Northeast red beans produce a thermostable and pH-stable defensin-like peptide with potent antifungal activity. - Wikidata - wikimedia - TriplyDB

Northeast red beans produce a thermostable and pH-stable defensin-like peptide with potent antifungal activity.

Northeast red beans produce a thermostable and pH-stable defensin-like peptide with potent antifungal activity.

http://www.wikidata.org/entity/Q34537492

about

Synergistic Activity of the Plant Defensin HsAFP1 and Caspofungin against Candida albicans Biofilms and Planktonic Cultures Study of the Antimicrobial Activity of Tilapia Piscidin 3 (TP3) and TP4 and Their Effects on Immune Functions in Hybrid Tilapia (Oreochromis spp.).Defensins: antifungal lessons from eukaryotes Plant antifungal proteins and their applications in agriculture.Convergent evolution of defensin sequence, structure and function.Amino Acid, Organic Acid, and Sugar Profiles of 3 Dry Bean (Phaseolus vulgaris L.) Varieties.Polyphenol-Rich Dry Common Beans (Phaseolus vulgaris L.) and Their Health Benefits.Peptides: Production, bioactivity, functionality, and applications.Impact of commercial precooking of common bean (Phaseolus vulgaris) on the generation of peptides, after pepsin-pancreatin hydrolysis, capable to inhibit dipeptidyl peptidase-IV.

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P2860

Northeast red beans produce a thermostable and pH-stable defensin-like peptide with potent antifungal activity.

http://www.wikidata.org/entity/Q34537492

description

2013 nî lūn-bûn

@nan

2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հուլիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

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Cell Biochemistry and Biophysics

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Tzi Bun Ng

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Yau Sang Chan

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P2860

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Human immunodeficiency virus type 1 (HIV-1) inhibition, DNA-binding, RNA-binding, and ribosome inactivation activities in the N-terminal segments of the plant anti-HIV protein GAP31

Method for Determination of the Amino Acid Sequence in Peptides

Purification, characterization, and sequencing of a novel type of antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat (Fagopyrum esculentum Moench.).

Vv-AMP1, a ripening induced peptide from Vitis vinifera shows strong antifungal activity.

A new family of small (5 kDa) protein inhibitors of insect alpha-amylases from seeds or sorghum (Sorghum bicolar (L) Moench) have sequence homologies with wheat gamma-purothionins.

Analysis of common bean expressed sequence tags identifies sulfur metabolic pathways active in seed and sulfur-rich proteins highly expressed in the absence of phaseolin and major lectins.

Purification, crystallization and X-ray characterization of a Kunitz-type trypsin inhibitor protein from the seeds of chickpea (Cicer arietinum).

Interactions of antifungal plant defensins with fungal membrane components.

Rat recombinant β-defensin 22 is a heparin-binding protein with antimicrobial activity.

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s12013-012-9508-1

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637-648

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scholarly article

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10.1007/S12013-012-9508-1

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3

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66

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