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Journal Article
Indian Journal of Urology, ISSN 0970-1591, 01/2018, Volume 34, Issue 1, pp. 56 - 61
Sacral agenesis (SA) is a caudal regression anomaly that can cause neurogenic bladder but is not generally recognized as high risk. We studied the clinical... 
Urologic diseases | Caudal regression syndrome | Research | Health risk assessment | Analysis | Risk factors | Spina bifida | Fecal incontinence | Ultrasonic imaging | Nephrology | Nuclear magnetic resonance--NMR | Compliance | Bladder | Spinal cord injuries | Urogenital system | Urology | Original
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2013, Volume 8, Issue 12, p. e82485
MtDef4 is a 47-amino acid cysteine-rich evolutionary conserved defensin from a model legume Medicago truncatula. It is an apoplast-localized plant defense... 
HUMAN IMMUNODEFICIENCY VIRUS | PISUM-SATIVUM DEFENSIN-1 | GROWTH-INHIBITION | EFFECTOR PROTEINS | MULTIDISCIPLINARY SCIENCES | CHEMICAL-SHIFT | ANTIMICROBIAL PEPTIDES | FUSARIUM-GRAMINEARUM | DAHLIA DAHLIA-MERCKII | 3-DIMENSIONAL SOLUTION STRUCTURE | ANIMAL HOST-CELLS | Antifungal Agents - pharmacology | Amino Acid Sequence | Defensins - metabolism | Plant Proteins - pharmacology | Amino Acids - chemistry | Models, Molecular | Molecular Sequence Data | Fusarium - drug effects | Antifungal Agents - chemistry | Defensins - chemistry | Medicago truncatula - chemistry | Medicago truncatula - metabolism | Static Electricity | Amino Acid Motifs | Sequence Alignment | Fusarium - physiology | Plant Proteins - chemistry | Defensins - pharmacology | Antifungal Agents - metabolism | Protein Binding | Protein Conformation | Phosphatidic Acids - metabolism | Plant Proteins - metabolism | Fusarium - ultrastructure | Legumes | Cysteine | Antifungal agents | Mimosaceae | Proteins | Fungi | Membrane lipids | Defense industry | Beans | Analysis | Physiological aspects | Blood lipids | Protein binding | Plasma | Membranes | Fungicides | Biosynthesis | Phospholipids | Recruitment | Antifungal activity | Evolutionary conservation | Fusarium | Chemical bonds | Plant sciences | Labeling | Phosphatidic acid | Translocation | Automation | Fusarium graminearum | Amino acid sequence | Alfalfa | Apoplast | Studies | Signaling | Acids | Internalization | Cytoplasm | Structure-function relationships
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 16157 - 13
Defensins are cysteine-rich cationic antimicrobial peptides contributing to the innate immunity in plants. A unique gene encoding a highly cationic bi-domain... 
Fungi | Phosphatidylinositol | Antifungal activity | Reactive oxygen species | Oligomerization | Defensins | Antimicrobial peptides | Amino acids | Innate immunity | Phospholipids | Cationic antimicrobial peptides
Journal Article
Annals of Emergency Medicine, ISSN 0196-0644, 10/2018, Volume 72, Issue 4, pp. S70 - S71
Journal Article
PHYTOPATHOLOGY, ISSN 0031-949X, 03/2019, Volume 109, Issue 3, pp. 402 - 408
Plant defensins are small, cysteine-rich antimicrobial peptides. These peptides have previously been shown to primarily inhibit the growth of fungal plant... 
SEEDS | DETERMINES | FUNGAL | MODE | CROWN ROT | ANTIMICROBIAL PEPTIDES | INSECT | ALFALFA | PLANT SCIENCES
Journal Article
Frontiers in Microbiology, ISSN 1664-302X, 05/2018, Volume 9, Issue MAY, p. 934
Journal Article
Journal of Visualized Experiments, ISSN 1940-087X, 09/2017, Volume 2017, Issue 130
Small cysteine-rich defensins are one of the largest groups of host defense peptides present in all plants. Many plant defensins exhibit potent in vitro... 
Antifungal | Fusarium graminearum | Mechanism of action (MOA) | Plant defensin | Internalization | Subcellular localization | Live-cell imaging | Neurospora crassa | NAD1 | subcellular localization | MULTIDISCIPLINARY SCIENCES | MECHANISMS | plant defensin | INSECT | mechanism of action (MOA) | antifungal | CANDIDA-ALBICANS | PEPTIDES | internalization | NEUROSPORA-CRASSA
Journal Article