Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum. - Wikidata - wikimedia - TriplyDB

Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.

Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.

http://www.wikidata.org/entity/Q39994820

about

ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular proteins A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum Endoplasmic reticulum chaperones and oxidoreductases: critical regulators of tumor cell survival and immunorecognition Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex TM9 family proteins control surface targeting of glycine-rich transmembrane domains Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER.Dynamic structure formation of peripheral membrane proteins.Further assembly required: construction and dynamics of the endoplasmic reticulum network.The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.Visualization of endoplasmic reticulum subdomains in cultured cells.A comprehensive comparison of transmembrane domains reveals organelle-specific properties.The Golgi localization of GOLPH2 (GP73/GOLM1) is determined by the transmembrane and cytoplamic sequences.A systematic approach to pair secretory cargo receptors with their cargo suggests a mechanism for cargo selection by Erv14.The membrane-spanning domain of gp41 plays a critical role in intracellular trafficking of the HIV envelope protein.Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum.Maize opaque10 Encodes a Cereal-Specific Protein That Is Essential for the Proper Distribution of Zeins in Endosperm Protein Bodies.SSH Analysis of Endosperm Transcripts and Characterization of Heat Stress Regulated Expressed Sequence Tags in Bread Wheat.Untangling the web: mechanisms underlying ER network formation.Anchors aweigh: protein localization and transport mediated by transmembrane domains Palmitoylation of membrane proteins (Review).ER exit sites--localization and control of COPII vesicle formation.Plasmodesmata viewed as specialised membrane adhesion sites.Cellular and molecular biology of glycosphingolipid glycosylation.Organization of the synthesis of glycolipid oligosaccharides in the Golgi complex.Membrane-mediated interactions--a physico-chemical basis for protein sorting.Arrivals and departures at the plasma membrane: direct and indirect transport routes.Trafficking of plant plasma membrane aquaporins: multiple regulation levels and complex sorting signals.De novo peroxisome biogenesis: Evolving concepts and conundrums.A positive signal prevents secretory membrane cargo from recycling between the Golgi and the ER.Targeted activation of conventional and novel protein kinases C through differential translocation patterns CDK5 regulatory subunit-associated protein 1-like 1 (CDKAL1) is a tail-anchored protein in the endoplasmic reticulum (ER) of insulinoma cells.Protein sorting and membrane-mediated interactions.On the role of acylation of transmembrane proteins.Structural mutants of dengue virus 2 transmembrane domains exhibit host-range phenotype.Multiple cytosolic and transmembrane determinants are required for the trafficking of SCAMP1 via an ER-Golgi-TGN-PM pathway.GRASP65 and GRASP55 sequentially promote the transport of C-terminal valine-bearing cargos to and through the Golgi complex.Dysfunction of bovine endogenous retrovirus K2 envelope glycoprotein is related to unsuccessful intracellular trafficking.Influence of hydrophobic mismatching on membrane protein diffusion.Intra-ER sorting of the peroxisomal membrane protein Pex3 relies on its luminal domain.Apicoplast targeting of a Toxoplasma gondii transmembrane protein requires a cytosolic tyrosine-based motif.

P2860

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P2860

Transmembrane domain-dependent partitioning of membrane proteins within the endoplasmic reticulum.

http://www.wikidata.org/entity/Q39994820

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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2008年學術文章

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name

Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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type

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Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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Journal of Cell Biology

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Transmembrane domain-dependent ...... hin the endoplasmic reticulum.

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P2093

Maura Francolini

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Nica Borgese

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Paolo Ronchi

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Sara Colombo

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P2860

Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER

Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae

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

Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells

Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway

A high-molecular-weight complex of membrane proteins BAP29/BAP31 is involved in the retention of membrane-bound IgD in the endoplasmic reticulum

Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization

Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast.

Rer1p as common machinery for the endoplasmic reticulum localization of membrane proteins.

A class of membrane proteins shaping the tubular endoplasmic reticulum.

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105-118

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10.1083/JCB.200710093

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1

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181

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18391072

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P921

transmembrane protein

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2287291

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