Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
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VIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against StressThe 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.A toolset of aequorin expression vectors for in planta studies of subcellular calcium concentrations in Arabidopsis thaliana.Branched-chain aminotransferase4 is part of the chain elongation pathway in the biosynthesis of methionine-derived glucosinolates in Arabidopsis.Subcellular localization and functions of the barley stem rust resistance receptor-like serine/threonine-specific protein kinase Rpg1.New putative chloroplast vesicle transport components and cargo proteins revealed using a bioinformatics approach: an Arabidopsis modelTwo Novel Vesicle-Inducing Proteins in Plastids 1 Genes Cloned and Characterized in Triticum urartu.Structure and dynamics of thylakoids in land plants.A role of VIPP1 as a dynamic structure within thylakoid centers as sites of photosystem biogenesis?Protection of Chloroplast Membranes by VIPP1 Rescues Aberrant Seedling Development in Arabidopsis nyc1 Mutant.Evaluating the role of phage-shock protein A in Burkholderia pseudomallei.The Tat system for membrane translocation of folded proteins recruits the membrane-stabilizing Psp machinery in Escherichia coli.Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and CyanobacteriaIn-depth profiling of the LiaR response of Bacillus subtilis.The vesicle-inducing protein 1 from Synechocystis sp. PCC 6803 organizes into diverse higher-ordered ring structuresMolecular determinants for PspA-mediated repression of the AAA transcriptional activator PspF.Subcellular localization, interactions and dynamics of the phage-shock protein-like Lia response in Bacillus subtilis.Essential role of VIPP1 in chloroplast envelope maintenance in Arabidopsis.Role of vesicle-inducing protein in plastids 1 in cpTat transport at the thylakoid.Membrane chaperoning by members of the PspA/IM30 protein family.PspA can form large scaffolds in Escherichia coli.The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding.Evidence for a role of VIPP1 in the structural organization of the photosynthetic apparatus in Chlamydomonas.PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport.Chloroplast-targeted Hsp90 plays essential roles in plastid development and embryogenesis in Arabidopsis possibly linking with VIPP1.The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.VIPP1 involved in chloroplast membrane integrity has GTPase activity in vitro.Escherichia coli phage-shock protein A (PspA) binds to membrane phospholipids and repairs proton leakage of the damaged membranes.IM30 triggers membrane fusion in cyanobacteria and chloroplasts
P2860
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P2860
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@en
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@nl
type
label
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@en
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@nl
prefLabel
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@en
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@nl
P2093
P2860
P356
P1476
Complex formation of Vipp1 depends on its alpha-helical PspA-like domain.
@en
P2093
Elena Aseeva
Friedrich Ossenbühl
Jürgen Soll
Lutz A Eichacker
P2860
P304
35535-35541
P356
10.1074/JBC.M401750200
P407
P577
2004-06-21T00:00:00Z