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References from Evolving and assembling to pierce through: Evolutionary and structural aspects of antimicrobial peptides. Local targets link to admitted publications; unresolved targets remain external evidence.
Unresolved reference
External reference
Antimicrobial peptides: an update on classifications and databases
10.3390/ijms222111691 · 2021 · External reference
10.1002/9783527652853
10.1002/9783527652853 · External reference
10.1038/415389a
10.1038/415389a · External reference
10.1111/j.1574-6976.2001.tb00579.x
10.1111/j.1574-6976.2001.tb00579.x · External reference
10.1007/978-1-4419-7692-5
10.1007/978-1-4419-7692-5 · External reference
10.1146/annurev.micro.55.1.165
10.1146/annurev.micro.55.1.165 · External reference
Plant antimicrobial peptides: structures, functions, and applications
10.1186/s40529-021-00312-x · 2021 · External reference
10.1038/nature04051
10.1038/nature04051 · External reference
The history of alamethicin: a review of the most extensively studied peptaibol
10.1002/cbdv.200790095 · 2007 · External reference
10.1093/nar/gkv1278
10.1093/nar/gkv1278 · External reference
10.1093/nar/gkab651
10.1093/nar/gkab651 · External reference
10.3389/fmicb.2020.582779
10.3389/fmicb.2020.582779 · External reference
The biology of lactoferrin, an iron-binding protein that can help defend against viruses and bacteria
10.3389/fimmu.2020.01221 · 2020 · External reference
Antimicrobial peptides, polymorphic toxins, and self-nonself recognition systems in archaea: an untapped armory for intermicrobial conflicts
10.1128/mbio.00715-19 · 2019 · External reference
10.1016/j.biochi.2015.06.004
10.1016/j.biochi.2015.06.004 · External reference
A halocin acting on Na+/H+ exchanger of haloarchaea as a new type of inhibitor in NHE of mammals
10.1007/bf03165754 · 2006 · External reference
10.1038/ng1202-569
10.1038/ng1202-569 · External reference
10.2307/2408229
10.2307/2408229 · External reference
Antimicrobial peptides: application informed by evolution
10.1126/science.aau5480 · 2020 · External reference
10.1016/j.cub.2015.11.063
10.1016/j.cub.2015.11.063 · External reference
10.1016/j.mib.2008.05.001
10.1016/j.mib.2008.05.001 · External reference
10.1111/j.1420-9101.2005.00925.x
10.1111/j.1420-9101.2005.00925.x · External reference
Balancing selection drives the maintenance of genetic variation in drosophila antimicrobial peptides
10.1093/gbe/evz191 · 2019 · External reference
Survey of global genetic diversity within the drosophila immune system
10.1534/genetics.116.195016 · 2017 · External reference
The potential for adaptive maintenance of diversity in insect antimicrobial peptides
10.1098/rstb.2015.0291 · 2016 · External reference
Rapid seasonal evolution in innate immunity of wild Drosophila melanogaster
2018 · External reference
Dynamic evolution of antimicrobial peptides underscores trade-offs between immunity and ecological fitness
10.3389/fimmu.2019.02620 · 2019 · External reference
Trade-offs in evolutionary immunology: just what is the cost of immunity?
10.1034/j.1600-0706.2000.880110.x · 2000 · External reference
Immunity and other defenses in pea aphids, Acyrthosiphon pisum
10.1186/gb-2010-11-2-r21 · 2010 · External reference
Increased alpha-defensin expression is associated with risk of coronary heart disease: a feasible predictive inflammatory biomarker of coronary heart disease in hyperlipidemia patients
10.1186/s12944-016-0285-5 · 2016 · External reference
10.1016/j.numecd.2009.01.001
10.1016/j.numecd.2009.01.001 · External reference
10.1016/j.coi.2008.06.008
10.1016/j.coi.2008.06.008 · External reference
Diversity, evolution and medical applications of insect antimicrobial peptides
10.1098/rstb.2015.0290 · 2016 · External reference
10.1038/nrmicro1441
10.1038/nrmicro1441 · External reference
10.1007/s11030-006-9031-7
10.1007/s11030-006-9031-7 · External reference
10.1186/1471-2148-8-113
10.1186/1471-2148-8-113 · External reference
10.1016/j.molimm.2007.06.354
10.1016/j.molimm.2007.06.354 · External reference
Cysteine-rich antimicrobial peptides in invertebrates
10.1002/(sici)1097-0282(1998)47:6<465::aid-bip5>3.0.co;2-# · 1998 · External reference
10.1111/febs.13129
10.1111/febs.13129 · External reference
alpha-Defensins in human innate immunity
10.1111/j.1600-065x.2011.01082.x · 2012 · External reference
The defensins consist of two independent, convergent protein superfamilies
10.1093/molbev/msw106 · 2016 · External reference
Laterosporulin10: a novel defensin like Class IId bacteriocin from Brevibacillus sp. strain SKDU10 with inhibitory activity against microbial pathogens
10.1099/mic.0.000316 · 2016 · External reference
Roles of diversifying selection and coordinated evolution in the evolution of amphibian antimicrobial peptides
10.1093/oxfordjournals.molbev.a004143 · 2002 · External reference
Antimicrobial peptide and sequence variation along a latitudinal gradient in two anurans
10.1186/s12863-020-00839-1 · 2020 · External reference
Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
10.1016/s0005-2736(99)00201-1 · 1999 · External reference
Mode-of-action of antimicrobial peptides: membrane disruption vs. intracellular mechanisms
10.3389/fmedt.2020.610997 · 2020 · External reference
10.1007/978-981-13-3588-4_11
10.1007/978-981-13-3588-4_11 · External reference
Structure-activity relationship study of novel peptoids that mimic the structure of antimicrobial peptides
10.1128/aac.00237-15 · 2015 · External reference
Membrane interactions of designed cationic antimicrobial peptides: the two thresholds
10.1002/bip.20917 · 2008 · External reference
10.1074/jbc.m413406200
10.1074/jbc.m413406200 · External reference
Effects of hydrophobic amino acid substitutions on antimicrobial peptide behavior
10.1007/s12602-017-9345-z · 2018 · External reference
Structure-activity analysis of brevinin 1E amide, an antimicrobial peptide from Rana esculenta
10.1016/s0167-4838(98)00123-x · 1998 · External reference
Energetics of peptide and protein binding to lipid membranes
10.1007/978-1-4419-6327-7_2 · 2010 · External reference
10.1128/aac.00925-06
10.1128/aac.00925-06 · External reference
Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
10.1016/s0005-2736(99)00201-1 · 1999 · External reference
Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment
10.1016/s0014-5793(97)01266-0 · 1997 · External reference
10.1016/j.jmb.2007.05.016
10.1016/j.jmb.2007.05.016 · External reference
Design, synthesis, and characterization of a cytotoxic peptide with melittin-like activity
10.1021/ja00393a035 · 1981 · External reference
Structure-activity relationships of multifunctional host defence peptides
10.2174/138955710791383983 · 2010 · External reference
Hemolytic and antimicrobial activities of the twenty-four individual omission analogs of melittin
10.1021/bi00233a006 · 1991 · External reference
10.1002/psc.2574
10.1002/psc.2574 · External reference
10.1016/0014-5793(88)80077-2
10.1016/0014-5793(88)80077-2 · External reference
Factors determining the efficacy of alpha-helical antimicrobial peptides
10.2174/0929866033478663 · 2003 · External reference
Optimization of the antimicrobial activity of magainin peptides by modification of charge
10.1016/s0014-5793(01)02648-5 · 2001 · External reference
Effects of net charge and the number of positively charged residues on the biological activity of amphipathic alpha-helical cationic antimicrobial peptides
10.1002/bip.20911 · 2008 · External reference
Amphipathic alpha helical antimicrobial peptides
2001 · External reference
Amphipathic, alpha-helical antimicrobial peptides
10.1002/1097-0282(2000)55:1<4::aid-bip30>3.0.co;2-m · 2000 · External reference
Effect of chain length of cationic model peptides on antibacterial activity
10.1246/bcsj.78.473 · 2005 · External reference
Length effects in antimicrobial peptides of the (RW)n series
10.1128/aac.00828-06 · 2007 · External reference
Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes
10.1021/bi051302m · 2005 · External reference
10.1021/acsinfecdis.6b00045
10.1021/acsinfecdis.6b00045 · External reference
Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I
10.1016/j.bbapap.2003.12.009 · 2004 · External reference
10.1016/j.bbamem.2012.03.015
10.1016/j.bbamem.2012.03.015 · External reference
Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding
10.1021/bi052629q · 2006 · External reference
10.1002/9780470740880.ch10
10.1002/9780470740880.ch10 · External reference
Kinetic constraints on self-assembly into closed supramolecular structures
10.1038/s41598-017-12528-8 · 2017 · External reference
10.1016/b978-0-12-812126-9.00010-9
10.1016/b978-0-12-812126-9.00010-9 · External reference
10.3390/pharmaceutics11040166
10.3390/pharmaceutics11040166 · External reference
10.1002/psc.2788
10.1002/psc.2788 · External reference
Nanostructured antimicrobial peptides: crucial steps of overcoming the bottleneck for clinics
10.3389/fmicb.2021.710199 · 2021 · External reference
10.1039/d1sm00839k
10.1039/d1sm00839k · External reference
10.1038/s41467-017-01447-x
10.1038/s41467-017-01447-x · External reference
10.1021/bm500981y
10.1021/bm500981y · External reference
10.1021/acsami.9b00581
10.1021/acsami.9b00581 · External reference
10.1021/acsabm.9b00172
10.1021/acsabm.9b00172 · External reference
Experimental study on self-assembly of KLD-12 peptide hydrogel and 3-D culture of MSC encapsulated within hydrogel in vitro
10.1007/s11596-009-0424-6 · 2009 · External reference
Designed supramolecular filamentous peptides: balance of nanostructure, cytotoxicity and antimicrobial activity
10.1039/c4cc08808e · 2015 · External reference
10.1016/s0021-9258(18)50079-x
10.1016/s0021-9258(18)50079-x · External reference
10.1038/mi.2014.100
10.1038/mi.2014.100 · External reference
10.1039/c5sc04194e
10.1039/c5sc04194e · External reference
10.1126/science.1218831
10.1126/science.1218831 · External reference
10.1021/ja5057906
10.1021/ja5057906 · External reference
10.1021/acs.accounts.6b00653
10.1021/acs.accounts.6b00653 · External reference
10.1021/acs.biochem.6b01111
10.1021/acs.biochem.6b01111 · External reference
The Human LL-37(17–29) antimicrobial peptide reveals a functional supramolecular structure
10.1038/s41467-020-17736-x · 2020 · External reference
Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9
10.1111/j.1742-4658.2008.06554.x · 2008 · External reference
10.1371/journal.pone.0075528
10.1371/journal.pone.0075528 · External reference
10.1016/j.bpj.2011.01.072
10.1016/j.bpj.2011.01.072 · External reference
10.1039/c4sm00907j
10.1039/c4sm00907j · External reference
Alzheimer's associated beta-amyloid protein inhibits influenza A virus and modulates viral interactions with phagocytes
10.1371/journal.pone.0101364 · 2014 · External reference
The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide
10.1371/journal.pone.0009505 · 2010 · External reference
10.3109/13506120209072440
10.3109/13506120209072440 · External reference
10.1073/pnas.1219059110
10.1073/pnas.1219059110 · External reference
Role of alpha-synuclein in inducing innate and adaptive immunity in Parkinson disease
10.3233/jpd-140491 · 2015 · External reference
Helical antimicrobial peptides assemble into protofibril scaffolds that present ordered dsDNA to TLR9
10.1038/s41467-019-08868-w · 2019 · External reference
10.1038/nature06116
10.1038/nature06116 · External reference
10.1038/nmat4298
10.1038/nmat4298 · External reference
Functional reciprocity of amyloids and antimicrobial peptides: rethinking the role of supramolecular assembly in host defense, immune activation, and inflammation
10.3389/fimmu.2020.01629 · 2020 · External reference
10.1016/j.cis.2016.02.003
10.1016/j.cis.2016.02.003 · External reference
Amyloid-beta peptide protects against microbial infection in mouse and worm models of Alzheimer's disease
10.1126/scitranslmed.aaf1059 · 2016 · External reference
10.1039/c9bm01785b
10.1039/c9bm01785b · External reference
Experimental evolution of resistance to an antimicrobial peptide
2006 · External reference
Bacterial strategies of resistance to antimicrobial peptides
2016 · External reference
10.1128/aac.02434-15
10.1128/aac.02434-15 · External reference
Functional synergy between antimicrobial peptoids and peptides against gram-negative bacteria
10.1128/aac.00578-11 · 2011 · External reference
Mechanism of synergism between antimicrobial peptides magainin 2 and PGLa
10.1021/bi9811617 · 1998 · External reference
10.1038/nrmicro1098
10.1038/nrmicro1098 · External reference
10.1038/s41467-019-12364-6
10.1038/s41467-019-12364-6 · External reference
10.1126/sciadv.aax1946
10.1126/sciadv.aax1946 · External reference
10.1074/jbc.m117.805499
10.1074/jbc.m117.805499 · External reference
