Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization - Test2 - elhamkhani - TriplyDB

Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization

Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization

http://www.wikidata.org/entity/Q24555822

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Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability Structural genomics of human proteins--target selection and generation of a public catalogue of expression clones The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes Evf, a virulence factor produced by the Drosophila pathogen Erwinia carotovora, is an S-palmitoylated protein with a new fold that binds to lipid vesicles Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase Complex Crystal structure of the yeast TRAPP-associated protein Tca17 Global analysis of protein palmitoylation in yeast The TRAPP complex: insights into its architecture and function Current perspective on protein S-acylation in plants: more than just a fatty anchor?Fatty acylation of proteins: The long and the short of it.Yarrowia lipolytica vesicle-mediated protein transport pathways.Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.Structure and mechanism in membrane trafficking.The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex Mutational analysis of the yeast TRAPP subunit Trs20p identifies roles in endocytic recycling and sporulation Role of tethering factors in secretory membrane traffic.Autopalmitoylation of TEAD proteins regulates transcriptional output of the Hippo pathway Protein lipidation.The importance of lipid modified proteins in plants.An outlook on protein S-acylation in plants: what are the next steps?The predominant species of nonstructural protein 4B in hepatitis C virus-replicating cells is not palmitoylated.A trs20 mutation that mimics an SEDT-causing mutation blocks selective and non-selective autophagy: a model for TRAPP III organization.Membrane skeletal association and post-translational allosteric regulation of Toxoplasma gondii GAPDH1.Evolution of the vertebrate bone matrix: an expression analysis of the network forming collagen paralogues in amphibian osteoblasts.

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P2860

Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization

http://www.wikidata.org/entity/Q24555822

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2005 nî lūn-bûn

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2005 թուականի Մարտին հրատարակուած գիտական յօդուած

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2005 թվականի մարտին հրատարակված գիտական հոդված

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2005年の論文

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Structure of palmitoylated BET ...... mbly and membrane localization

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Structure of palmitoylated BET ...... mbly and membrane localization

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Structure of palmitoylated BET ...... mbly and membrane localization

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Structure of palmitoylated BET ...... mbly and membrane localization

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Structure of palmitoylated BET ...... mbly and membrane localization

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Structure of palmitoylated BET ...... mbly and membrane localization

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The EMBO Journal

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Structure of palmitoylated BET ...... mbly and membrane localization

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Andrew P Turnbull

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Bianka Prinz

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Caterina Holz

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Christine Lang

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Daniel Kümmel

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Eva-Christina Müller

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Frank H Niesen

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Heinrich Delbrück

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Jeffrey Schultchen

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Joachim Behlke

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P2860

The genome sequence of Schizosaccharomyces pombe

Functional organization of the yeast proteome by systematic analysis of protein complexes

Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.

TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion.

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda

High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings

Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands

Maximum-likelihood density modification

Automated protein model building combined with iterative structure refinement

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