Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12

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Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12 is …
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P356DOI10.1074/JBC.M110.134510
P8608Fatcat IDrelease_s2ywy7pukzfxtjjj2pvjrvfr5q
P3181OpenCitations bibliographic resource ID3160458
P932PMC publication ID2962499
P698PubMed publication ID20739285

P50authorJean-François TrempeQ67207978
Kalle GehringQ28037054
P2093author name stringNicholas R Brown
Edward D Lowe
Jane A Endicott
Colin Gordon
Martin E M Noble
Jonas Boehringer
Christiane Riedinger
P2860cites workThe structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box moduleQ24319910
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Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensorQ42936102
Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23.Q43862937
Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteinsQ44342716
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ESyPred3D: Prediction of proteins 3D structuresQ48622625
Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised.Q52579023
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Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognitionQ81643532
DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5aQ27642353
Proteasome subunit Rpn13 is a novel ubiquitin receptorQ27650664
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Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13Q27657027
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The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.Q27929822
Proteasome subunit Rpn1 binds ubiquitin-like protein domainsQ27930136
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Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasomeQ27934803
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Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasomeQ27937521
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Proteins containing the UBA domain are able to bind to multi-ubiquitin chainsQ29614360
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Subunit architecture of intact protein complexes from mass spectrometry and homology modeling.Q33322101
Functional analysis of the proteasome regulatory particleQ33654847
Rad23 promotes the targeting of proteolytic substrates to the proteasomeQ34283029
Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition.Q34412166
Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1.Q34556881
Molecular mechanisms of proteasome assemblyQ34928594
Complement and the multifaceted functions of VWA and integrin I domainsQ35238346
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Measuring ubiquitin chain linkage: Rap80 uses a molecular ruler mechanism for ubiquitin linkage specificityQ37326489
PCI complexes: Beyond the proteasome, CSN, and eIF3 Troika.Q37580456
The diversity of ubiquitin recognition: hot spots and varied specificityQ37764527
Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1.Q38340703
Monoubiquitination of RPN10 regulates substrate recruitment to the proteasome.Q41257869
Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80.Q42080792
Mechanism of Lys48-linked polyubiquitin chain recognition by the Mud1 UBA domainQ42139176
P433issue44
P407language of work or nameEnglishQ1860
P921main subjectcell biologyQ7141
K48-linked polyubiquitin modification-dependent protein bindingQ21111536
P304page(s)33992-4003
P577publication date2010-10-29
P1433published inJournal of Biological ChemistryQ867727
P1476titleStructure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12
P478volume285