Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition. - Wikidata - wikimedia - TriplyDB

Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition.

Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition.

http://www.wikidata.org/entity/Q33899633

about

PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells Inhibitors of Protein Translocation Across the ER Membrane Subcellular Partitioning of Protein Tyrosine Phosphatase 1B to the Endoplasmic Reticulum and Mitochondria Depends Sensitively on the Composition of Its Tail Anchor A Conserved Archaeal Pathway for Tail-Anchored Membrane Protein Insertion The mechanism of membrane-associated steps in tail-anchored protein insertion A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum.The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes.Distinct pathways mediate the sorting of tail-anchored proteins to the plastid outer envelope.Membrane protein insertion at the endoplasmic reticulum.Msp1/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteins Lipid-dependent membrane protein topogenesis.In vitro dissection of protein translocation into the mammalian endoplasmic reticulum.A monomeric membrane peptide that lives in three worlds: in solution, attached to, and inserted across lipid bilayers.New roles of carboxypeptidase E in endocrine and neural function and cancer.Unassisted translocation of large polypeptide domains across phospholipid bilayers Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation pH-sensitive membrane peptides (pHLIPs) as a novel class of delivery agents.Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway.Peroxin-dependent targeting of a lipid-droplet-destined membrane protein to ER subdomains Tail-anchored membrane protein insertion into the endoplasmic reticulum.Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.Ca2+-calmodulin inhibits tail-anchored protein insertion into the mammalian endoplasmic reticulum membrane.Biogenesis of tail-anchored proteins: the beginning for the end?Tail-anchored membrane proteins: exploring the complex diversity of tail-anchored-protein targeting in plant cells.Chaperone receptors: guiding proteins to intracellular compartments.A portrait of the GET pathway as a surprisingly complicated young man.All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum.Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.Targeting acidity in diseased tissues: mechanism and applications of the membrane-inserting peptide, pHLIP.The emerging role of calcium-modulating cyclophilin ligand in posttranslational insertion of tail-anchored proteins into the endoplasmic reticulum membrane.CAML mediates survival of Myc-induced lymphoma cells independent of tail-anchored protein insertion.Tail-anchored Protein Insertion in Mammals: FUNCTION AND RECIPROCAL INTERACTIONS OF THE TWO SUBUNITS OF THE TRC40 RECEPTOR.A biochemical analysis of the constraints of tail-anchored protein biogenesis.CDK5 regulatory subunit-associated protein 1-like 1 (CDKAL1) is a tail-anchored protein in the endoplasmic reticulum (ER) of insulinoma cells.Mice lacking WRB reveal differential biogenesis requirements of tail-anchored proteins in vivo.Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum.Hydrophobic handoff for direct delivery of peroxisome tail-anchored proteins.Chloroplast envelope protein targeting fidelity is independent of cytosolic components in dual organelle assays.

P2860

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P2860

Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition.

http://www.wikidata.org/entity/Q33899633

description

2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005 թվականի հունիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Transmembrane topogenesis of a ...... by membrane lipid composition.

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Transmembrane topogenesis of a ...... by membrane lipid composition.

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type

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Transmembrane topogenesis of a ...... by membrane lipid composition.

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Transmembrane topogenesis of a ...... by membrane lipid composition.

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Transmembrane topogenesis of a ...... by membrane lipid composition.

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Transmembrane topogenesis of a ...... by membrane lipid composition.

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P356

SJ.EMBOJ.7600730

P1433

The EMBO Journal

P1476

Transmembrane topogenesis of a ...... by membrane lipid composition.

@en

P2093

Marja Makarow

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

Monica Yabal

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

Paolo Soffientini

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

Sandra Stefanovic

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

Silvia Brambillasca

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P2860

A protein of the endoplasmic reticulum involved early in polypeptide translocation

Signal recognition particle mediates post-translational targeting in eukaryotes

Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane

Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.

A tetrameric complex of membrane proteins in the endoplasmic reticulum

The tale of tail-anchored proteins: coming from the cytosol and looking for a membrane.

A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus

Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane.

Tail-anchored protein biosynthesis at the endoplasmic reticulum: the same but different.

The role of lipids in membrane insertion and translocation of bacterial proteins.

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2533-2542

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scholarly article

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10.1038/SJ.EMBOJ.7600730

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14

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24

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Ramanujan Shankar Hegde

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2005-06-23T00:00:00Z

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7770955

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15973434

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P921

transmembrane protein

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1176458

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