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Xia Li
Researcher at University of Nebraska Medical Center
Publications - 10
Citations - 2850
Xia Li is an academic researcher from University of Nebraska Medical Center. The author has contributed to research in topics: Peptide & Fusion protein. The author has an hindex of 10, co-authored 10 publications receiving 2310 citations. Previous affiliations of Xia Li include Eppley Institute for Research in Cancer and Allied Diseases.
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APD3: the antimicrobial peptide database as a tool for research and education
Guangshun Wang,Xia Li,Zhe Wang +2 more
TL;DR: Newly annotated are AMPs with antibiofilm, antimalarial, anti-protist, insecticidal, spermicidal, chemotactic, wound healing, antioxidant and protease inhibiting properties and various database applications in research and education are summarized.
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APD2: the updated antimicrobial peptide database and its application in peptide design
Guangshun Wang,Xia Li,Zhe Wang +2 more
TL;DR: Using frequently occurring residues, database-aided peptide design in different ways is demonstrated, and GLK-19 showed a higher activity against Escherichia coli than human LL-37 and Leu, Ala, Gly and Lys in amphibian peptides.
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Solution Structures of Human LL-37 Fragments and NMR-Based Identification of a Minimal Membrane-Targeting Antimicrobial and Anticancer Region
TL;DR: It is proposed that hydrophobic defects in the new amphipathic structure of the D-peptide provide a structural basis for the improvement in cell selectivity of the LL-37 fragment.
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Correlation of Three-dimensional Structures with the Antibacterial Activity of a Group of Peptides Designed Based on a Nontoxic Bacterial Membrane Anchor
Guangshun Wang,Yifeng Li,Xia Li +2 more
TL;DR: 31P solid state NMR spectroscopy of lipid bilayers showed that the extent of lipid vesicle disruption by these peptides is proportional to their membrane perturbation potential, which is defined by interfacial hydrophobic patches and basic residues in the case of cationic peptides.
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Cloning, expression, isotope labeling, and purification of human antimicrobial peptide LL-37 in Escherichia coli for NMR studies.
Yifeng Li,Xia Li,Guangshun Wang +2 more
TL;DR: The successful application to the expression of the 66-residue cytoplasmic tail of human MUC1 indicates that the system can be applied to other peptides as well, and indicates a broader application of formic acid than cyanogen bromide in cleaving fusion proteins.