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References from The limits of prediction: Why intrinsically disordered regions challenge our understanding of antimicrobial peptides. Local targets link to admitted publications; unresolved targets remain external evidence.
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Human hemoglobin-derived peptides exhibit antimicrobial activity: a class of host defense peptides
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Binding of an antimicrobial peptide to bacterial cells: Interaction with different species, strains and cellular components
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Mode-of-action of antimicrobial peptides: membrane disruption vs. intracellular mechanisms
10.3389/fmedt.2020.610997 · 2020 · External reference
The dual interaction of antimicrobial peptides on bacteria and cancer cells; mechanism of action and therapeutic strategies of nanostructures
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Spectroscopic study of antimicrobial peptides: structure and functional activity
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Engineering approaches for the development of antimicrobial peptide-based antibiotics
2022 · External reference
10.1021/acs.accounts.1c00047
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Membrane-disruptive peptides/peptidomimetics-based therapeutics: promising systems to combat bacteria and cancer in the drug-resistant era
2021 · External reference
The antimicrobial peptides and their potential clinical applications
2019 · External reference
Antimicrobial peptides: classification, design, application and research progress in multiple fields
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Unresolved reference
2022 · External reference
10.1146/annurev.biophys.37.032807.125924
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Does lack of secondary structure imply intrinsic disorder in proteins? A sequence analysis
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Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
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Cationic intrinsically disordered antimicrobial peptides (CIDAMPs) represent a new paradigm of innate defense with a potential for novel anti-infectives
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Specific metallo-protein interactions and antimicrobial activity in Histatin-5, an intrinsically disordered salivary peptide
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Structural and mechanistic insights into EchAMP: a antimicrobial protein from the Echidna milk
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The alphabet of intrinsic disorder: I. Act like a Pro: on the abundance and roles of proline residues in intrinsically disordered proteins
10.4161/idp.24360 · 2013 · External reference
10.1093/nar/gkab1082
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A theoretical approach to spot active regions in antimicrobial proteins
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MobiDB: 10 years of intrinsically disordered proteins
10.1093/nar/gkac1065 · 2023 · External reference
AMPA: an automated web server for prediction of protein antimicrobial regions
10.1093/bioinformatics/btr604 · 2011 · External reference
The C-terminus of panusin, a lobster β-defensin, is crucial for optimal antimicrobial activity and serum stability
10.3390/pharmaceutics15061777 · 2023 · External reference
Antibacterial activity of the human host defence peptide LL-37 and selected synthetic cationic lipids against bacteria associated with oral and upper respiratory tract infections
10.1093/jac/dks434 · 2012 · External reference
10.1093/nar/gks419
10.1093/nar/gks419 · External reference
10.1093/nar/gkw329
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10.1038/nprot.2006.202 · External reference
10.1073/pnas.1500851112
10.1073/pnas.1500851112 · External reference
Recombinant production of human antimicrobial peptide LL- 37 and its secondary structure
10.1007/s11756-023-01539-8 · 2023 · External reference
Physicochemical-guided design of cathelicidin-derived peptides generates membrane active variants with therapeutic potential
10.1038/s41598-020-66164-w · 2020 · External reference
10.1007/s13238-010-0004-3
10.1007/s13238-010-0004-3 · External reference
Design of an α-helical antimicrobial peptide with improved cell-selective and potent anti-biofilm activity
10.1038/srep27394 · 2016 · External reference
Membranome 2.0: database for proteome-wide profiling of bitopic proteins and their dimers
10.1093/bioinformatics/btx720 · 2018 · External reference
10.1093/nar/gkw712
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10.1080/08927020902902742
10.1080/08927020902902742 · External reference
Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes
10.1016/j.bbamem.2007.12.022 · 2008 · External reference
Topography studies on the membrane interaction mechanism of the eosinophil cationic protein
10.1021/bi061190e · 2007 · External reference
The antimicrobial peptide 1018-K6 interacts distinctly with eukaryotic and bacterial membranes, the basis of its specificity and bactericidal activity
10.3390/ijms232012392 · 2022 · External reference
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10.1021/acs.langmuir.1c02392 · External reference
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10.1093/nar/gkac933 · 2022 · External reference
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10.1038/s41467-023-36994-z · External reference
sAMPpred-GAT: prediction of antimicrobial peptide by graph attention network and predicted peptide structure
2022 · External reference
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10.1021/acs.jmedchem.1c00795 · External reference
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