article Open AccessTop 1% cited
Toroidal pores formed by antimicrobial peptides show significant disorder
Biochimica et Biophysica Acta (BBA) - Biomembranes · 2008 · Vol. 1778(10) · pp. 2308–2317
Durba Sengupta(University of Groningen)Hari Leontiadou(University of Groningen)Alan E. Mark(The University of Queensland)Siewert J. Marrink✉(University of Groningen)
Antimicrobial Peptides and ActivitiesLipid Membrane Structure and BehaviorBiochemical and Structural CharacterizationMelittinPeptideMembraneBiophysicsAntimicrobial peptidesTransmembrane proteinLipid bilayerChemistryBilayerDipalmitoylphosphatidylcholine
MeSH terms
Anti-Infective AgentsComputer SimulationLipid BilayersMelittenMembrane FluidityMembrane LipidsMolecular ConformationThermodynamics1,2-DipalmitoylphosphatidylcholineAntimicrobial Cationic Peptides
Funding
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
Citations
557
FWCI
16.62
field-weighted impact
References
66
Percentile
100%
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References
Detergent-like actions of linear amphipathic cationic antimicrobial peptides
Biochimica et Biophysica Acta (BBA) - Biomembranes · 2006 · 585 citations
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Nature Reviews Microbiology · 2005 · 5,673 citations
Molecular dynamics with coupling to an external bath
The Journal of Chemical Physics · 1984 · 30,535 citations
LINCS: A linear constraint solver for molecular simulations
Journal of Computational Chemistry · 1997 · 16,756 citations
Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores
Biophysical Journal · 2001 · 1,091 citations
GROMACS: Fast, flexible, and free
Journal of Computational Chemistry · 2005 · 18,562 citations
Peptide Antibiotics
Antimicrobial Agents and Chemotherapy · 1999 · 1,169 citations
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