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Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding

Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding

http://www.wikidata.org/entity/Q35812368

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N-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule Pathway Perspectives and Insights into the Competition for Aminoacyl-tRNAs between the Translational Machinery and for tRNA Dependent Non-Ribosomal Peptide Bond Formation Autophagy signal transduction by ATG proteins: from hierarchies to networks The different roles of selective autophagic protein degradation in mammalian cells Formation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative Stress Glioma-derived cancer stem cells are hypersensitive to proteasomal inhibition.Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets.A Review of the Human Sigma-1 Receptor Structure.Berberine-induced autophagic cell death by elevating GRP78 levels in cancer cells.Plant arginyltransferases (ATEs).Structure biology of selective autophagy receptors.New insights into the protein aggregation pathology in myotilinopathy by combined proteomic and immunolocalization analyses.Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications.Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway.Identification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Formyl-methionine as a degradation signal at the N-termini of bacterial proteins.GRP78 at the Centre of the Stage in Cancer and Neuroprotection.To deliver or to degrade - an interplay of the ubiquitin-proteasome system, autophagy and vesicular transport in plants.Post-translational protein arginylation in the normal nervous system and in neurodegeneration.Autophagy proteins in antigen processing for presentation on MHC molecules.p62/SQSTM1-Dr. Jekyll and Mr. Hyde that prevents oxidative stress but promotes liver cancer.Crosstalk and Interplay between the Ubiquitin-Proteasome System and Autophagy.Degradation of Serotonin N-Acetyltransferase, a Circadian Regulator, by the N-end Rule Pathway.p62/SQSTM1/Sequestosome-1 is an N-recognin of the N-end rule pathway which modulates autophagosome biogenesis.Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration Protein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts.Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.The arginylation branch of the N-end rule pathway positively regulates cellular autophagic flux and clearance of proteotoxic proteins.An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes.HSF1 stress response pathway regulates autophagy receptor SQSTM1/p62-associated proteostasis Arginylation: a new regulator of mRNA stability and heat stress response.Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System.Clusterin protects neurons against intracellular proteotoxicity.The endoplasmic reticulum-residing chaperone BiP is short-lived and metabolized through N-terminal arginylation.HSPA5 negatively regulates lysosomal activity through ubiquitination of MUL1 in head and neck cancer.Regulation of selective autophagy: the p62/SQSTM1 paradigm.A reference-based protein degradation assay without global translation inhibitors.p62 filaments capture and present ubiquitinated cargos for autophagy.

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P2860

Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding

http://www.wikidata.org/entity/Q35812368

description

2015 nî lūn-bûn

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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

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

@zh-cn

name

Amino-terminal arginylation ta ...... autophagy through p62 binding

@ast

Amino-terminal arginylation ta ...... autophagy through p62 binding

@en

type

label

Amino-terminal arginylation ta ...... autophagy through p62 binding

@ast

Amino-terminal arginylation ta ...... autophagy through p62 binding

@en

prefLabel

Amino-terminal arginylation ta ...... autophagy through p62 binding

@ast

Amino-terminal arginylation ta ...... autophagy through p62 binding

@en

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Nature Cell Biology

P1476

Amino-terminal arginylation ta ...... autophagy through p62 binding

@en

P2093

Adriana Zakrzewska

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

Bo Yeon Kim

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

Dong Hoon Han

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

Hee Gu Lee

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

Hyunjoo Cha-Molstad

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

Ji Eun Yu

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

Jong Seog Ahn

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

Joonsung Hwang

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

Jun Min Jang

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

Jung Gi Kim

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

P2860

Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway

Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice

The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy

A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons.

Activation of chaperone-mediated autophagy during oxidative stress

The N-end rule pathway

Chaperone-mediated autophagy: a unique way to enter the lysosome world

Diversity of degradation signals in the ubiquitin-proteasome system

Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway

Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway

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P304

917-929

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scholarly article

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10.1038/NCB3177

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7

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17

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Aaron Ciechanover

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2015-06-15T00:00:00Z

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278330613

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P698

26075355

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P921

molecular chaperones

endoplasmic reticulum

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4490096

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