Membrane proteins of the endoplasmic reticulum induce high-curvature tubules. - Wikidata - awgldk - TriplyDB

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

http://www.wikidata.org/entity/Q27939309

about

Mutations in the ER-shaping protein reticulon 2 cause the axon-degenerative disorder hereditary spastic paraplegia type 12 Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formation A class of dynamin-like GTPases involved in the generation of the tubular ER network Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin Endoplasmic Reticulum: The Favorite Intracellular Niche for Viral Replication and Assembly The endoplasmic reticulum: structure, function and response to cellular signaling Architecture and biogenesis of plus-strand RNA virus replication factories Membrane-shaping disorders: a common pathway in axon degeneration Building a nuclear envelope at the end of mitosis: coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation Membrane-mediated interaction between strongly anisotropic protein scaffolds Putting the Squeeze on Plasmodesmata: A Role for Reticulons in Primary Plasmodesmata Formation Peroxins Pex30 and Pex29 Dynamically Associate with Reticulons to Regulate Peroxisome Biogenesis from the Endoplasmic Reticulum ER network formation requires a balance of the dynamin-like GTPase Sey1p and the Lunapark family member Lnp1p.The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum.Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit.Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution Association of the yeast RNA-binding protein She2p with the tubular endoplasmic reticulum depends on membrane curvature.Reticulons Regulate the ER Inheritance Block during ER Stress.A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature.ER membrane-bending proteins are necessary for de novo nuclear pore formation Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-like fashion Transmembrane protein TMEM170A is a newly discovered regulator of ER and nuclear envelope morphogenesis in human cells Inner/Outer nuclear membrane fusion in nuclear pore assembly: biochemical demonstration and molecular analysis REEPs are membrane shaping adapter proteins that modulate specific g protein-coupled receptor trafficking by affecting ER cargo capacity A model for the generation and interconversion of ER morphologies Mutations in REEP6 Cause Autosomal-Recessive Retinitis Pigmentosa The Charcot Marie Tooth disease protein LITAF is a zinc-binding monotopic membrane protein.Identification of endoplasmic reticulum-shaping proteins in Plasmodium parasites Transmembrane and coiled-coil domain family 1 is a novel protein of the endoplasmic reticulum Endoplasmic reticulum-mediated signalling in cellular microdomains.Probing microscopic material properties inside simulated membranes through spatially resolved three-dimensional local pressure fields and surface tensions Cisternal organization of the endoplasmic reticulum during mitosis.Microtubules, the ER and Exu: new associations revealed by analysis of mini spindles mutations The small molecule dispergo tubulates the endoplasmic reticulum and inhibits export Kinectin-mediated endoplasmic reticulum dynamics supports focal adhesion growth in the cellular lamella Stacked endoplasmic reticulum sheets are connected by helicoidal membrane motifs.A spastic paraplegia mouse model reveals REEP1-dependent ER shaping.Direct observation of molecular arrays in the organized smooth endoplasmic reticulum.

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P2860

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

http://www.wikidata.org/entity/Q27939309

description

2008 nî lūn-bûn

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2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@ast

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@en

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@nl

type

label

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@ast

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@en

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@nl

prefLabel

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@ast

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@en

Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@nl

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SCIENCE.1153634

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Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.

@en

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Christiane Voss

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

Junjie Hu

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

Margaret Coughlin

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

Michael M Kozlov

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

Tom Shemesh

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

William A Prinz

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

Yoko Shibata

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

Zongli Li

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

P2860

Mechanism of endophilin N-BAR domain-mediated membrane curvature

Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms.

Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol

Curvature of clathrin-coated pits driven by epsin

BAR domains as sensors of membrane curvature: the amphiphysin BAR structure

How synaptotagmin promotes membrane fusion.

Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion.

Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p.

Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis

The dynamin superfamily: universal membrane tubulation and fission molecules?

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10.1126/SCIENCE.1153634

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319

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18309084

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endoplasmic reticulum