Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
about
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machineryThe Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding DomainStructure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12A new crystal form of Lys48-linked diubiquitinStructural and functional characterization of Rpn12 identifies residues required for Rpn10 proteasome incorporationMechanism of the Rpn13-induced activation of Uch37Molecular architecture and assembly of the eukaryotic proteasomeNew conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitinLocalization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopyRpn1 and Rpn2 coordinate ubiquitin processing factors at proteasomeStructure of the TbBILBO1 protein N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch.The Rad23 ubiquitin receptor, the proteasome and functional specificity in transcriptional control.Recent advances in polyubiquitin chain recognition.Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targetsLife and destruction: ubiquitin-mediated proteolysis in aging and longevityMultiDsk: a ubiquitin-specific affinity resinA screenable in vivo assay to study proteostasis networks in Caenorhabditis elegans.Regulated protein turnover: snapshots of the proteasome in action.Gates, Channels, and Switches: Elements of the Proteasome MachineRpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasomeUbp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.The ubiquitin-proteasome system of Saccharomyces cerevisiae.Roles of p97-associated deubiquitinases in protein quality control at the endoplasmic reticulumRecognition and cleavage of related to ubiquitin 1 (Rub1) and Rub1-ubiquitin chains by components of the ubiquitin-proteasome systemDesign principles of a universal protein degradation machine.Linkage-specific conformational ensembles of non-canonical polyubiquitin chainsThe Proteasome Ubiquitin Receptor hRpn13 and Its Interacting Deubiquitinating Enzyme Uch37 Are Required for Proper Cell Cycle ProgressionUbiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.Evaluation of selected binding domains for the analysis of ubiquitinated proteomesA proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress.Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Structural insights into proteasome activation by the 19S regulatory particle.Proteomics to study the diversity and dynamics of proteasome complexes: from fundamentals to the clinic.Ubiquitin-binding domains: mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin-modified proteomes.Structural disorder and its role in proteasomal degradation.Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.Structure and recognition of polyubiquitin chains of different lengths and linkage.Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome.DNA-damage-inducible 1 protein (Ddi1) contains an uncharacteristic ubiquitin-like domain that binds ubiquitin.
P2860
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P2860
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@en
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@nl
type
label
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@en
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@nl
prefLabel
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@en
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@nl
P2093
P2860
P1433
P1476
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
@en
P2093
Daoning Zhang
David Fushman
Michael H Glickman
Rina Rosenzweig
Vered Bronner
Yulia Matiuhin
P2860
P304
P356
10.1016/J.MOLCEL.2009.11.012
P577
2009-12-01T00:00:00Z