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PLoS ONE, ISSN 1932-6203, 12/2013, Volume 8, Issue 12, pp. e84112 - e84112
The avian eggshell membranes are essential elements in the fabrication of the calcified shell as a defense against bacterial penetration. Ovocalyxin-36... 
GRAM-POSITIVE BACTERIA | PSEUDOMONAS-AERUGINOSA INFECTION | LIPOPOLYSACCHARIDE-BINDING PROTEIN | MULTIDISCIPLINARY SCIENCES | NEGATIVE BACTERIA | FUNCTIONAL VARIANT | TERMINAL FRAGMENT | PROTEOMIC ANALYSIS | BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN | HEN EGG-WHITE | STATISTICAL-MODEL | Egg Proteins - metabolism | Anti-Infective Agents - isolation & purification | Membrane Glycoproteins - metabolism | Anti-Infective Agents - metabolism | Lipopolysaccharides - metabolism | Acute-Phase Proteins - genetics | Antimicrobial Cationic Peptides - metabolism | Blood Proteins - metabolism | Tandem Mass Spectrometry | Blood Proteins - genetics | Blood Proteins - isolation & purification | Teichoic Acids - metabolism | Chromatography, Liquid | Cell Membrane - metabolism | Acute-Phase Proteins - isolation & purification | Antimicrobial Cationic Peptides - genetics | Bacterial Infections - microbiology | Membrane Glycoproteins - isolation & purification | Enzyme-Linked Immunosorbent Assay | Acute-Phase Proteins - metabolism | Blotting, Western | Membrane Glycoproteins - genetics | Carrier Proteins - genetics | Bacterial Infections - prevention & control | Animals | Antimicrobial Cationic Peptides - isolation & purification | Carrier Proteins - metabolism | Carrier Proteins - isolation & purification | Chickens | Polymorphism, Single Nucleotide - genetics | Bacteria - pathogenicity | Egg Proteins - isolation & purification | Egg Proteins - genetics | Bacterial Infections - metabolism | Single nucleotide polymorphisms | Chromosomes | Mitogens | Escherichia coli | Organic acids | Protein binding | Membranes | Egg shells | Protein purification | Serine | Lung | Lipoteichoic acid | Membrane permeability | Proline | Homology | Single-nucleotide polymorphism | Phosphatase | Eggs | Molecular weight | Lipopolysaccharides | Proteins | Fabrication | Anion exchange | Reproduction | Breeding success | Bacteria | Product safety | Lipopolysaccharide-binding protein | Amino acid sequence | Cation exchanging | Pattern recognition | Permeability | Mammals | Epithelium | Membrane proteins | Anion exchanging | Calcification | Sepsis | BPI protein | Palate | Food safety | Index Medicus
Journal Article
Small, ISSN 1613-6810, 05/2018, Volume 14, Issue 19, pp. 1870087 - n/a
In article number 1704020 , Richard W. Pickersgill and co‐workers uncover the orientation of shell proteins within synthetic protein nanotubes and bacterial... 
protein nanotubes | bacterial microcompartment shell proteins | transmission electron microscopy | self‐assembly | Proteins | Nanotubes | Disks
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 3, pp. e18187 - e18187
Under the shell of a chicken egg are two opposed proteinaceous disulfide-rich membranes. They are fabricated in the avian oviduct using fibers formed from... 
DICTYOSTELIUM | MATRIX | SULFHYDRYL OXIDASE | EGG-WHITE | MINERALIZATION | BIOLOGY | CHEMICAL-SHIFT | BOND FORMATION | KERATIN-ASSOCIATED PROTEINS | IDENTIFICATION | GENE DOMAIN | Disulfides - metabolism | Conserved Sequence - genetics | Membranes | Molecular Sequence Data | Substrate Specificity | Avian Proteins - chemistry | Chickens - metabolism | Egg Shell - cytology | Repetitive Sequences, Amino Acid | Peptides - metabolism | Lizards | Cysteine - metabolism | Membrane Proteins - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Avian Proteins - metabolism | Membrane Proteins - isolation & purification | Finches | Magnetic Resonance Spectroscopy | Peptides - chemistry | Dictyosteliida - metabolism | Egg Shell - metabolism | Amino Acid Motifs | Animals | Membrane Proteins - chemistry | Avian Proteins - isolation & purification | Microscopy, Fluorescence | Evolution, Molecular | Proteins | Cysteine | Nucleotide sequencing | Cystine | Protein binding | DNA sequencing | Residues | Nuclear magnetic resonance--NMR | Peptides | Egg shells | Modules | Escherichia coli | Biochemistry | Experiments | Biopolymers | Alkylation | Eggs | Gene sequencing | Fibers | Fragmentation | Keratin | Protein composition | Epidermal growth factor | Mineralization | Proteolysis | Slime molds | Chemical bonds | Oviduct | Coat protein | Deoxyribonucleic acid--DNA | Disulfide bonds | Nucleotide sequence | Crosslinking | C-Terminus | Permeability | Slime | Chemistry | Acids | Microscopy | Lysine | Collagen | Morphology | Reductive alkylation | Index Medicus | Deoxyribonucleic acid | Nuclear magnetic resonance | NMR | DNA
Journal Article
Angewandte Chemie International Edition, ISSN 1433-7851, 09/2016, Volume 55, Issue 38, pp. 11668 - 11672
Journal Article
Particle & Particle Systems Characterization, ISSN 0934-0866, 12/2017, Volume 34, Issue 12, pp. 1770040 - n/a
The adsorption of bovine serum albumin on mixtures of gold nanoparticles with diameters ranging from 20 to 100 nm can be concurrently detected using... 
bovine serum albumin shell | competitive adsorption | differential centrifugal sedimentation | gold nanoparticles | Nanoparticles | Proteins | Gold | Serum albumin | Protein adsorption | Sedimentation | Sedimentation & deposition
Journal Article
by Bao, J and Chen, W and Liu, TT and Zhu, YL and Jin, PY and Wang, LY and Liu, JF and Wei, YG and Li, YD
ACS NANO, ISSN 1936-0851, 11/2007, Volume 1, Issue 4, pp. 293 - 298
In this article, we report the synthesis of bifunctional Au-Fe3O4 nanoparticles that are formed by chemical bond linkage. Due to the introduction of Au... 
GOLD NANOPARTICLES | protein separation | SHELL | magnetic nanomaterials | MATERIALS SCIENCE, MULTIDISCIPLINARY | CHEMISTRY, PHYSICAL | NANOSCIENCE & NANOTECHNOLOGY | MAGNETIC NANOCRYSTALS | POLYNUCLEOTIDES | CANCER | CHEMISTRY, MULTIDISCIPLINARY | PROBES | bifunctional nanoparticles | DNA | NANOTECHNOLOGY
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2012, Volume 109, Issue 2, pp. 478 - 483
Journal Article