The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides. - Wikidata - awgldk - TriplyDB

The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides.

The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides.

http://www.wikidata.org/entity/Q30165294

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Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance Watching single proteins using engineered nanopores Dimerization is important for the GTPase activity of chloroplast translocon components atToc33 and psToc159 The mitochondrial oxidase assembly protein1 (Oxa1) insertase forms a membrane pore in lipid bilayers.Evidence for glycoprotein transport into complex plastids The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Polyglycine Acts as a Rejection Signal for Protein Transport at the Chloroplast Envelope OEP40, a Regulated Glucose-permeable β-Barrel Solute Channel in the Chloroplast Outer Envelope Membrane.The chloroplast outer envelope protein P39 in Arabidopsis thaliana belongs to the Omp85 protein family.New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways The TpsB translocator HMW1B of haemophilus influenzae forms a large conductance channel.Functional and phylogenetic properties of the pore-forming beta-barrel transporters of the Omp85 family.OEP37 is a new member of the chloroplast outer membrane ion channels.Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore.Evolution of the general protein import pathway of plastids (review).The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains.Interactions of peptides with a protein pore.Prediction of the plant beta-barrel proteome: a case study of the chloroplast outer envelope.Tic32, an essential component in chloroplast biogenesis.Filling the gap, evolutionarily conserved Omp85 in plastids of chromalveolates.Tic20 forms a channel independent of Tic110 in chloroplasts.Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity.A GTP-driven motor moves proteins across the outer envelope of chloroplasts.Applications of biological pores in nanomedicine, sensing, and nanoelectronics Ligand recognition by the TPR domain of the import factor Toc64 from Arabidopsis thaliana.Oep23 forms an ion channel in the chloroplast outer envelope Non-native, N-terminal Hsp70 molecular motor recognition elements in transit peptides support plastid protein translocation.A proteomic analysis of the chromoplasts isolated from sweet orange fruits [Citrus sinensis (L.) Osbeck].The motors of protein import into chloroplasts.The Plastid Outer Envelope - A Highly Dynamic Interface between Plastid and Cytoplasm Single molecule detection of intermediates during botulinum neurotoxin translocation across membranes.Stimulation of transit-peptide release and ATP hydrolysis by a cochaperone during protein import into chloroplasts.Bacterial origin of a mitochondrial outer membrane protein translocase: new perspectives from comparative single channel electrophysiology.Multi-functional roles for the polypeptide transport associated domains of Toc75 in chloroplast protein import Anthrax toxin-induced rupture of artificial lipid bilayer membranes.Factors governing helix formation in peptides confined to carbon nanotubes.

P2860

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P2860

The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides.

http://www.wikidata.org/entity/Q30165294

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2002年の論文

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2002年論文

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2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

The chloroplast protein import ...... raction with transit peptides.

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type

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The chloroplast protein import ...... raction with transit peptides.

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The chloroplast protein import ...... raction with transit peptides.

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S0006-3495(02)75216-8

P1433

Biophysical Journal

P1476

The chloroplast protein import ...... raction with transit peptides.

@en

P2093

Natalia Sveshnikova

http://www.w3.org/2001/XMLSchema#string

Richard Wagner

http://www.w3.org/2001/XMLSchema#string

Roswitha Harrer

http://www.w3.org/2001/XMLSchema#string

Silke C Hinnah

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structures explain functional properties of two E. coli porins

Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment].

Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels.

Detection of likely transmembrane beta strand regions in sequences of mitochondrial pore proteins using the Gibbs sampler.

The structural flexibility of the preferredoxin transit peptide.

Mechanisms of solute transport through outer membrane porins: burning down the house.

Origin of a chloroplast protein importer.

Protein import into chloroplasts.

Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids.

Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis.

P304

899-911

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scholarly article

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10.1016/S0006-3495(02)75216-8

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P433

2

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83

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2002-08-01T00:00:00Z

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11255281

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12124272

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1302194

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