Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. - Wikidata - awgldk - TriplyDB

Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.

Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.

http://www.wikidata.org/entity/Q37098025

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Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1 Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1 accumulation and aggresome formation Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death Gene overexpression: uses, mechanisms, and interpretation Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13 The Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding Domain Structural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporation Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6.Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome.A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis.Rpn1 and Rpn2 coordinate ubiquitin processing factors at proteasome Regulation of proteasome activity in health and disease Recognition and processing of ubiquitin-protein conjugates by the proteasome Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2 Molecular mechanisms of proteasome plasticity in aging.Assembly, structure, and function of the 26S proteasome.VWA domain of S5a restricts the ability to bind ubiquitin and Ubl to the 26S proteasome.Improved quantitative mass spectrometry methods for characterizing complex ubiquitin signals.Pharmacogenomics of bortezomib test-dosing identifies hyperexpression of proteasome genes, especially PSMD4, as novel high-risk feature in myeloma treated with Total Therapy 3 Base-CP proteasome can serve as a platform for stepwise lid formation Extended ubiquitin species are protein-based DUB inhibitors.APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1 Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome The ubiquitin-proteasome system of Saccharomyces cerevisiae.Ubiquitin receptors and protein quality control Ubiquilin/Dsk2 promotes inclusion body formation and vacuole (lysosome)-mediated disposal of mutated huntingtin UBQLN2 Mediates Autophagy-Independent Protein Aggregate Clearance by the Proteasome.Regulated endoplasmic reticulum-associated degradation of a polytopic protein: p97 recruits proteasomes to Insig-1 before extraction from membranes Proteomics to study the diversity and dynamics of proteasome complexes: from fundamentals to the clinic.Structural disorder and its role in proteasomal degradation.Tuning the proteasome to brighten the end of the journey.The deubiquitylating enzyme Ubp12 regulates Rad23-dependent proteasomal degradation.Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.A reduced VWA domain-containing proteasomal ubiquitin receptor of Giardia lamblia localizes to the flagellar pore regions in microtubule-dependent manner.Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome.Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism.BAG6 regulates the quality control of a polytopic ERAD substrate.S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains

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P2860

Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.

http://www.wikidata.org/entity/Q37098025

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

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh

2008年學術文章

@zh-hant

name

Extraproteasomal Rpn10 restric ...... ng protein Dsk2 to proteasome.

@en

Extraproteasomal Rpn10 restric ...... ng protein Dsk2 to proteasome.

@nl

type

label

Extraproteasomal Rpn10 restric ...... ng protein Dsk2 to proteasome.

@en

Extraproteasomal Rpn10 restric ...... ng protein Dsk2 to proteasome.

@nl

prefLabel

Extraproteasomal Rpn10 restric ...... ng protein Dsk2 to proteasome.

@en

Extraproteasomal Rpn10 restric ...... ng protein Dsk2 to proteasome.

@nl

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J.MOLCEL.2008.10.011

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P1476

Extraproteasomal Rpn10 restric ...... ing protein Dsk2 to proteasome

@en

P2093

Arun Dakshinamurthy

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

Inbal Ziv

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

Noa Reis

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

Oded Kleifeld

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

Woong Kim

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

Yulia Matiuhin

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P2860

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

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains

Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains

A ubiquitin ligase complex assembles linear polyubiquitin chains

Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.

Recognition of the polyubiquitin proteolytic signal

Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series

The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome

Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a

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415-425

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scholarly article

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10.1016/J.MOLCEL.2008.10.011

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3

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32

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Donald S Kirkpatrick

Michael H Glickman

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2008-11-01T00:00:00Z

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23460379

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18995839

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2643056

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