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Construction and bacteriostatic effect analyses of a recombinant thermostable Newcastle disease virus expressing cecropin AD.
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Hubei Provincial Key Laboratory of Animal Pathogenic Microbiology, Institute of Animal Husbandry and Veterinary, Hubei Academy of Agricultural Sciences, Wuhan 430064, China; Key Laboratory of Prevention and Control Agents for Animal Bacteriosis (Ministry of Agriculture and Rural Affairs), Institute of Animal Husbandry and Veterinary, Hubei Academy of Agricultural Sciences, Wuhan 430064, China. Electronic address:
Cecropin AD (CAD), a hybrid antimicrobial peptide composed of the first 11 residues of cecropin A and last 26 residues of cecropin D, is a promising antibiotic candidate. Therefore, an efficient and convenient method for producing CAD is necessary for commercial applications. The Newcastle disease virus (NDV) has been widely used as a platform for gene delivery and exogenous protein expression.
View Article and Find Full Text PDFStructure-Function Relationship of the β-Hairpin of HB27 Laccase.
Int J Mol Sci
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Departamento de Micro y Nanotecnologías, Instituto de Ciencias Aplicadas y Tecnología, Universidad Nacional Autónoma de México, Cto. Exterior S/N, C.U., Coyoacán, Ciudad de México C.P. 04510, Mexico.
Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) and one with a partially modified β-hairpin (P1Tth-Lac). Enzymatic activity was assayed with different substrates with and without copper.
View Article and Find Full Text PDFProbing the Dual Role of Ca in the LH1-RC Complex by Constructing and Analyzing Ca-Bound and Ca-Free LH1 Complexes.
Biomolecules
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Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
The genome of the mildly thermophilic hot spring purple sulfur bacterium, (.) , contains a multigene family that encodes a series of α- and β-polypeptides, collectively forming a heterogeneous light-harvesting 1 (LH1) complex. The LH1, therefore, offers a unique model for studying an intermediate phenotype between phototrophic thermophilic and mesophilic bacteria, particularly regarding their LH1 transition and moderately enhanced thermal stability.
View Article and Find Full Text PDFCharacterization of the second type of tubuliform spidroin (TuSp1 variant 2) elucidates the essential role of cysteine within the repetitive domain in liquid-liquid phase separation-mediated silk formation and the mechanical properties of silk fibers.
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Department of Ophthalmology, The Quzhou Affiliated Hospital of Wenzhou Medical University, Quzhou People's Hospital, Quzhou, Zhejiang 324000, China; Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou, Zhejiang 325000, China. Electronic address:
Orb-weaver spiders utilize morphologically differentiated abdominal glands to produce up to seven types of silks throughout their life cycles. Tubuliform silk is unique as it serves to protect developing embryos and hatchlings. However, our current understanding of the relationship between structure and function of tubuliform silk protein remains limited.
View Article and Find Full Text PDFSalidroside production through cascade biocatalysis with a thermostability-enhanced UDP-glycosyltransferase.
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School of Marine Sciences, Sun Yat-Sen University, Zhuhai 519080, China. Electronic address:
Salidroside is a phenylpropanoid glycoside with wide applications in the food, pharmaceutical, and cosmetic industries; however, the plant genus Rhodiola, the natural source of salidroside, has slow growth and limited distribution. In this study, we designed a novel six-enzyme biocatalytic cascade for the efficient production of salidroside, utilizing cost-effective bio-based L-Tyrosine as the starting material. A preliminary analysis revealed that the poor thermostability of the Bacillus licheniformis UDP-glycosyltransferase (EC 2.
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