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Ping Chen

Researcher at University of Alabama at Birmingham

Publications -  15
Citations -  1355

Ping Chen is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Peptide sequence & Lantibiotics. The author has an hindex of 12, co-authored 15 publications receiving 1316 citations.

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Identification of the Immunodominant Protein and Other Proteins of the Bacillus anthracis Exosporium

TL;DR: Using a large panel of unique antispore monoclonal antibodies, it is demonstrated that BclA is the immunodominant antigen on the B. anthracis spore surface and showed that the B clA protein and not a carbohydrate constituent directs the dominant immune response.
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The Group I Strain of Streptococcus mutans, UA140, Produces Both the Lantibiotic Mutacin I and a Nonlantibiotic Bacteriocin, Mutacin IV

TL;DR: Production of mutacins I and IV by UA140 appears to be regulated by different mechanisms under different physiological conditions, and the significance of producing two mutacin by one strain under different conditions and the implication of this property in terms of the ecology of S. mutans in the oral cavity are discussed.
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Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium.

TL;DR: This study demonstrated that two O-linked oligosaccharides are released from spore- and exosporium-associated BclA by hydrazinolysis, and determined that the structure of the tetrasaccharide is 2-O-methyl-4-(3-hydroxy-3-methylbutamido)-4,6-dideoxy-β-d-glucopyranosyl-(1→3)-α-l-rhamn
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Purification of Mutacin III from Group III Streptococcus mutans UA787 and Genetic Analyses of Mutacin III Biosynthesis Genes

TL;DR: The cloned and sequenced the mutacin III biosynthesis gene locus from a group III strain of S. mutans, UA787, consistent with the supposition that mutac in III has posttranslational modifications similar to those of the lantibiotic epidermin.
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Orientation within the Exosporium and Structural Stability of the Collagen-Like Glycoprotein BclA of Bacillus anthracis

TL;DR: It is shown that recombinant BclA, encoded by the B. anthracis Sterne strain and synthesized in Escherichia coli, forms a collagen-like triple helix as judged by collagenase sensitivity and circular dichroism spectroscopy, and observed that CTD trimers are resistant to many proteases and readily form large crystalline sheets.