez, Adriana E. Hernandez-Pedraza, Nestor G. Casillas-Vega, Patricia Gonzalez-Barranco et Xristo Zarate. « The Small Metal-Binding Protein SmbP Simplifies the Recombinant Expression and Purification of the Antimicrobial Peptide LL-37 ». Antibiotics 10, no 10 (19 octobre 2021) : 1271. http://dx.doi.org/10.3390/antibiotics10101271.
Sigurdardottir, Thorgerdur, Pia Andersson, Mina Davoudi, Martin Malmsten, Artur Schmidtchen et Mikael Bodelsson. « In Silico Identification and Biological Evaluation of Antimicrobial Peptides Based on Human Cathelicidin LL-37 ». Antimicrobial Agents and Chemotherapy 50, no 9 (septembre 2006) : 2983–89. http://dx.doi.org/10.1128/aac.01583-05.
Yang, De, Qian Chen, Albert P. Schmidt, G. Mark Anderson, Ji Ming Wang, Joseph Wooters, Joost J. Oppenheim et Oleg Chertov. « Ll-37, the Neutrophil Granule–And Epithelial Cell–Derived Cathelicidin, Utilizes Formyl Peptide Receptor–Like 1 (Fprl1) as a Receptor to Chemoattract Human Peripheral Blood Neutrophils, Monocytes, and T Cells ». Journal of Experimental Medicine 192, no 7 (2 octobre 2000) : 1069–74. http://dx.doi.org/10.1084/jem.192.7.1069.
Rinker, Sherri D., Michael P. Trombley, Xiaoping Gu, Kate R. Fortney et Margaret E. Bauer. « Deletion ofmtrCin Haemophilus ducreyi Increases Sensitivity to Human Antimicrobial Peptides and Activates the CpxRA Regulon ». Infection and Immunity 79, no 6 (28 mars 2011) : 2324–34. http://dx.doi.org/10.1128/iai.01316-10.
Zhang, Yingxia, Jayaram Lakshmaiah Narayana, Qianhui Wu, Xiangli Dang et Guangshun Wang. « Structure and Activity of a Selective Antibiofilm Peptide SK-24 Derived from the NMR Structure of Human Cathelicidin LL-37 ». Pharmaceuticals 14, no 12 (30 novembre 2021) : 1245. http://dx.doi.org/10.3390/ph14121245.
Yason, John Anthony, Sitara Swarna Rao Ajjampur et Kevin Shyong Wei Tan. « Blastocystis Isolate B Exhibits Multiple Modes of Resistance against Antimicrobial Peptide LL-37 ». Infection and Immunity 84, no 8 (23 mai 2016) : 2220–32. http://dx.doi.org/10.1128/iai.00339-16.
Amagai, Ryo, Toshiya Takahashi, Hitoshi Terui, Taku Fujimura, Kenshi Yamasaki, Setsuya Aiba et Yoshihide Asano. « The Antimicrobial Peptide Cathelicidin Exerts Immunomodulatory Effects via Scavenger Receptors ». International Journal of Molecular Sciences 24, no 1 (3 janvier 2023) : 875. http://dx.doi.org/10.3390/ijms24010875.
Mirzaee, Malihe, Edita Holásková, Alžbeta Mičúchová, David J. Kopečný, Zhila Osmani et Ivo Frébort. « Long-Lasting Stable Expression of Human LL-37 Antimicrobial Peptide in Transgenic Barley Plants ». Antibiotics 10, no 8 (23 juillet 2021) : 898. http://dx.doi.org/10.3390/antibiotics10080898.
Thèses sur le sujet "Peptide LL-37":
El, Abbouni Sarah. « Microencapsulation of LL-37 Antimicrobial Peptide in PLGA ». Digital WPI, 2016. https://digitalcommons.wpi.edu/etd-theses/235.
Dannehl, Claudia. « Fragments of the human antimicrobial LL-37 and their interaction with model membranes ». Phd thesis, Universität Potsdam, 2013. http://opus.kobv.de/ubp/volltexte/2013/6814/.
Aufgrund der steigenden Resistenzen von Zellstämmen gegen traditionelle Therapeutika sind alternative medizinische Behandlungsmöglichkeiten für bakterielle Infektionen und Krebs stark gefragt. Antimikrobielle Peptide (AMPs) sind Bestandteil der unspezifischen Immunabwehr und kommen in jedem Organismus vor. AMPs lagern sich von außen an die Zellmembran an und zerstören ihre Integrität. Das macht sie effizient und vor allem schnell in der Wirkung gegen Bakterien, Viren, Pilzen und sogar Krebszellen. Das Ziel dieser Arbeit lag in der physikalisch-chemischen Charakterisierung zweier Peptidfragmente die unterschiedliche biologische Aktivität aufweisen. Die Peptide LL-32 und LL-20 waren Teile des humanen LL-37 aus der Kathelizidin-Familie. LL-32 wies eine stärke Aktivität als das Mutterpeptid auf, während LL-20 kaum aktiv gegen die verschiedenen Zelltypen war. In dieser Arbeit wurde die Wechselwirkung der Peptide mit Zellmembranen systematisch anhand von zweidimensionalen Modellmembranen in dieser Arbeit untersucht. Dafür wurden Filmwaagenmessungen mit IR-spektroskopischen und Röntgenstreumethoden gekoppelt. Circulardichroismus-Spektroskopie im Volumen komplementierte die Ergebnisse. In der ersten Näherung wurde die Struktur der Peptide in Lösung mit der Struktur an der Wasser/Luft-Grenzfläche verglichen. In wässriger Lösung sind beide Peptidfragmente unstrukturiert, nehmen jedoch eine α-helikale Sekundärstruktur an, wenn sie an die Wasser/Luft-Grenzfläche adsorbiert sind. Das biologisch unwirksamere LL-20 bleibt dabei teilweise ungeordnet. Das steht im Zusammenhang mit einer geringeren Grenzflächenaktivität des Peptids. In der Zweiten Näherung wurden Versuche mit Lipidmonoschichten als biomimetisches Modell für die Wechselwirkung mit der Zellmembran durchgeführt. Es konnte gezeigt werden, dass sich die Peptide fluidisierend auf negativ geladene Dipalmitylphosphatidylglycerol (DPPG) Monoschichten auswirken, was einer Membranverdünnung an Bakterienzellen entspricht. Eine Interaktion der Peptide mit zwitterionischem Phosphatidylcholin (PC), das als Modell für Säugetierzellen verwendet wurde, konnte nicht klar beobachtet werden, obwohl biologische Experimente das hämolytische Verhalten zumindest von LL-32 zeigten. In der dritten Näherung wurde das Membranmodell näher an die Membran von humanen Erythrozyten angepasst, indem gemischte Monoschichten aus Sphingomyelin (SM) und PC hergestellt wurden. Die physikalisch-chemischen Eigenschaften der Lipidfilme wurden zunächst ausgearbeitet und anschließend der Einfluss der Peptide untersucht. Es konnte anhand verschiedener Versuche gezeigt werden, dass die Wechselwirkung von LL-32 mit der Modellmembran verstärkt ist, wenn eine Koexistenz von fluiden und Gelphasen auftritt. Zusätzlich wurde die Wechselwirkung der Peptide mit der Membran von Krebszellen imitiert, indem ein geringer Anteil negativ geladener Lipide in die Monoschicht eingebaut wurde. Das hatte allerdings keinen nachweislichen Effekt, so dass geschlussfolgert werden konnte, dass die hohe Aktivität von LL-32 gegen Krebszellen ihren Grund in der veränderten Fluidität der Membran hat und nicht in der veränderten Oberflächenladung. Darüber hinaus wurden Ähnlichkeiten zu Melittin, einem AMP aus dem Bienengift, dargelegt. Die Ergebnisse dieser Arbeit sprechen für einen Detergenzien-artigen Wirkmechanismus des Peptids LL-32 an der Zellmembran.
Filewod, Niall Christopher Jack. « Immunomodulatory effects of LL-37 in the epithelia ». Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/927.
Li, Yue Xin. « The human cationic host defense peptide LL-37 modulates neutrophil apoptosis and chemokine responses ». Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31726.
Science, Faculty of
Microbiology and Immunology, Department of
Graduate
Zhang, P. « Identification of staphylococcal genes involved in resistance to the human antimicrobial peptide LL-37 ». Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1380282/.
Milhan, Noala Vicensoto Moreira [UNESP]. « Avaliação do peptídeo LL-37 em contato com células-tronco da polpa dentária ». Universidade Estadual Paulista (UNESP), 2017. http://hdl.handle.net/11449/149791.
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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
O peptídeo LL-37 (catelicidina derivada de humano), é liberado por algumas células humanas e capaz de neutralizar os tecidos com lipopolissacarídeo (LPS), além de atrair células da polpa, e induzir a angiogênese, características que o tornam um possível adjunto para a regeneração do complexo dentino-pulpar. O objetivo desse trabalho foi avaliar in vitro a biocompatibilidade do peptídeo LL-37 nas concentrações de 5 e 10 μg/mL, e sua possível atuação na diferenciação de células-tronco da polpa dentária (DPSC) para odontoblastos- like. Com esse propósito, foram avaliados: (a) a citotoxicidade, pelo teste MTT; (b) a genotoxicidade, através do ensaio do micronúcleo; (c) a produção e quantificação de óxido nítrico; (d) as fases do ciclo celular, por citometria; (e) a expressão de alguns genes associados à formação de tecido mineralizado, através do teste qRT-PCR; (f) o conteúdo de proteína total; (g) a atividade de fosfatase alcalina (ALP); e (h) a produção de sialofosfoproteína dentinária (DSPP), pelo ensaio imunoenzimático ELISA. Foi observado que as concentrações de 5 e 10 μg/mL de LL-37 não foram citotóxicas e ainda aumentaram, em geral, a viabilidade celular (p<0,05), sendo que os maiores valores de absorbância foram observados no 3° dia de contato. As concentrações testadas também não induziram genotoxicidade, após 7 dias de contato, tendo sido genotóxico apenas o grupo controle positivo (EMS) (p<0,05). Ainda, não foi observado diferença estatisticamente significativa na produção de nitrito, pelas células expostas ao LL-37 após 7 dias, em ambas as concentrações. A análise do ciclo celular, evidenciou maior porcentual de células na fase G0/G1, em todos os grupos (p<0,05). Quando estes foram comparados, foi observado maior quantidade de células na fase G0/G1 na concentração de 10 μg/mL de LL- 37 comparada ao grupo controle (p<0,05). Por outro lado, o grupo controle exibiu mais células na fase G2 e em mitose (M) que os grupos tratados com 5 e 10 μg/mL de LL-37 (p<0,05), e mais células na interfase (S) que o grupo tratado com 10 μg/mL de LL-37 (p<0,05). A análise da expressão gênica demonstrou que não houve aumento de expressão dos genes fosfatase alcalina, osteocalcina, osteopontina e Runx2 após tratamento com ambas as concentrações do peptídeo, no 3° dia. Além disso, não foi observado diferença estatisticamente significativa na ALP nos grupos tratados e controle, após 3 e 14 dias, enquanto o conteúdo de proteína total foi maior aos 14 dias nos grupos tratados com LL-37 (p<0,05). Ainda, aos 3 dias, a produção da proteína DSPP foi maior no grupo tratado com 10 μg/mL de LL-37 (p<0,05). Com base nesses resultados, pode-se concluir que o LL-37 é biocompatível nas concentrações testadas nesse trabalho, e ainda aumenta o número de células viáveis, principalmente em período inicial. Além disso, aos 3 dias, na concentração de 10 μg/mL, ele retarda o ciclo celular e aumenta a expressão da proteína DSPP, além de aumentar a síntese proteica aos 14 dias, o que indica que esse peptídeo pode desempenhar algum tipo de função na diferenciação odontoblástica.
The LL-37 peptide (human derived cathelicidin) is released by some human cells and able of neutralizing the tissues that present lipopolysaccharide (LPS), as well as, attracts pulp cells and induces angiogenesis; characteristics that makes it a possible adjunct for regeneration of the dentin-pulp complex. The aim of this study was evaluate in vitro the biocompatibility of LL-37 in the concentrations of 5 and 10 μg/mL, and its possible performance in the differentiation of dental pulp stem cells (DPSC) into odontoblasts-like cells. For this purpose, it was evaluated: (a) the cytotoxicity by MTT assay; (b) the genotoxicity by the micronucleus test; (c) the production and quantification of nitric oxide; (d) the cell cycle, by flow cytometry; (e) the expression of genes associated with the mineralization by qRT-PCR; (f) the total protein content; (g) the alkaline phosphatase activity (ALP); and (h) the production of dentine sialofosfoprotein (DSPP) by indirect enzyme-linked immunosorbent assay (ELISA). It was observed that the concentrations of 5 and 10 μg/ml of LL-37 were not cytotoxic, in addition to they increased, in general, the cell viability (p<0,05). Moreover, higher absorbance values were observed on 3rd day of contact. After 7 days, the tested concentrations also did not induce genotoxicity, (p<0,05); only the positive control group (EMS) was genotoxic (p<0.05). Furthermore, there was not statistical significance in the nitrite production by the cells exposed to LL-37 for 7 days, in both concentrations. The cell cycle test showed higher percentage of cells in the phase G0/G1 in all groups (p<0.05). When they were compared, it was noticied that concentration of 10 ug/ml of LL-37 arrested the cells in G0/G1 compared to the control group (p<0.05). On the other hand, the control group, exhibited higher amount of cells in G2 and mitosis (M) than the others (p<0.05) and also higher number of cells in interfase (S) than the group treated with 10 μg/mL of LL-37 (p<0.05). On the 3rd day, the analysis of gene expression demonstrated no increase in the expression of the genes alkaline phosphatase, osteocalcin, osteopontin and Runx2, after treatment with both peptide concentrations. Furthermore, it was not observed statistical significance in the ALP in the treated and control groups after 3 and 14 days, while total protein content was higher in the groups treated with LL-37, at 14 days (p<0.05). On the 3rd day, the production of DSPP protein was higher in the group treated with 10 μg/mL of LL-37 (p<0.05). Based on these results, it can be concluded that LL-37 is biocompatible at these concentrations and increases the number of viable cells, especially in the initial period. Moreover, on the 3rd day, the concentration of 10 μg/mL arrests the cell cycle, and increases the expression of DSPP protein, in addition to raising the protein content at 14 days, which indicates that this peptide may present some kind of function in the odontoblastic differentiation.
Ghannad, Mona. « Design and Synthesis of Collagen-binding Anti-microbial Proteins ». Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/19981.
Li, Hsin-Ni. « Impact of cationic host defence peptide LL-37 on human neutrophil death and inflammatory responses ». Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/5597.
Milhan, Noala Vicensoto Moreira. « Avaliação do peptideo LL-37 em contato com células-tronco da polpa dentária / ». São José dos Campos, 2017. http://hdl.handle.net/11449/149791.
Banca: Luana Marotta Reis de Vasconcellos
Banca: Mônica Ghislaine Oliveira Alves
Banca: Cristina Pacheco Soares
Banca: Cacio de Moura Netto
Resumo: O peptídeoLL-37 (catelicidina derivada de humano), é liberado por algumas células humanas e capaz de neutralizar os tecidos com lipopolissacarídeo (LPS), além de atrair células da polpa, e induzir a angiogênese, características que o tornam um possível adjunto para a regeneração do complexo dentino-pulpar. O objetivo desse trabalho foi avaliar in vitro a biocompatibilidade do peptídeo LL-37 nas concentrações de 5 e 10 µg/mL, e sua possível atuação na diferenciação de células-tronco da polpa dentária (DPSC) para odontoblastoslike. Com esse propósito, foram avaliados: (a) a citotoxicidade, pelo teste MTT; (b) a genotoxicidade, através do ensaio do micronúcleo; (c) a produção e quantificação de óxido nítrico; (d) as fases do ciclo celular, por citometria; (e) a expressão de alguns genes associados à formação de tecido mineralizado, através do teste qRT-PCR; (f) o conteúdo de proteína total; (g) a atividade de fosfatase alcalina (ALP); e (h) a produção de sialofosfoproteína dentinária (DSPP), pelo ensaio imunoenzimático ELISA. Foi observado que as concentrações de 5 e 10 µg/mL de LL-37 não foram citotóxicas e ainda aumentaram, em geral, a viabilidade celular (p<0,05), sendo que os maiores valores de absorbância foram observados no 3° dia de contato. As concentrações testadas também não induziram genotoxicidade, após 7 dias de contato, tendo sido genotóxico apenas o grupo controle positivo (EMS) (p<0,05). Ainda, não foi observado diferença estatisticamente significativa na produção de nitrito, pelas células expostas ao LL-37 após 7 dias, em ambas as concentrações. A análise do ciclo celular, evidenciou maior porcentual de células na fase G0/G1, em todos os grupos (p<0,05). Quando estes foram comparados, foi observado maior quantidade de células na fase G0/G1 na concentração de... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract : The LL 37 peptide (human derived cathelicidin) is released by some human cells and able of neutralizing the tissues that present lipopolysaccharide (LPS), as well as, attracts pulp cells and induces angiogenesis; characteristics that makes it a possible adjunct for regeneration of the dentin-pulp complex. The aim of this study was evaluate in vitro the biocompatibility of LL-37 in the concentrations of 5 and 10 µg/mL, and its possible performance in the differentiation of dental pulp stem cells (DPSC) into odontoblasts-like cells. For this purpose, it was evaluated: (a) the cytotoxicity by MTT assay; (b) the genotoxicity by the micronucleus test; (c) the production and quantification of nitric oxide; (d) the cell cycle, by flow cytometry; (e) the expression of genes associated with the mineralization by qRT-PCR; (f) the total protein content; (g) the alkaline phosphatase activity (ALP); and (h) the production of dentine sialofosfoprotein (DSPP) by indirect enzyme-linked immunosorbent assay (ELISA). It was observed that the concentrations of 5 and 10 µg/ml of LL-37 were not cytotoxic, in addition to they increased, in general, the cell viability (p<0,05). Moreover, higher absorbance values were observed on 3rd day of contact. After 7 days, the tested concentrations also did not induce genotoxicity, (p<0,05); only the positive control group (EMS) was genotoxic (p<0.05). Furthermore, there was not statistical significance in the nitrite production by the cells exposed to LL-37 for 7 days, in both concentrations. The cell cycle test showed higher percentage of cells in the phase G0/G1 in all groups (p<0.05). When they were compared, it was noticied that concentration of 10 ug/ml of LL-37 arrested the cells in G0/G1 compared to the control group (p<0.05). On the other hand, the control group, exhibited higher amount of cells in G2 and mitosis...(Resumo completo, clicar acesso eletrônico abaixo)
Doutor
Zreika, Sami. « Etude de l'impact de la protéine antimicrobienne humaine hCAP18/LL-37 sur le cancer du sein ». Thesis, Tours, 2011. http://www.theses.fr/2011TOUR4052.
The peptide hCAP18/LL-37, part of the innate immune defense, has now been recognized as multifunctional for eukaryotic cells. Our studies demonstrate its contribution to cancer development, showing that it is overexpressed in most human breast tumors, activates ERBB signaling and increases the metastatic potential of breast cancer cells. Our comparison on two breast cancer lines did not reveal any common receptors but identical structural prerequisites for the peptide in all its activities. We hypothesize that LL-37 indirectly activates transmembrane receptors by attaching to the cellular membrane. Truncated derivatives inhibit its activities and may help to design a future anticancer therapy
Chapitres de livres sur le sujet "Peptide LL-37":
Beaumont, Paula E., Hsin-Ni Li et Donald J. Davidson. « LL-37 : An Immunomodulatory Antimicrobial Host Defence Peptide ». Dans Antimicrobial Peptides and Innate Immunity, 97–121. Basel : Springer Basel, 2012. http://dx.doi.org/10.1007/978-3-0348-0541-4_4.
Nylén, Frank, Peter Bergman, Gudmundur H. Gudmundsson et Birgitta Agerberth. « Assays for Identifying Inducers of the Antimicrobial Peptide LL-37 ». Dans Methods in Molecular Biology, 271–81. New York, NY : Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6737-7_19.
Wang, Guangshun, Jayaram Lakshmaiah Narayana, Biswajit Mishra, Yingxia Zhang, Fangyu Wang, Chunfeng Wang, D. Zarena, Tamara Lushnikova et Xiuqing Wang. « Design of Antimicrobial Peptides : Progress Made with Human Cathelicidin LL-37 ». Dans Advances in Experimental Medicine and Biology, 215–40. Singapore : Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-3588-4_12.
Sorkin, M., F. Jacobsen, D. Mittler, T. Hirsch, A. Gerhards, M. Lehnhardt, H. U. Steinau et L. Steinstraesser. « Kutane adenovirale Gentherapie mit humanem Host Defense Peptid LL-37 in infizierten Verbrennungswunden der Ratte ». Dans Chirurgisches Forum 2006, 357–58. Berlin, Heidelberg : Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-34668-6_123.
Actes de conférences sur le sujet "Peptide LL-37":
Biondi, Barbara, Silvia Millan, Fernando Formaggio, Alessandra Semenzato et Cristina Peggion. « Synthesis and conformationof short peptides modeled after peptide LL-37 ». Dans 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.195.
Lee, Jia-Yi, Chung-Yih Wang, Chi-Fang Huang et An-Ting Cheng. « Interdigitated electrodes based on impedance biosensor for sensing peptide LL-37 ». Dans 2011 33rd Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2011. http://dx.doi.org/10.1109/iembs.2011.6089899.
Wang, Guangshun. « Design potent peptide antibiotics against the ESKAPE pathogens based on human antimicrobial peptide LL-37 ». Dans 4th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland : MDPI, 2018. http://dx.doi.org/10.3390/ecmc-4-05882.
Lu, Xiuxiu, Qi Zhang, Guowei Song, Xiaodai Cui, Jian Yang et Baoyuan Zhang. « The Changes of Plasma Antibacterial Peptide ll-37 in the Bloodstream Infected Children ». Dans Selection of Abstracts From NCE 2016. American Academy of Pediatrics, 2018. http://dx.doi.org/10.1542/peds.141.1_meetingabstract.331.
McCaskill, Michael L., Jill A. Poole, Diane S. Allen-Gipson, Jane M. DeVasure et Todd A. Wyatt. « Ethanol Consumption Leads To Reduced Levels Of Lung Tissue Vitamin D And Anti-Microbial Peptide LL-37 In C57Bl/6 Mice ». Dans American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4670.
Krasnodembskaya, Anna, Yuanlin Song, Jae-Woo Lee et Michael A. Matthay. « Human Mesenchymal Stem Cells Exert Antimicrobial Activity In Vitro And In Vivo In Part Through The Secretion Of The Antimicrobial Peptide LL-37 ». Dans American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1246.
Schrumpf, Jasmijn, Renate Verhoosel et Pieter Hiemstra. « Vitamin D-mediated expression of the antimicrobial peptide hCAP18/LL-37 and killing of non-typeablehaemophilus influenzae(NTHi) is reduced after 14 days exposure to TNF-α and IL-1β in primary bronchial epithelial cells (PBEC) ». Dans Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.oa1785.
Valencia, Yeny Y. P., Gabriel C. A. da Hora et Thereza A. Soares. « INTERAÇÃO DE AGREGADOS DE POPG NA PRESENÇA DE PEPTIDEO ANTIMICROBIANOS LL 37 ». Dans Encontro Anual da biofisica 2019. São Paulo : Editora Blucher, 2019. http://dx.doi.org/10.5151/biofisica2019-23.