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Expanding the ubiquitin code through post-translational modification

Expanding the ubiquitin code through post-translational modification

http://www.wikidata.org/entity/Q26798369

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)UFMylation: A Unique & Fashionable Modification for Life Ubiquitination independent of E1 and E2 enzymes by bacterial effectors Absence of alsin function leads to corticospinal motor neuron vulnerability via novel disease mechanisms The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria.Phospho-ubiquitin: upending the PINK-Parkin-ubiquitin cascade Ubiquitin S65 phosphorylation engenders a pH-sensitive conformational switch.Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications.Exploring the diversity of protein modifications: special bacterial phosphorylation systems.Chemical and semisynthetic approaches to study and target deubiquitinases.Chemical ubiquitination for decrypting a cellular code.The increasing complexity of the ubiquitin code.Methylglyoxal-induced AMPK activation leads to autophagic degradation of thioredoxin 1 and glyoxalase 2 in HT22 nerve cells.Fine-tuning autophagy: from transcriptional to posttranslational regulation.The emerging complexity of ubiquitin architecture.Ubiquitin recognition by the proteasome.Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights.Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways.Genomics and epigenomics in rheumatic diseases: what do they provide in terms of diagnosis and disease management?Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9.Endophilin-A Deficiency Induces the Foxo3a-Fbxo32 Network in the Brain and Causes Dysregulation of Autophagy and the Ubiquitin-Proteasome System.Synthesis of Isomeric Phosphoubiquitin Chains Reveals that Phosphorylation Controls Deubiquitinase Activity and Specificity.ρ⁰ Cells Feature De-Ubiquitination of SLC Transporters and Increased Levels and Fluxes of Amino Acids.Parkinson's disease-related DJ-1 functions in thiol quality control against aldehyde attack in vitro.Plekhg5-regulated autophagy of synaptic vesicles reveals a pathogenic mechanism in motoneuron disease.Backbone and side-chain resonance assignments of Plasmodium falciparum SUMO.The Molecular Mechanisms of Regulation on USP2's Alternative Splicing and the Significance of Its Products.Ubiquitin turnover and endocytic trafficking in yeast are regulated by Ser57 phosphorylation of ubiquitin.Ubiquitin signaling and autophagy.Chemical biology approaches for studying posttranslational modifications.Ub-ProT reveals global length and composition of protein ubiquitylation in cells.Endosomal Rab cycles regulate Parkin-mediated mitophagy.Deubiquitylating enzymes and drug discovery: emerging opportunities.Impact of different ionization states of phosphorylated Serine-65 on ubiquitin structure and interactions.Understanding and exploiting autophagy signaling in plants.Biosynthesis and genetic encoding of phosphothreonine through parallel selection and deep sequencing.Regulation of the Stress-Activated Degradation of Mitochondrial Respiratory Complexes in Yeast.USP7/HAUSP: A SUMO deubiquitinase at the heart of DNA replication.Unexpected mitochondrial matrix localization of Parkinson's disease-related DJ-1 mutants but not wild-type DJ-1.

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P2860

Expanding the ubiquitin code through post-translational modification

http://www.wikidata.org/entity/Q26798369

description

2015 nî lūn-bûn

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2015 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2015年の論文

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2015年論文

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2015年論文

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2015年論文

@zh-hk

2015年論文

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2015年論文

@zh-tw

2015年论文

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name

Expanding the ubiquitin code through post-translational modification

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Expanding the ubiquitin code through post-translational modification

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Expanding the ubiquitin code through post-translational modification

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type

label

Expanding the ubiquitin code through post-translational modification

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Expanding the ubiquitin code through post-translational modification

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Expanding the ubiquitin code through post-translational modification

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prefLabel

Expanding the ubiquitin code through post-translational modification

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Expanding the ubiquitin code through post-translational modification

@en

Expanding the ubiquitin code through post-translational modification

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Expanding the ubiquitin code through post-translational modification

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Lina Herhaus

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P2860

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

Ubiquitin is phosphorylated by PINK1 to activate parkin

MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin

Phosphorylation-dependent activity of the deubiquitinase DUBA

Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth

Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase

Autoregulation of Parkin activity through its ubiquitin-like domain

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

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1071-83

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scholarly article

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1495966

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10.15252/EMBR.201540891

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4576978

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