The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome. - Wikidata - wikimedia - TriplyDB

The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome.

The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome.

http://www.wikidata.org/entity/Q37467606

about

Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?Role of Ubiquitin-Mediated Degradation System in Plant Biology The recognition of ubiquitinated proteins by the proteasome Functions of the 19S complex in proteasomal degradation Ubiquitin chain topology in plant cell signaling: a new facet to an evergreen story Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6.Autoregulation of the 26S proteasome by in situ ubiquitination Perilous journey: a tour of the ubiquitin-proteasome system Enhancement of proteasome activity by a small-molecule inhibitor of USP14 Proteasome proteolysis supports stimulated platelet function and thrombosis Ubiquitin-specific protease 14 regulates c-Jun N-terminal kinase signaling at the neuromuscular junction Nonenzymatic polymerization of ubiquitin: single-step synthesis and isolation of discrete ubiquitin oligomers HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate Immunity Clinically used antirheumatic agent auranofin is a proteasomal deubiquitinase inhibitor and inhibits tumor growth Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes.VRK1 regulates Cajal body dynamics and protects coilin from proteasomal degradation in cell cycle Gates, Channels, and Switches: Elements of the Proteasome Machine HAUSP-nucleolin interaction is regulated by p53-Mdm2 complex in response to DNA damage response Sequential ubiquitination and deubiquitination enzymes synchronize the dual sensor and effector functions of TRIM21 Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.Open-gate mutants of the mammalian proteasome show enhanced ubiquitin-conjugate degradation Unraveling the complexity of ubiquitin signaling Anthrax toxin-mediated delivery of the Pseudomonas exotoxin A enzymatic domain to the cytosol of tumor cells via cleavable ubiquitin fusions.Conserved Sequence Preferences Contribute to Substrate Recognition by the Proteasome.Ubiquitin C-terminal hydrolase37 regulates Tcf7 DNA binding for the activation of Wnt signalling.Expanding role of ubiquitination in NF-κB signaling.E3 ubiquitin ligases and abscisic acid signaling.Proteomics to study the diversity and dynamics of proteasome complexes: from fundamentals to the clinic.Review: unchained maladie - a reassessment of the role of Ubb(+1) -capped polyubiquitin chains in Alzheimer's disease.Role of the ubiquitin-proteasome system in nervous system function and disease: using C. elegans as a dissecting tool.The ubiquitin proteasome system - implications for cell cycle control and the targeted treatment of cancer.DNA damage emergency: cellular garbage disposal to the rescue?Ubiquitin pathways in neurodegenerative disease.Screening for E3-ubiquitin ligase inhibitors: challenges and opportunities.Immunity-related GTPase M (IRGM) proteins influence the localization of guanylate-binding protein 2 (GBP2) by modulating macroautophagy.The Arabidopsis RING E3 ubiquitin ligase AtAIRP2 plays combinatory roles with AtAIRP1 in abscisic acid-mediated drought stress responses.Control of Amino Acid Homeostasis by a Ubiquitin Ligase-Coactivator Protein Complex.Functional roles of the pepper RING finger protein gene, CaRING1, in abscisic acid signaling and dehydration tolerance.The Arabidopsis C3H2C3-type RING E3 ubiquitin ligase AtAIRP1 is a positive regulator of an abscisic acid-dependent response to drought stress.Ubiquitination of plant immune receptors

P2860

Q24617857-00D31495-788E-434F-9A04-DA62723371C5 Q26744849-F8DE8B94-EA0B-4694-B2B1-428574964421 Q26748001-999EB020-DFC1-4A7B-9759-0ED5107BA1F7 Q26996345-357EF432-C570-4DC0-A8EA-D4235B94AE48 Q27025223-FE059922-2976-4A69-885C-079D66CB3FE9 Q27935947-B7600F14-A8F9-4247-AD3E-C836159AB256 Q28238443-CC433887-837D-4DF3-AB14-2B223E4F3337 Q28306492-0C69CA1C-579A-4800-8C58-0D94BD5F706C Q29616735-939E5B1D-DF6D-4653-BAF0-C0592957ED41 Q30580785-357D3293-76CD-4BCE-B87B-6DFED2E76511 Q30646859-907524F8-3D32-4C16-B1B1-4FE074AA343D Q33852992-948CE97A-D01A-4C40-9A69-7285A6DDF21F Q33883877-7BACB9CE-8039-43EE-9F39-632CEED90A34 Q34221890-CD90DCE7-1DEF-4A0F-A9C5-8E0108E2E607 Q34994389-7C13971E-4FB2-4137-9F27-6332B2447B23 Q35727732-9CD24B75-E409-4F15-8851-AA6EE8FFD9B4 Q35862786-33EB7B8E-D5FE-4DD7-88CA-205072CC9135 Q35913537-52AC2211-CED5-449C-BEBF-7931B8D7E872 Q35961313-5ADF52E6-21A0-452F-B377-5C3A690BD3B7 Q36074198-768A0550-09E8-43DB-8DEB-012A340F4A54 Q36675188-66376B60-E419-4203-82B0-72AD514F976D Q36722909-317B035B-B8B4-46BC-97DC-AFD943BC5B9C Q36829224-C3FEAB21-9A24-4C37-A00E-6A22D487F21C Q37078653-20E1FD00-CC77-4F04-9C13-00D6A0834D0E Q37642658-8ED3A336-7859-449E-A494-AA5A85C7BE12 Q37816941-98379BE7-8242-4B53-921A-75BE7F28FD9D Q37848612-83E00EB9-0971-4244-8544-4B674737F07E Q37912201-3CB5555B-5A53-4942-AB61-4017E028638A Q37955915-6D6601C3-2737-4413-9882-49517E8C4DE2 Q37989861-F45EFD55-A2E8-4C89-B2A6-2FA1A21AEBF5 Q38087182-0D348777-E2EA-458E-9B99-3383500C1395 Q38090434-35E74AD3-8ACE-4783-90D9-9767EF9D42C3 Q38234883-49C120BA-4C8C-464C-BA36-DDDF5630D2AE Q38252591-FACB1D02-5A2B-45DD-B5D1-1CC8764ADE8C Q38263938-85F4A9FD-103D-4117-8CAA-E2D792B1A05D Q38945356-C47E9B04-9D06-4B57-BCEF-D92C1B0EBA95 Q39013730-6C2954F9-640C-4E67-959A-A464463F71B1 Q39179829-C779AB4F-2731-413C-A8C3-90086EB1FA10 Q39416205-67668AE7-E1A1-494A-A0BF-0B5938DE9FC8 Q39457370-A848FD28-6A3C-475C-B749-C89464511D3E

P2860

The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome.

http://www.wikidata.org/entity/Q37467606

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on December 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@en

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@nl

type

label

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@en

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@nl

prefLabel

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@en

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@nl

P1433

Q37467606-F47645AE-6341-4288-AB1B-C89C0B405638

P1476

Q37467606-AD9B5C82-54C7-441C-97EB-768BCBD57E87

P2093

Q37467606-372ABD69-CDBB-458C-A1E0-D885F7C43E8B

Q37467606-44A900B3-C63C-43CF-86EB-2E4AFDCC392A

Q37467606-70B8FB45-0447-4E30-8597-C9A7B2260DBB

Q37467606-7E8FC322-99BD-40DE-8776-D70105C4804A

Q37467606-96CA778E-BB3C-47D2-AF53-3DDF87BA3284

Q37467606-CC674323-E014-4FAB-A634-4B3ECABEB8AE

Q37467606-D1A617FB-36B9-4E23-9C14-7C8B29171175

P2860

Q37467606-00D0B5C4-A8F3-4480-803E-39CF60BBC43D

Q37467606-02BE5280-FA34-4E64-8ED1-D4238554073D

Q37467606-0AE92616-9CFE-4EB4-9752-0D103A4A4D65

Q37467606-0C38FF39-2DE3-4D3C-AFC7-DCC72779222C

Q37467606-135820BF-D82A-4208-808E-D6F2DF2764A6

Q37467606-16ECE0D9-6F55-4767-992C-339A080004E1

Q37467606-16F1C1E3-1805-41FC-8EF3-AD9121A4511C

Q37467606-19C51176-6266-4470-AECA-8C80EEC4C884

Q37467606-2244354D-DE87-45AF-AC1D-21D02754A754

Q37467606-228C00B3-A32C-458F-8C0B-A20ED722C7FD

P304

Q37467606-5F04DEA3-F873-4D2E-A5B8-58555010AF4F

P31

Q37467606-9D0A751B-CA2F-481C-B190-74A0ACCC502C

P356

Q37467606-4C96D2F5-32C8-4842-BC63-8A6E76219E79

P407

Q37467606-012A58D2-5B4F-4705-A2F0-B7A284B132F2

P433

Q37467606-89288FBB-7C1E-4E1B-86D3-AE4810E218AA

P478

Q37467606-9DD06172-9479-44BF-8F11-74057A242FCF

P577

Q37467606-BC09ECB2-0A4E-499E-949A-676868C14A76

P698

Q37467606-F8B8F025-785F-4362-ADFD-774F5DFA5617

P921

Q37467606-463C95DE-67F3-4650-9EED-F7348EE3FDDA

P932

Q37467606-54B6EC99-B821-4FA8-93D8-EE4F0CD67450

P356

JBC.M109.052928

P1433

Journal of Biological Chemistry

P1476

The lysine 48 and lysine 63 ub ...... rently by the 26 s proteasome.

@en

P2093

Andrew D Jacobson

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

Chang-Wei Liu

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

Junmin Peng

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

Ke-Jun Han

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

Nan-Yan Zhang

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

Ping Xu

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

Seth Noone

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

P2860

Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair

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

Chromosome alignment and segregation regulated by ubiquitination of survivin

Mass spectrometric characterization of the affinity-purified human 26S proteasome complex

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling

A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes

A ubiquitin ligase complex assembles linear polyubiquitin chains

Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome

K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1

Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex

P304

35485-35494

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

P31

scholarly article

P356

10.1074/JBC.M109.052928

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

P407

P433

51

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

P478

284

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

P577

2009-12-01T00:00:00Z

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

P698

19858201

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

P921

ubiquitin-proteasome system

P932

2790978

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