Small surfactant-like peptides can drive soluble proteins into active aggregates.
about
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Screening and identification of genetic loci involved in producing more/denser inclusion bodies in Escherichia coli.Formation of active inclusion bodies induced by hydrophobic self-assembling peptide GFIL8Dissecting the contribution of Staphylococcus aureus α-phenol-soluble modulins to biofilm amyloid structure.Engineering protein self-assembling in protein-based nanomedicines for drug delivery and gene therapy.A cleavable self-assembling tag strategy for preparing proteins and peptides with an authentic N-terminus.Aggregating tags for column-free protein purification.The promises and challenges of fusion constructs in protein biochemistry and enzymology.Visible-Light Microscopic Discovery of Up to 150 μm Long Helical Amyloid Fibrils Built of the Dodecapeptide H-(Val-Ala-Leu)4 -OH and of Decapeptides Derived from Insulin.A nanostructured bacterial bioscaffold for the sustained bottom-up delivery of protein drugs.Extracellular DNA facilitates the formation of functional amyloids in Staphylococcus aureus biofilms.Application of an E. coli signal sequence as a versatile inclusion body tagPackaging protein drugs as bacterial inclusion bodies for therapeutic applicationsWhy and how protein aggregation has to be studied in vivo.Self-assembling amphipathic alpha-helical peptides induce the formation of active protein aggregates in vivo.Reassessment of inclusion body-based production as a versatile opportunity for difficult-to-express recombinant proteins.Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli.Enhanced production of leech hyaluronidase by optimizing secretion and cultivation in Pichia pastoris.Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.Recombinant expression of antimicrobial peptides using a novel self-cleaving aggregation tag in Escherichia coli.Direct production of a genetically-encoded immobilized biodiesel catalystMagnetization of active inclusion bodies: comparison with centrifugation in repetitive biotransformationsFusion of a Coiled-Coil Domain Facilitates the High-Level Production of Catalytically Active Enzyme Inclusion Bodies
P2860
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P2860
Small surfactant-like peptides can drive soluble proteins into active aggregates.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@ast
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@en
type
label
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@ast
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@en
prefLabel
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@ast
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@en
P2093
P2860
P356
P1476
Small surfactant-like peptides can drive soluble proteins into active aggregates.
@en
P2093
Bihong Zhou
Xian-En Zhang
Zhanglin Lin
P2860
P2888
P356
10.1186/1475-2859-11-10
P577
2012-01-18T00:00:00Z
P5875
P6179
1001771196