Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid. - Wikidata - awgldk - TriplyDB

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

http://www.wikidata.org/entity/Q46023393

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Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cells VIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against Stress Release of proteins from intact chloroplasts induced by reactive oxygen species during biotic and abiotic stress.The puzzle of chloroplast vesicle transport - involvement of GTPases.Vipp1 is essential for the biogenesis of Photosystem I but not thylakoid membranes in Synechococcus sp. PCC 7002.New putative chloroplast vesicle transport components and cargo proteins revealed using a bioinformatics approach: an Arabidopsis model Two Novel Vesicle-Inducing Proteins in Plastids 1 Genes Cloned and Characterized in Triticum urartu.Structure and dynamics of thylakoids in land plants.Membrane remodelling in bacteria.Revisiting the photosystem II repair cycle A role of VIPP1 as a dynamic structure within thylakoid centers as sites of photosystem biogenesis?Possible function of VIPP1 in thylakoids: protection but not formation?Localisation and interactions of the Vipp1 protein in cyanobacteria.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.Chloroplast-targeted Hsp90 plays essential roles in plastid development and embryogenesis in Arabidopsis possibly linking with VIPP1.In vitro reconstitution of co-translational D1 insertion reveals a role of the cpSec-Alb3 translocase and Vipp1 in photosystem II biogenesis.The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.Proteome analysis of cytoplasmatic and plastidic β-carotene lipid droplets in Dunaliella bardawil.Proteomic evidence for genetic epistasis: ClpR4 mutations switch leaf variegation to virescence in Arabidopsis.VIPP1 involved in chloroplast membrane integrity has GTPase activity in vitro.IM30 triggers membrane fusion in cyanobacteria and chloroplasts

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P2860

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

http://www.wikidata.org/entity/Q46023393

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh-hant

name

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@en

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@nl

type

label

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@en

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@nl

prefLabel

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@en

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@nl

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J.1365-313X.2012.05020.X

P1433

The Plant Journal

P1476

Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.

@en

P2093

Shari M Lo

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

Steven M Theg

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P2860

Vipp1 deletion mutant of Synechocystis: a connection between bacterial phage shock and thylakoid biogenesis?

VIPP1, a nuclear gene of Arabidopsis thaliana essential for thylakoid membrane formation

COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS

Tat subunit stoichiometry in Arabidopsis thaliana challenges the proposed function of TatA as the translocation pore.

A stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.

Unassisted membrane insertion as the initial step in DeltapH/Tat-dependent protein transport.

In vivo transport of folded EGFP by the DeltapH/TAT-dependent pathway in chloroplasts of Arabidopsis thaliana.

Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli.

Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway.

Multiple precursor proteins bind individual Tat receptor complexes and are collectively transported

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656-668

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scholarly article

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10.1111/J.1365-313X.2012.05020.X

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4

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71

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2012-06-18T00:00:00Z

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22487220

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