PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35173253-6 2022 Interestingly, some AMPs, such as SMAP29, dissociated from the AMP-HDL complex and translocated to bacteria upon contact, while some AMPs, such as LL37, remained in complex with HDL. Adenylyl sulfate 133-137 cathelicidin antimicrobial peptide Homo sapiens 147-151 35077676-3 2022 Here, we used native mass spectrometry to measure the stoichiometry of three different AMPs-LL-37, indolicidin, and magainin-2-in lipid nanodiscs. Adenylyl sulfate 87-91 cathelicidin antimicrobial peptide Homo sapiens 92-97 34787608-1 2021 Antimicrobial peptides (AMPs), such as LL37 peptides, may be immobilized on the surface of medical devices to render them with antimicrobial and angiogenic properties. Adenylyl sulfate 24-28 cathelicidin antimicrobial peptide Homo sapiens 39-43 28606090-6 2017 Among various AMPs tested LL-37 and indolicidin, showed promise to be potential candidates for eliciting enhanced host innate immune responses. Adenylyl sulfate 14-18 cathelicidin antimicrobial peptide Homo sapiens 26-31 30845777-11 2019 Our study determines an extensive profile of AMPs expressed in the human cornea during S. pneumoniae infection, and suggests the potential of LL-37 to be developed as an alternative therapeutic intervention to fight increasing antibiotic resistance among bacteria. Adenylyl sulfate 45-49 cathelicidin antimicrobial peptide Homo sapiens 142-147 30095901-1 2018 Antimicrobial peptides (AMPs) such as LL37 are promising alternatives to antibiotics to treat wound infections due to their broad activity, immunomodulatory functions, and low likelihood of antimicrobial resistance. Adenylyl sulfate 24-28 cathelicidin antimicrobial peptide Homo sapiens 38-42 28094872-3 2017 AMPs that are present on human skin include psoriasin (S100A7), RNase 7, lysozyme, LL-37 and defensins. Adenylyl sulfate 0-4 cathelicidin antimicrobial peptide Homo sapiens 83-88 28666755-6 2017 LL37 and HbetaD3 were the most active AMPs tested, with MICs ranging from 3.2- >= 200 mg/L and 4.8- >= 200 mg/L, respectively, except for Achromobacter that was resistant. Adenylyl sulfate 38-42 cathelicidin antimicrobial peptide Homo sapiens 0-4 32183275-2 2020 In the respiratory tract, the cationic peptide LL-37 is one of the most abundant AMPs and capable of building pore complexes in usually negatively charged bacterial membranes, leading to the destruction of bacteria. Adenylyl sulfate 81-85 cathelicidin antimicrobial peptide Homo sapiens 47-52 30833557-2 2019 Some AMPs are also strongly immunomodulatory: LL37-DNA complexes potently amplify Toll-like receptor 9 (TLR9) activation in immune cells and exacerbate autoimmune diseases. Adenylyl sulfate 5-9 cathelicidin antimicrobial peptide Homo sapiens 46-50 29211886-3 2018 We investigated the capacity of the human cationic AMP LL-37 to kill SCVs in the presence of physiological concentrations of bicarbonate, which are reported to alter bacterial membrane permeability and change resistance of bacteria to AMPs. Adenylyl sulfate 235-239 cathelicidin antimicrobial peptide Homo sapiens 55-60 28298400-8 2017 In stable COPD, high sputum hCAP18/LL-37 levels were associated with increased risk of AECOPD, non-typeable Haemophilus influenzae colonisation, higher age, ex-smoking and higher levels of inflammatory markers.Altered levels of selected AMPs are linked to airway inflammation, infection and AECOPD, suggesting a role for these peptides in airway defence mechanisms in COPD. Adenylyl sulfate 237-241 cathelicidin antimicrobial peptide Homo sapiens 28-34 28298400-8 2017 In stable COPD, high sputum hCAP18/LL-37 levels were associated with increased risk of AECOPD, non-typeable Haemophilus influenzae colonisation, higher age, ex-smoking and higher levels of inflammatory markers.Altered levels of selected AMPs are linked to airway inflammation, infection and AECOPD, suggesting a role for these peptides in airway defence mechanisms in COPD. Adenylyl sulfate 237-241 cathelicidin antimicrobial peptide Homo sapiens 35-40 24588384-4 2014 Two AMPs, human beta-defensin 2 and LL-37, were fused to the self-cleaving tag and expressed as active protein aggregates. Adenylyl sulfate 4-8 cathelicidin antimicrobial peptide Homo sapiens 36-41 27232359-10 2016 Combinations among AMPs, mainly LL-37, were positively associated with caries levels. Adenylyl sulfate 19-23 cathelicidin antimicrobial peptide Homo sapiens 32-37 23884095-3 2014 In humans, AMPs include the defensins (alpha- and beta-families) and the cathelicidin, LL-37. Adenylyl sulfate 11-15 cathelicidin antimicrobial peptide Homo sapiens 87-92 27440892-3 2016 In this study, through the expression of a small library of human secretory proteins containing amphipathic alpha-helix structures, we identified the human cathelicidin antimicrobial peptide (CAMP), the only known member of the cathelicidin family of antimicrobial peptides (AMPs) in humans and expressed mainly in bone marrow and leukocytes. Adenylyl sulfate 275-279 cathelicidin antimicrobial peptide Homo sapiens 156-190 27440892-3 2016 In this study, through the expression of a small library of human secretory proteins containing amphipathic alpha-helix structures, we identified the human cathelicidin antimicrobial peptide (CAMP), the only known member of the cathelicidin family of antimicrobial peptides (AMPs) in humans and expressed mainly in bone marrow and leukocytes. Adenylyl sulfate 275-279 cathelicidin antimicrobial peptide Homo sapiens 192-196 24747281-4 2014 Human AMPs; cathelicidin (LL37) and defensins have immunomodulatory properties and are involved in the pathogenesis of many inflammatory disorders. Adenylyl sulfate 6-10 cathelicidin antimicrobial peptide Homo sapiens 26-30 24747281-10 2014 However, serum LL37 and defensins were found to be remarkably higher in FMF patients compared to healthy individuals both at baseline and 6 months after initiation of colchicine therapy which suggest that AMPs might have a role in the pathogenesis of FMF. Adenylyl sulfate 205-209 cathelicidin antimicrobial peptide Homo sapiens 15-19 24265220-5 2014 CAMP is manually curated and currently holds 6756 sequences and 682 3D structures of AMPs. Adenylyl sulfate 85-89 cathelicidin antimicrobial peptide Homo sapiens 0-4 24174616-5 2013 In this study, we describe that p33, a negatively charged surface protein found on endothelial cells also known as gC1q receptor, protects host cells from a cytolytic attack by antimicrobial peptides (AMPs), such as LL37 and beta-defensin 3. Adenylyl sulfate 201-205 cathelicidin antimicrobial peptide Homo sapiens 216-220 22410863-1 2012 Overexpression of antimicrobial peptides and proteins (AMPs) such as human beta-defensin-2 (hBD2), LL37, and psoriasin has frequently been observed in lesional skin of psoriasis patients. Adenylyl sulfate 55-59 cathelicidin antimicrobial peptide Homo sapiens 99-103 19923233-11 2010 CAMP will be a useful database for study of sequence-activity and -specificity relationships in AMPs. Adenylyl sulfate 96-100 cathelicidin antimicrobial peptide Homo sapiens 0-4 22023339-2 2012 We previously found that the AMPs (antimicrobial peptides) LL37 and hBD-3 (human beta-defensin-3) inhibited C. albicans viability and its adhesion to plastic. Adenylyl sulfate 29-33 cathelicidin antimicrobial peptide Homo sapiens 59-63 22144482-6 2012 Time course assays monitoring the degradation of LL-37 and C18G showed that EHEC cells degraded both AMPs faster than EPEC cells in an OmpT-dependent manner. Adenylyl sulfate 101-105 cathelicidin antimicrobial peptide Homo sapiens 49-54 22144482-10 2012 We hypothesize that the different contributions of EHEC and EPEC OmpT to the degradation and inactivation of LL-37 may be due to their adaptation to their respective niches within the host, the colon and small intestine, respectively, where the environmental cues and abundance of AMPs are different. Adenylyl sulfate 281-285 cathelicidin antimicrobial peptide Homo sapiens 109-114 20195469-8 2010 Surprisingly, the secretion of two inducible AMPs, LL-37 and hBD2, was not affected by L94A mutation. Adenylyl sulfate 45-49 cathelicidin antimicrobial peptide Homo sapiens 51-56 22521196-1 2012 To develop novel antimicrobial peptides (AMPs) with shorter lengths, improved prokaryotic selectivity and retained lipolysaccharide (LPS)-neutralizing activity compared to human cathelicidin AMP, LL-37, a series of amino acid-substituted analogs based on IG-19 (residues 13-31 of LL-37) were synthesized. Adenylyl sulfate 41-45 cathelicidin antimicrobial peptide Homo sapiens 280-285 18717821-1 2008 Cathelicidin (hCAP-18/LL-37) and beta-defensin 1 (HBD-1) are human antimicrobial peptides (AMPs) with high basal expression levels, which form the first line of host defence against infections over the epithelial surfaces. Adenylyl sulfate 91-95 cathelicidin antimicrobial peptide Homo sapiens 14-21 18717821-1 2008 Cathelicidin (hCAP-18/LL-37) and beta-defensin 1 (HBD-1) are human antimicrobial peptides (AMPs) with high basal expression levels, which form the first line of host defence against infections over the epithelial surfaces. Adenylyl sulfate 91-95 cathelicidin antimicrobial peptide Homo sapiens 22-27 16100459-1 2005 Defensins and cathelicidins (LL-37) are major antimicrobial peptides (AMPs) of the innate immune system of the human skin. Adenylyl sulfate 70-74 cathelicidin antimicrobial peptide Homo sapiens 29-34 18508823-3 2008 Pulmonary expression of the neutrophil-derived AMPs human cathelicidin (hCAP)-18/LL-37 and alpha-defensins (human neutrophil peptides (HNP) 1-3), and the epithelial cell-derived AMPs human beta-defensin (hBD)-2, elafin and secretory leukoprotease inhibitor (SLPI) were measured in stable lung transplant recipients and those with BOS. Adenylyl sulfate 47-51 cathelicidin antimicrobial peptide Homo sapiens 81-86 17107401-1 2006 BACKGROUND: The epidermal expression of antimicrobial peptides (AMPs) such as human beta-defensin (hBD)-2 and cathelicidin LL-37 is downregulated in atopic eczema (AE) as compared with psoriasis. Adenylyl sulfate 64-68 cathelicidin antimicrobial peptide Homo sapiens 123-128