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Protein Science, ISSN 0961-8368, 04/2011, Volume 20, Issue 4, pp. 641 - 655
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the... 
cell penetrating peptides | dynamics | topology | membrane protein | solid‐state NMR | antimicrobial peptides | structure | Solid-state NMR | Membrane protein | Cell penetrating peptides | Dynamics | Antimicrobial peptides | Topology | Structure | SPIN-DIFFUSION NMR | ANTENNAPEDIA HOMEODOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-MAGNETIC-RESONANCE | CELL-PENETRATING PEPTIDES | DEPENDENT K+ CHANNEL | HUMAN IMMUNODEFICIENCY VIRUS | solid-state NMR | HAIRPIN ANTIMICROBIAL PEPTIDE | PRECURSOR LIPID II | HUMAN ALPHA-DEFENSINS | ARGININE-RICH PEPTIDES | Humans | Peptides - genetics | Molecular Sequence Data | Peptides, Cyclic - chemistry | alpha-Defensins - genetics | Peptides, Cyclic - genetics | Antimicrobial Cationic Peptides - genetics | Cell-Penetrating Peptides - chemistry | Potassium Channels, Voltage-Gated - genetics | Amino Acid Sequence | Cell-Penetrating Peptides - genetics | Cations - chemistry | Magnetic Resonance Spectroscopy - methods | Potassium Channels, Voltage-Gated - chemistry | alpha-Defensins - chemistry | Peptides - chemistry | Antimicrobial Cationic Peptides - chemistry | Membrane Proteins - genetics | Models, Molecular | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | Animals | Membrane Proteins - chemistry | Protein Conformation | Lipid Bilayers - chemistry | Peptides | Lipids | Review
Journal Article
Journal of Cellular Physiology, ISSN 0021-9541, 09/2017, Volume 232, Issue 9, pp. 2558 - 2568
Real‐time quantitative reverse transcription‐polymerase chain reaction (qRT‐PCR) analysis showed that AGP extracted from acacia or baobab seeds induced a... 
PRO-INFLAMMATORY CYTOKINES | PHYSIOLOGY | DEPENDENT BIOACTIVITY | CYTO-TOXICITY | ROOT | HUMAN SKIN FIBROBLASTS | POLYSACCHARIDES | HUMAN EPIDERMAL-KERATINOCYTES | ANTIMICROBIAL PEPTIDES | EXPRESSION | PLANT-CELL WALLS | CELL BIOLOGY | Up-Regulation | Immunologic Factors - isolation & purification | Skin - metabolism | Humans | Interleukin-1alpha - metabolism | Dose-Response Relationship, Drug | Mucoproteins - pharmacology | Adansonia - chemistry | Time Factors | Plant Proteins - chemistry | Toll-Like Receptor 6 - genetics | Interleukin-1alpha - genetics | Seeds - chemistry | beta-Defensins - metabolism | Phytotherapy | Real-Time Polymerase Chain Reaction | Acacia - chemistry | Skin - immunology | Plant Proteins - isolation & purification | Toll-Like Receptor 6 - metabolism | Cell Line | Immunologic Factors - chemistry | beta-Defensins - genetics | Plant Proteins - pharmacology | Immunity, Innate - drug effects | Reverse Transcriptase Polymerase Chain Reaction | Mucoproteins - isolation & purification | Keratinocytes - immunology | Keratinocytes - drug effects | Mucoproteins - chemistry | Keratinocytes - metabolism | Protein Conformation | Immunologic Factors - pharmacology | Plants, Medicinal | Skin - drug effects | Proteins | Skin | Seeds | Analysis | Innate immunity | Immunology | Immune response | Index Medicus | Biotechnology | Gametogenesis | Biochemistry, Molecular Biology | Genomics | Cellular Biology | Chemical Sciences | Life Sciences | Phytopathology and phytopharmacy | Plant breeding | Biomolecules | Development Biology | Vegetal Biology | Subcellular Processes | Polymers | Molecular Networks | Molecular biology | Cell Behavior
Journal Article
Journal Article
Journal Article
Amino Acids, ISSN 0939-4451, 10/2012, Volume 43, Issue 4, pp. 1471 - 1483
Salt-bridge interactions between acidic and basic amino acids contribute to the structural stability of proteins and to protein–protein interactions. A... 
Biochemistry, general | Neurobiology | Salt-bridge | Proteolytic stability | Life Sciences | Analytical Chemistry | Crp4 | Life Sciences, general | Proteomics | Biochemical Engineering | Defensin | Cryptdin-4 | Structure | Folding | CHEMICAL-SHIFTS | MAMMALIAN DEFENSINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BETA-DEFENSINS | ANTIMICROBIAL PEPTIDES | DISULFIDE ARRAY | MATRIX METALLOPROTEINASE-7 | AMINO-ACIDS | HOST-DEFENSE | PANETH CELLS | MOUSE CRYPTDIN-4 | Salts | Recombinant Fusion Proteins - pharmacology | Gram-Positive Bacteria - drug effects | Anti-Infective Agents - pharmacology | Glutamic Acid - genetics | Molecular Sequence Data | alpha-Defensins - genetics | Proteolysis | Anti-Infective Agents - chemistry | Arginine - genetics | Protein Stability | Gram-Positive Bacteria - growth & development | Amino Acid Sequence | alpha-Defensins - chemistry | Magnetic Resonance Spectroscopy | Microbial Viability - drug effects | Protein Structure, Secondary | Recombinant Fusion Proteins - chemistry | Arginine - chemistry | alpha-Defensins - pharmacology | Matrix Metalloproteinase 7 - chemistry | Gram-Negative Bacteria - drug effects | Paneth Cells - physiology | Animals | Gram-Negative Bacteria - growth & development | Hydrophobic and Hydrophilic Interactions | Recombinant Fusion Proteins - genetics | Mice | Mutation | Trypsin - chemistry | Glutamic Acid - chemistry | Backbone | Degradation | Microorganisms | Stability | Peptides | Amino acids | Bacteria | Flexibility | Biokemi | Biochemistry | Chemical Sciences | Naturvetenskap | Kemi | Natural Sciences | Organisk kemi | Organic Chemistry
Journal Article
Biophysical Journal, ISSN 0006-3495, 2009, Volume 97, Issue 8, pp. 2250 - 2257
The oligo-acyl-lysyl, C K- , is comprised of only three Lys residues. Despite its small size, it exhibits potent bacteriostatic activity against Gram-positive... 
BIOPHYSICS | MECHANISM | LYSINE OLIGOMERS | ESCHERICHIA-COLI | MODE | LIPOPOLYSACCHARIDE | DEFENSINS | ANTIMICROBIAL PEPTIDES | Escherichia coli - drug effects | Peptidoglycan - chemistry | DNA, Bacterial - chemistry | Teichoic Acids - chemistry | Periplasm - drug effects | Cell Membrane - chemistry | Dose-Response Relationship, Drug | Cell Wall - drug effects | Anti-Bacterial Agents - chemistry | Edetic Acid - pharmacology | Periplasm - chemistry | Cell Membrane - drug effects | Dipeptides - pharmacology | Chelating Agents - chemistry | Membranes, Artificial | Cell Wall - chemistry | Chelating Agents - pharmacology | Permeability | Dipeptides - chemistry | Escherichia coli - chemistry | Static Electricity | Staphylococcus aureus - chemistry | Edetic Acid - chemistry | Models, Biological | Peptidoglycan - drug effects | Anti-Bacterial Agents - pharmacology | Lipopolysaccharides - chemistry | Staphylococcus aureus - drug effects | Binding | Membranes | Bacteria | Lipids | Position (location) | Adhesion | Electrostatics | Walls | Contact | CAC, critical aggregation concentration | DSC, differential scanning calorimetry | ONPG, ortho-nitrophenyl-β-D-galactoside | ITC, isothermal titration calorimetry | LTA, lipoteichoic acid | CL, cardiolipin | ANTS, 8-aminonaphthalene-1,3,6-trisulfonic acid | PE, phosphatidylethanolamine | DOPG, dioleoyl phosphatidylglycerol | OAK, oligo-acyl-lysyl | MIC, minimal inhibitory concentration | TOCL, tetraoleoyl cardiolipin | LUV, large unilamellar vesicle | PG, phosphatidylglycerol | POPE, 1-palmitoyl-2-oleoylphosphatidylethanolamine | PBS, phosphate-buffered saline | DPX, p-xylene-bis-pyridinium bromide | LB, Luria-Bertani broth | TSB, tryptic soy broth | CFU, colony-forming unit | Membrane | LPS, lipopolysaccharide | ONP, ortho-nitrophenyl | SPR, surface plasmon resonance
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 03/2016, Volume 291, Issue 13, pp. 7097 - 7106
The structural similarity between defensins and scorpion neurotoxins suggests that they might have evolved from a common ancestor. However, there is no direct... 
VENOM | PORE REGION | bacteria | TOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | structure-function | KV1.3 CHANNEL | STRUCTURAL BASIS | FUNGAL DEFENSIN | defensin | INSECT DEFENSINS | neurotoxin | potassium channel | MESOBUTHUS-MARTENSII | PROTEOMIC ANALYSIS | K+ CHANNELS | Kv1.2 Potassium Channel - antagonists & inhibitors | Humans | Micrococcus luteus - growth & development | Potassium Channel Blockers - metabolism | Bacillus subtilis - growth & development | Defensins - pharmacology | Kv1.3 Potassium Channel - metabolism | Potassium Channel Blockers - pharmacology | Kv1.1 Potassium Channel - genetics | Amino Acid Sequence | Gene Expression | Methicillin-Resistant Staphylococcus aureus - drug effects | Models, Molecular | Recombinant Proteins - chemistry | Methicillin-Resistant Staphylococcus aureus - growth & development | Scorpion Venoms - chemistry | Kv1.2 Potassium Channel - metabolism | Neurotoxins - metabolism | Anti-Bacterial Agents - pharmacology | Mice | Scorpion Venoms - biosynthesis | Potassium Channel Blockers - chemistry | Defensins - metabolism | Defensins - genetics | Kv1.1 Potassium Channel - metabolism | Molecular Sequence Data | Neurotoxins - genetics | Structure-Activity Relationship | Defensins - chemistry | Kv1.3 Potassium Channel - genetics | Micrococcus luteus - drug effects | Scorpions - physiology | Anti-Bacterial Agents - chemistry | Protein Interaction Domains and Motifs | Recombinant Proteins - metabolism | Neurotoxins - chemistry | Protein Structure, Secondary | Kv1.1 Potassium Channel - antagonists & inhibitors | Anti-Bacterial Agents - metabolism | Scorpions - chemistry | Recombinant Proteins - genetics | Kv1.3 Potassium Channel - antagonists & inhibitors | Recombinant Proteins - pharmacology | Neurotoxins - pharmacology | Kv1.2 Potassium Channel - genetics | Sequence Alignment | Animals | Structural Homology, Protein | Staphylococcus aureus - drug effects | Staphylococcus aureus - growth & development | Bacillus subtilis - drug effects | Index Medicus | Cell Biology
Journal Article