Cathelicidins, multifunctional peptides of the innate immunity

Antimicrobial peptides of multicellular organisms

Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457

Endogenous Antimicrobial Peptides and Skin Infections in Atopic Dermatitis

Ong, P. Y., Ohtake, T., Brandt, C., Strickland, I., Boguniewicz, M., Ganz, T., Gallo, R. L., & Leung, D. Y. M. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa021481 · Cited by 1,960

Amphipathic, α-helical antimicrobial peptides

Tossi, A., Sandri, L., & Giangaspero, A. (2000) · Biopolymers · doi:10.1002/1097-0282(2000)55:1 · Cited by 1,259

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

Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J., Wooters, J., Oppenheim, J. J., & Chertov, O. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1069 · Cited by 1,238

The role of cationic antimicrobial peptides in innate host defences

Hancock, R. E. W., & Diamond, G. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01823-0 · Cited by 1,233

Innate antimicrobial peptide protects the skin from invasive bacterial infection

Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198

Biology of the Syndecans: A Family of Transmembrane Heparan Sulfate Proteoglycans

Bernfield, M. R., Kokenyesi, R., Kato, M., Hinkes, M. T., Spring, J., Gallo, R. L., & Lose, E. J. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.002053 · Cited by 1,099

Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Sørensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., & Borregaard, N. (2001) · Blood · doi:10.1182/blood.v97.12.3951 · Cited by 894

An angiogenic role for the human peptide antibiotic LL-37/hCAP-18

Koczulla, R., von Degenfeld, G., Kupatt, C., Krötz, F., Zahler, S., GLOE, T. R., Issbrücker, K., Unterberger, P., Zaiou, M., Lebherz, C., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17545 · Cited by 880

The Expression of the Gene Coding for the Antibacterial Peptide LL-37 Is Induced in Human Keratinocytes during Inflammatory Disorders

Frohm, M., Agerberth, B., Ahangari, G., Ståhle‐Bäckdahl, M., Lidén, S., Wigzell, H., & Gudmundsson, G. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15258 · Cited by 803

Cathelicidin Peptide LL-37 Modulates TREM-1 Expression and Inflammatory Responses to Microbial Compounds

Amatngalim, G. D., Nijnik, A., Hiemstra, P. S., & Hancock, R. E. W. (2010) · Inflammation · doi:10.1007/s10753-010-9248-6 · Cited by 29

Regulation of LL-37 in Bone and Periodontium Regeneration

Chinipardaz, Z., Zhong, J. M., & Yang, S. (2022) · Life · doi:10.3390/life12101533 · Cited by 28

Antimicrobial peptides (AMPs) from microalgae as an alternative to conventional antibiotics in aquaculture

Vasquez-Moscoso, C. A., Merlano, J. A. R., Gálvez, A. O., & Almeida, D. V. (2024) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2024.2365357 · Cited by 29

Tissue specificity and species superiority of cathelicidin gene expression in Chinese indigenous Min pigs

Ma, Q., Jiao, W., Wang, Z. Y., Wu, C., Shan, A. S., Wang, Y. B., & Cai, J. (2014) · Livestock Science · doi:10.1016/j.livsci.2014.01.004 · Cited by 28

Human cathelicidin peptide LL37 binds telomeric G-quadruplex

Jana, J., Kar, R. K., Ghosh, A., Biswas, A., Ghosh, S., Bhunia, A., & Chatterjee, S. (2013) · Molecular BioSystems · doi:10.1039/c3mb70030e · Cited by 28

Extra-skeletal effects of vitamin D deficiency in chronic kidney disease

Chonchol, M., Kendrick, J., & Targher, G. (2011) · Annals of Medicine · doi:10.3109/07853890.2010.543923 · Cited by 29

Albumin-Based LL37 Peptide Nanoparticles as a Sustained Release System against Pseudomonas aeruginosa Lung Infection

Yang, L., Liu, Y., Wang, N., Wang, H., Wang, K., Luo, X., Dai, R., Tao, R., Wang, H., Yang, J., et al. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c01084 · Cited by 28

Efficacy of Cathelicidin LL-37 in an MRSA Wound Infection Mouse Model

Simonetti, O., Cirioni, O., Goteri, G., Lucarini, G., Kamysz, E., Kamysz, W., Orlando, F., Rizzetto, G., Molinelli, E., Morroni, G., et al. (2021) · Antibiotics · doi:10.3390/antibiotics10101210 · Cited by 28

Changes in the Profile of Fecal Microbiota and Metabolites as Well as Serum Metabolites and Proteome After Dietary Inulin Supplementation in Dairy Cows With Subclinical Mastitis

Wang, Y., Nan, X., Zhao, Y., Jiang, L., Wang, H., Zhang, F., Hua, D., Liu, J., Yang, L., Yao, J., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.809139 · Cited by 27

An outer membrane protease of the omptin family prevents activation of the Citrobacter rodentium PhoPQ two‐component system by antimicrobial peptides

Sage, V. L., Zhu, L., Lepage, C., Portt, A. E., Viau, C., Daigle, F., Gruenheid, S., & Moual, H. L. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06854.x · Cited by 27

Expression of Antimicrobial Peptides in Human Monocytic Cells and Neutrophils in Response to Dengue Virus Type 2

Castañeda‐Sánchez, J. I., Domínguez-Martínez, D. A., Olivar-Espinosa, N., García‐Pérez, B. E., Loroño-Pino, M. A., Luna‐Herrera, J., & Salazar, M. I. (2016) · Intervirology · doi:10.1159/000446282 · Cited by 28

Diversity, immunoregulatory action and structure-activity relationship of green sea turtle cathelicidins

Qiao, X., Yang, H., Gao, J., Zhang, F., Chu, P., Yang, Y., Zhang, M., Wang, Y., & Yu, H. (2019) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2019.05.005 · Cited by 27

Targeting Damage-Associated Molecular Pattern Molecules (DAMPs) and DAMP Receptors in Melanoma

Boone, B. A., & Lotze, M. T. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-727-3_29 · Cited by 27

PMAP-36 reduces the innate immune response induced by Bordetella bronchiseptica-derived outer membrane vesicles

Balhuizen, M. D., Versluis, C. M., van Harten, R. M., de Jonge, E. F., Brouwers, J. F. H. M., van de Lest, C. H. A., Veldhuizen, E. J. A., Tommassen, J., & Haagsman, H. P. (2020) · Current Research in Microbial Sciences · doi:10.1016/j.crmicr.2020.100010 · Cited by 27

Characterization of Noncompetitive Regulators of Proteasome Activity

Gaczynska, M. E., & Osmulski, P. A. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)98035-x · Cited by 27

Pulmonary defense and the human cathelicidin hCAP-18/LL-37

Fahy, R. J., & Wewers, M. D. (2005) · Immunologic Research · doi:10.1385/ir:31:2:075 · Cited by 27

Antimicrobial Host Defense Peptides in an Arteriviral Infection: Differential Peptide Expression and Virus Inactivation

Sang, Y., Ruchala, P. P., Lehrer, R. I., Ross, C. R., Rowland, R. R. R., & Blecha, F. (2009) · Viral Immunology · doi:10.1089/vim.2009.0005 · Cited by 27

Induction and antimicrobial activity of platelet basic protein derivatives in human monocytes

Schaffner, A., King, C. C., Schaer, D. J., & Guiney, D. G. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0404261 · Cited by 27

When less means more: dehydration improves innate immunity in rattlesnakes

Brusch, G. A., & DeNardo, D. F. (2017) · Journal of Experimental Biology · doi:10.1242/jeb.155028 · Cited by 26

Bioactive Synthetic Peptides for Oral Tissues Regeneration

Bermúdez, M., Hoz, L., Montoya, G. A., Campos, M. N., Pérez‐Soria, A., Romo, E., Soto‐Barreras, U., Garnica-Palazuelos, J. C., Aguilar‐Medina, M., Ramos‐Payán, R., et al. (2021) · Frontiers in Materials · doi:10.3389/fmats.2021.655495 · Cited by 26

Molecular characterization of cathelicidin in tiger frog (Hoplobatrachus rugulosus): Antimicrobial activity and immunomodulatory activity

Chen, J., Lin, Y., Chen, J.-H., Chen, X., & Lin, Z. (2021) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2021.109072 · Cited by 26

Scale-up production of and dietary supplementation with the recombinant antimicrobial peptide tilapia piscidin 4 to improve growth performance in Gallus gallus domesticus

Tai, H.-M., You, M., Lin, C., Tsai, T.-Y., Pan, C., & Chen, J. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253661 · Cited by 26

Modulation of cytokine gene expression by cathelicidin BMAP-28 in LPS-stimulated and -unstimulated macrophages

D’Este, F., Tomasinsig, L., Skerlavaj, B., & Zanetti, M. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.01.010 · Cited by 26

Copy number polymorphisms are not a common feature of innate immune genes

Linzmeier, R. M., & Ganz, T. (2006) · Genomics · doi:10.1016/j.ygeno.2006.03.005 · Cited by 26

Identification and characterization of novel bi-functional cathelicidins from the black-spotted frog (Pelophylax nigromaculata) with both anti-infective and antioxidant activities

Wang, Y., Ouyang, J., Luo, X., Zhang, M., Jiang, Y., Zhang, F., Jiang, Z., & Wang, Y. (2020) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2020.103928 · Cited by 25

Rescuing humanity by antimicrobial peptides against colistin-resistant bacteria

Moghadam, M. T., Mojtahedi, A., Moghaddam, M. M., Fasihi‐Ramandi, M., & Mirnejad, R. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11940-z · Cited by 26

Influence of Vitamin D on Periodontal Inflammation: A Review

Meghil, M. M., & Cutler, C. W. (2023) · Pathogens · doi:10.3390/pathogens12091180 · Cited by 25

Substance P in Polymicrobial Sepsis: Molecular Fingerprint of Lung Injury in Preprotachykinin-A−/− Mice

Hegde, A., Tamizhselvi, R., Manikandan, J., Melendez, A. J., Moochhala, S., & Bhatia, M. (2010) · Molecular Medicine · doi:10.2119/molmed.2009.00166 · Cited by 25

Expression and regulation of antimicrobial peptide rCRAMP after bacterial infection in primary rat meningeal cells

Brandenburg, L., Varoga, D. J., Nicolaeva, N., Leib, S. L., Podschun, R., Wruck, C. J., Wilms, H., Lucius, R., & Pufe, T. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.10.004 · Cited by 25

Differential proteomic analysis reveals increased cathelicidin expression in porcine bronchoalveolar lavage fluid after an Actinobacillus pleuropneumoniae infection

Hennig‐Pauka, I., Jacobsen, I. D., Blecha, F., Waldmann, K.-H., & Gerlach, G.-F. (2005) · Veterinary Research · doi:10.1051/vetres:2005043 · Cited by 25

Gr-1+CD11b+ cells as an accelerator of sepsis stemming fromPseudomonas aeruginosawound infection in thermally injured mice

Kobayashi, M., Yoshida, T., Takeuchi, D., Jones, V. C., Shigematsu, K., Herndon, D. N., & Suzuki, F. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.0807541 · Cited by 25

MrgX2‑mediated internalization of LL‑37 and degranulation of human LAD2 mast cells

Murakami, T., Suzuki, K., Niyonsaba, F., Tada, H., Reich, J., Tamura, H., & Nagaoka, I. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9532 · Cited by 25

Comparative activity and mechanism of action of three types of bovine antimicrobial peptides against pathogenic Prototheca spp.

Tomasinsig, L., Skerlavaj, B., Scarsini, M., Guida, F., Piccinini, R., Tossi, A., & Zanetti, M. (2011) · Journal of Peptide Science · doi:10.1002/psc.1422 · Cited by 24

Perforin-2 Breaches the Envelope of Phagocytosed Bacteria Allowing Antimicrobial Effectors Access to Intracellular Targets

Bai, F., McCormack, R., Hower, S., Plano, G. V., Lichtenheld, M. G., & Munson, G. P. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800365 · Cited by 23

Bombyx mori gloverin A2 alleviates enterotoxigenic Escherichia coli-induced inflammation and intestinal mucosa disruption

Lin, Q., Su, G., Wu, A., Chen, D., Yu, B., Huang, Z., Luo, Y., Mao, X., Zheng, P., Yu, J., et al. (2019) · Antimicrobial Resistance and Infection Control · doi:10.1186/s13756-019-0651-y · Cited by 24

Antimicrobial activity of a bovine myeloid antimicrobial peptide (BMAP‐28) against methicillin‐susceptible and methicillin‐resistant Staphylococcus aureus

Takagi, S., Hayashi, S., Takahashi, K., Isogai, H., Bai, L., Hiroshi Yoneyama, C., Ando, T., Ito, K., & Isogai, E. (2011) · Animal Science Journal · doi:10.1111/j.1740-0929.2011.00979.x · Cited by 24

Gingival crevicular fluid levels of human beta‐defensin‐2 and cathelicidin in smoker and non‐smoker patients: a cross‐sectional study

Ertuğrul, A. S., Sahin, H., Dikilitaş, A., Alpaslan, N. Z., Bozoğlan, A., & Tekin, Y. (2013) · Journal of Periodontal Research · doi:10.1111/jre.12105 · Cited by 24

Alarmins and antimicrobial immunity

Yang, D., & Oppenheim, J. J. (2009) · Medical Mycology · doi:10.1080/13693780902721416 · Cited by 24

Expression, Purification and Antibacterial Activity of NK-Lysin Mature Peptides from the Channel Catfish (Ictalurus punctatus)

Cai, S., Wang, J., Wang, K., Chen, D., Dong, X.-W., Liu, T., Zeng, Y., Wang, X., & Wu, D. (2016) · Applied Sciences · doi:10.3390/app6090240 · Cited by 24

Entamoeba histolytica Cathepsin-Like Enzymes

Kissoon‐Singh, V., Mortimer, L. M., & Chadee, K. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-8414-2_5 · Cited by 24

Antimicrobial peptides isolated from the blood of farm animals

Yu, P., van der Linden, D. S., Sugiarto, H., & Anderson, R. C. (2010) · Animal Production Science · doi:10.1071/ea07185 · Cited by 23

Induced expression of cathelicidins in trout ( Oncorhynchus mykiss ) challenged with four different bacterial pathogens

Furlan, M., Rosani, U., Gambato, S., Irato, P., Manfrin, A., Mardirossian, M., Venier, P., Pallavicini, A., & Scocchi, M. (2018) · Journal of Peptide Science · doi:10.1002/psc.3089 · Cited by 23

Heparin– LL 37 complexes are less cytotoxic for human dental pulp cells and have undiminished antimicrobial and LPS ‐neutralizing abilities

Yoshida, K., Suzuki, S., Kawada‐Matsuo, M., Nakanishi, J., Hirata‐Tsuchiya, S., Komatsuzawa, H., Yamada, S., & Shiba, H. (2019) · International Endodontic Journal · doi:10.1111/iej.13130 · Cited by 24

Design of a Sea Snake Antimicrobial Peptide Derivative with Therapeutic Potential against Drug-Resistant Bacterial Infection

Gao, J., Zhang, M., Zhang, F., Wang, Y., Ouyang, J., Luo, X., Yang, H., Zhang, D., Chen, Y., Yu, H., et al. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00255 · Cited by 23

Biological role of fish antimicrobial peptides

Chaves-Pozo, E., Cuesta, A., Esteban, M. Á., Valero, Y., & Meseguer, J. (2013) · Cited by 23

PR-39, a porcine host defence peptide, is prominent in mucosa and lymphatic tissue of the respiratory tract in healthy pigs and pigs infected with actinobacillus pleuropneumoniae

Hennig‐Pauka, I., Koch, R., Hoeltig, D., Gerlach, G.-F., Waldmann, K.-H., Blecha, F., Brauer, C., & Gasse, H. (2012) · BMC Research Notes · doi:10.1186/1756-0500-5-539 · Cited by 23

Transcriptional regulation of antimicrobial peptides in mucosal tissues of Atlantic codGadus morhuaL. in response to different stimuli

Ruangsri, J., Lokesh, J., Fernandes, J. M. O., & Kiron, V. (2013) · Aquaculture Research · doi:10.1111/are.12136 · Cited by 23

Structure dependence of biological activities for primate cathelicidins

Tomasinsig, L., Morgera, F., Antcheva, N., Pacor, S., Skerlavaj, B., Zanetti, M., & Tossi, A. (2009) · Journal of Peptide Science · doi:10.1002/psc.1143 · Cited by 23

Enhanced antimicrobial activity of peptide-cocktails against common bacterial contaminants of ex vivo stored platelets

Mohan, K. V. K., Rao, S. S., Gao, Y. S., & Atreya, C. D. (2013) · Clinical Microbiology and Infection · doi:10.1111/1469-0691.12326 · Cited by 23

Modulation of cathelicidins, IFNβ and TNFα by bovine alpha-herpesviruses is dependent on the stage of the infectious cycle

Burucúa, M., Quintana, S., Lendez, P. A., Cobo, E. R., Ceriani, M. C., Dolcini, G. L., Odeón, A. C., Pérez, S., & Marin, M. S. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.04.022 · Cited by 23

Two short antimicrobial peptides derived from prosaposin-like proteins in the starry flounder (Platichthys stellatus)

Choi, K.-M., Hwang, S. D., Joo, M.-S., Hwang, J. Y., Kwon, M., Jeong, J.-M., Seo, J. S., Lee, J. H., Lee, H.-C., & Park, C. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.05.075 · Cited by 23

Expression of antimicrobial peptide genes oscillates along day/night rhythm protecting mice skin from bacteria

Bilska, B., Zegar, A., Slominski, A. T., Kleszczyński, K., Cichy, J., & Pyza, E. (2020) · Experimental Dermatology · doi:10.1111/exd.14229 · Cited by 23

Inhibition of Adherence and Killing of Candida albicans with a 23-Mer Peptide (Fn/23) with Dual Antifungal Properties

Klotz, S., Gaur, N., Rauceo, J. M., Lake, D., Park, Y., Hahm, K., & Lipke, P. (2004) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.48.11.4337-4341.2004 · Cited by 28

Anti-endotoxic and antibacterial effects of a dermal substitute coated with host defense peptides

Kasetty, G., Kalle, M., Mörgelin, M., Brune, J. C., & Schmidtchen, A. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.02.111 · Cited by 22

Vitamin D Status and Expression of Vitamin D Receptor and LL-37 in Patients with Spontaneous Bacterial Peritonitis

Zhang, C., Zhao, L., Ma, L., Lv, C., Ding, Y., Xia, T., Wang, J., & Dou, X. (2011) · Digestive Diseases and Sciences · doi:10.1007/s10620-011-1824-6 · Cited by 22

Association of vitamin D receptor gene polymorphisms with chronic and aggressive periodontitis in Jordanian patients

Karasneh, J. A., Ababneh, K. T., Taha, A. H., Al‐Abbadi, M. S., Marzouka, N., Jaradat, S. A., & Thornhill, M. H. (2013) · European Journal Of Oral Sciences · doi:10.1111/eos.12085 · Cited by 22

Proline‐Rich Peptide Mimics Effects of Enamel Matrix Derivative on Rat Oral Mucosa Incisional Wound Healing

Villa, O., Wohlfahrt, J. C., Mdla, I., Petzold, C., Reseland, J. E., Snead, M. L., & Lyngstadaas, S. P. (2015) · Journal of Periodontology · doi:10.1902/jop.2015.150207 · Cited by 22

Assessing the potential of four cathelicidins for the management of mouse candidiasis and Candida albicans biofilms

Yu, H., Liu, X., Wang, C., Qiao, X., Wu, S., Wang, H., Feng, L., & Wang, Y. (2015) · Biochimie · doi:10.1016/j.biochi.2015.11.028 · Cited by 22

Human cathelicidin LL-37 inhibits platelet aggregation and thrombosis via Src/PI3K/Akt signaling

Su, W., Chen, Y., Wang, C., Ding, X., Rwibasira, G., & Kong, Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.095 · Cited by 22

Tryptophan end-tagging for promoted lipopolysaccharide interactions and anti-inflammatory effects

Singh, S., Datta, A., Schmidtchen, A., Bhunia, A., & Malmsten, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-00188-7 · Cited by 22

Helicobacter pylori promote inflammation and host defense through the cagA‐dependent activation of mTORC1

Feng, G., Chen, Y., & Li, K. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29826 · Cited by 22

Malassezia sympodialis differently affects the expression of LL‐37 in dendritic cells from atopic eczema patients and healthy individuals

Agerberth, B., Buentke, E., Bergman, P., Eshaghi, H., Gabrielsson, S., Gudmundsson, G. H., & Scheynius, A. (2005) · Allergy · doi:10.1111/j.1398-9995.2005.00952.x · Cited by 22

Targeting the lipopolysaccharides: still a matter of debate?

Nahra, R., & Dellinger, R. P. (2008) · Current Opinion in Anaesthesiology · doi:10.1097/aco.0b013e3282f5335c · Cited by 22

Complementary Effects of Carbamylated and Citrullinated LL37 in Autoimmunity and Inflammation in Systemic Lupus Erythematosus

Lande, R., Pietraforte, I., Mennella, A., Palazzo, R., Spinelli, F. R., Giannakakis, K., Spadaro, F., Falchi, M., Riccieri, V., Stefanantoni, K., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041650 · Cited by 21

Potential Novel Biomarkers for Mastitis Diagnosis in Sheep

Libera, K., Konieczny, K., Grabska, J., Smulski, S., Szczerbal, I., Szumacher‐Strabel, M., & Pomorska‐Mól, M. (2021) · Animals · doi:10.3390/ani11102783 · Cited by 21

Synergy Mechanisms of Daptomycin-Fosfomycin Combinations in Daptomycin-Susceptible and -Resistant Methicillin-Resistant Staphylococcus aureus: In Vitro , Ex Vivo , and In Vivo Metrics

Mishra, N. N., Lew, C., Abdelhady, W., Lapitan, C. K., Proctor, R. A., Rose, W. E., & Bayer, A. S. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01649-21 · Cited by 25

Cathelicidin-HG Alleviates Sepsis-Induced Platelet Dysfunction by Inhibiting GPVI-Mediated Platelet Activation

Xiong, W., Chai, J., Wu, J., Li, J., Lu, W., Tian, M., Jmel, M. A., Ippel, H., Kotsyfakis, M., Dijkgraaf, I., et al. (2024) · Research · doi:10.34133/research.0381 · Cited by 21

The effects of the BT/TAMUS 2032 cationic peptides on innate immunity and susceptibility of young chickens to extraintestinal Salmonella enterica serovar Enteritidis infection

Kogut, M. H., Genovese, K. J., He, H., Li, M. A., & Jiang, Y. (2007) · International Immunopharmacology · doi:10.1016/j.intimp.2007.02.011 · Cited by 21

The Antimicrobial Peptide Lysozyme Is Induced after Multiple Trauma

Klüter, T., Fitschen‐Oestern, S., Lippross, S., Weuster, M., Mentlein, R., Steubesand, N., Neunaber, C., Hildebrand, F., Pufe, T., Tohidnezhad, M., et al. (2014) · Mediators of Inflammation · doi:10.1155/2014/303106 · Cited by 21

Heparan Sulfate Proteoglycan–Involving Immunomodulation by Cathelicidin Antimicrobial Peptides LL-37 and PR-39

Kaneider, N. C., Djanani, A. M., & Wiedermann, C. J. (2007) · The Scientific World JOURNAL · doi:10.1100/tsw.2007.285 · Cited by 21

Insect-Derived Short Proline-Rich and Murine Cathelicidin-Related Antimicrobial Peptides Act Synergistically on Gram-Negative Bacteria In Vitro

Knappe, D., Kabankov, N., Herth, N., & Hoffmann, R. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0083 · Cited by 21

Cathelicidin augments VDR-dependent anti-leishmanial immune response in Indian Post-Kala-Azar Dermal Leishmaniasis

Das, S., Sardar, A. H., Abhishek, K., Kumar, A., Rabidas, V. N., & Das, P. K. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.06.010 · Cited by 21

Bacterial Evasion of Host Antimicrobial Peptide Defenses

Cole, J. N., & Nizet, V. (2016) · ASM Press eBooks · doi:10.1128/9781555819286.ch15 · Cited by 21

Tumor macrophage redox and effector mechanisms associated with hypoxia

Espey, M. G. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.026 · Cited by 21

In Vitro Activities of Tritrpticin Alone and in Combination with Other Antimicrobial Agents against Pseudomonas aeruginosa

Cirioni, O., Giacometti, A., Silvestri, C., Vittoria, A. D., Licci, A., Riva, A., & Scalise, G. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00652-06 · Cited by 21

Molecular characterization of a novel ovodefensin gene in chickens

Yu, L., Xiao, Y., Li, J., Ran, J., Yin, L., Liu, Y., & Zhang, L. (2018) · Gene · doi:10.1016/j.gene.2018.08.029 · Cited by 20

Current approaches and future prospects of nanofibers: a special focus on antimicrobial drug delivery

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