The structural flexibility of the preferredoxin transit peptide.
about
Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathwayThe POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides.Identification of protein N-termini in Cyanophora paradoxa cyanelles: transit peptide composition and sequence determinants for precursor maturation.Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I.The N-terminal portion of the preToc75 transit peptide interacts with membrane lipids and inhibits binding and import of precursor proteins into isolated chloroplasts.The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domainsLet's talk about...chloroplast import.Plasmodium falciparum apicoplast transit peptides are unstructured in vitro and during apicoplast import.Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions.Sequence Motifs in Transit Peptides Act as Independent Functional Units and Can Be Transferred to New Sequence Contexts.2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensitive channel MscSRole of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5.Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata.Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4.Fidelity of targeting to chloroplasts is not affected by removal of the phosphorylation site from the transit peptide.Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5.Differential transit peptide recognition during preprotein binding and translocation into flowering plant plastids.Arabidopsis nuclear-encoded plastid transit peptides contain multiple sequence subgroups with distinctive chloroplast-targeting sequence motifs.Identification of a Hsp70 recognition domain within the rubisco small subunit transit peptide.
P2860
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P2860
The structural flexibility of the preferredoxin transit peptide.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The structural flexibility of the preferredoxin transit peptide.
@ast
The structural flexibility of the preferredoxin transit peptide.
@en
type
label
The structural flexibility of the preferredoxin transit peptide.
@ast
The structural flexibility of the preferredoxin transit peptide.
@en
prefLabel
The structural flexibility of the preferredoxin transit peptide.
@ast
The structural flexibility of the preferredoxin transit peptide.
@en
P2093
P2860
P1433
P1476
The structural flexibility of the preferredoxin transit peptide.
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(99)00653-5
P407
P577
1999-06-01T00:00:00Z