Capturing protein interactions in the secretory pathway of living cells. - Test2 - elhamkhani - TriplyDB

Capturing protein interactions in the secretory pathway of living cells.

Capturing protein interactions in the secretory pathway of living cells.

http://www.wikidata.org/entity/Q33758366

about

Annexin A2 is involved in the formation of hepatitis C virus replication complex on the lipid raft A proteome-scale map of the human interactome network The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.Popular computational methods to assess multiprotein complexes derived from label-free affinity purification and mass spectrometry (AP-MS) experiments The Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible Molecule ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57 Interaction of glutaric aciduria type 1-related glutaryl-CoA dehydrogenase with mitochondrial matrix proteins Molecular and functional mapping of EED motifs required for PRC2-dependent histone methylation A two-hybrid assay to study protein interactions within the secretory pathway InterPred: A pipeline to identify and model protein-protein interactions.Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells.APEx 2-hybrid, a quantitative protein-protein interaction assay for antibody discovery and engineering Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36.Identification of ERGIC-53 as an intracellular transport receptor of alpha1-antitrypsin.Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.Phosphorylation modification of wheat lectin VER2 is associated with vernalization-induced O-GlcNAc signaling and intracellular motility.Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.LEC-BiFC: a new method for rapid assay of protein interaction.Bimolecular fluorescence complementation: lighting up seven transmembrane domain receptor signalling networks Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells.c-Abl activates janus kinase 2 in normal hematopoietic cells.Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation.Split-protein systems: beyond binary protein-protein interactions Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.An experimentally derived confidence score for binary protein-protein interactions.Molecular basis of LMAN1 in coordinating LMAN1-MCFD2 cargo receptor formation and ER-to-Golgi transport of FV/FVIII ZP2 and ZP3 cytoplasmic tails prevent premature interactions and ensure incorporation into the zona pellucida.A molecular specificity code for the three mammalian KDEL receptors.In situ visualization of protein interactions in sensory neurons: glutamic acid-rich proteins (GARPs) play differential roles for photoreceptor outer segment scaffolding High-throughput methods for identification of protein-protein interactions involving short linear motifs.Combined deficiency of factor V and factor VIII is due to mutations in either LMAN1 or MCFD2 Distinct CCR7 glycosylation pattern shapes receptor signaling and endocytosis to modulate chemotactic responses.Shining light on signaling and metabolic networks by genetically encoded biosensors.Visualization of molecular interactions by fluorescence complementation.Wnt7a interaction with Fzd5 and detection of signaling activation using a split eGFP Cysteine cathepsin non-inhibitory binding partners: modulating intracellular trafficking and function.Up-regulation of GABA(B) receptor signaling by constitutive assembly with the K+ channel tetramerization domain-containing protein 12 (KCTD12)Bioluminescence: a versatile technique for imaging cellular and molecular features.Yeast surface two-hybrid for quantitative in vivo detection of protein-protein interactions via the secretory pathway.

P2860

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P2860

Capturing protein interactions in the secretory pathway of living cells.

http://www.wikidata.org/entity/Q33758366

description

2005 nî lūn-bûn

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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Capturing protein interactions in the secretory pathway of living cells.

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Capturing protein interactions in the secretory pathway of living cells.

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Capturing protein interactions in the secretory pathway of living cells.

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Capturing protein interactions in the secretory pathway of living cells.

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Capturing protein interactions in the secretory pathway of living cells.

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Capturing protein interactions in the secretory pathway of living cells.

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PNAS.0501976102

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Proceedings of the National Academy of Sciences of the United States of America

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Capturing protein interactions in the secretory pathway of living cells.

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P2093

Beat Nyfeler

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Hans-Peter Hauri

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Stephen W Michnick

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P2860

Visualization of biochemical networks in living cells

Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein

Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt

VIPL, a VIP36-like membrane protein with a putative function in the export of glycoproteins from the endoplasmic reticulum

Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa

A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation

Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs

Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins

Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications

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6350-6355

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10.1073/PNAS.0501976102

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