Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
about
Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survivalAlternative Antigen Processing for MHC Class I: Multiple Roads Lead to RomeA novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14Ras1 interacts with multiple new signaling and cytoskeletal loci in Drosophila eggshell patterning and morphogenesisChronic ethanol feeding affects proteasome-interacting proteinsMolecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II.Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms.The ubiquitin-proteasome system as a drug target in cerebrovascular disease: therapeutic potential of proteasome inhibitors.A giant protease with a twist: the TPP II complex from Drosophila studied by electron microscopy.Tripeptidyl peptidase II regulates sperm function by modulating intracellular Ca(2+) stores via the ryanodine receptor.Proteases in MHC class I presentation and cross-presentationVoltage sensor mutations differentially target misfolded K+ channel subunits to proteasomal and non-proteasomal disposal pathways.Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active siteAnalysis of the role of tripeptidyl peptidase II in MHC class I antigen presentation in vivoMechanisms of MHC class I-restricted antigen presentation.The role of the ubiquitin/proteasome system in cellular responses to radiation.Epstein-Barr virus oncogenesis and the ubiquitin-proteasome system.Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII.Molecular machines for protein degradation.Complexity, contradictions, and conundrums: studying post-proteasomal proteolysis in HLA class I antigen presentation.Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout miceNeed for tripeptidyl-peptidase II in major histocompatibility complex class I viral antigen processing when proteasomes are detrimental.Trafficking of exogenous peptides into proteasome-dependent major histocompatibility complex class I pathway following enterotoxin B subunit-mediated delivery.Tumors acquire inhibitor of apoptosis protein (IAP)-mediated apoptosis resistance through altered specificity of cytosolic proteolysis.The Enigma of Tripeptidyl-Peptidase II: Dual Roles in Housekeeping and Stress.Tripeptidyl Peptidase II Is Required for c-MYC-Induced Centriole Overduplication and a Novel Therapeutic Target in c-MYC-Associated NeoplasmsThe insert within the catalytic domain of tripeptidyl-peptidase II is important for the formation of the active complex.PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation.Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production.Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells.Size matters for the tripeptidylpeptidase II complex from Drosophila: The 6-MDa spindle form stabilizes the activated state.
P2860
Q24542503-2ADF3205-693C-4936-9F35-D346CED56FA7Q26864074-E1659AD4-E2BA-463B-94D2-977B171192CDQ28359750-491658FC-DD6A-478A-A0FF-A7C30D473937Q28362128-2F94A4C1-FB4C-44A1-BD79-2C85816C9486Q28582843-849699D4-3D4A-4689-8F4F-7AB77B8E13E5Q30476037-813A47D0-AF69-4B52-8927-25942E84945EQ31026772-85185989-B232-43D2-9E39-9B2846915B97Q33892755-1F4E6B64-52BD-46F3-B276-6EEEC6EDA0DAQ34370046-44F1618D-60C8-4837-A9EE-E27BBB68A8C8Q34789584-22D80960-4461-4075-BE76-8A290F6512F1Q34979864-8D51B814-E628-4707-A040-3EA58129704EQ35006046-43442E2B-B6C6-46D7-B87E-ECBD086204ACQ35037226-FB0AF9AC-D787-4C0A-8883-9B7C0457D8A2Q35041080-1A33723D-84D9-4116-BD43-FEF02BCF1120Q35050403-F26E2BD1-C8CC-464D-A4BB-8AC9762A9157Q35208807-EECF653F-446B-445E-BB99-084C1A5F5B3CQ35691576-9454AB3B-EBF8-45BF-9149-C13F0B84BF9BQ35821221-E9D9F73D-13D4-4DC9-8691-0E0D8862AD43Q36023030-D2518399-F792-4A44-B48A-599382D3B5B2Q36266433-966B3160-AF04-483F-8B69-660762BC9D8EQ36516221-2EA9F3A8-6041-456C-95EF-EE9A373B7AB0Q40211477-242D3821-2513-4B31-BBB6-8F18DBC3E9E6Q40519775-AB54C24E-2367-42B2-9E4B-F27A3CB48746Q41764558-7F4CB07B-0BAC-4E94-8C74-F279068CB06BQ42063622-395EE05C-68B5-478C-97D6-EC8DB14F4127Q42731717-5A40677B-6874-4EA5-9009-F4A35249F121Q43902827-DA0A510F-1818-4B59-9268-25ADD4E981E1Q44249684-0659D718-B8BC-449A-8BC0-2794161E7A6CQ44253376-99C8FAFA-18EC-42A5-83B1-D1B2EB96474DQ44572793-6EFF785C-9759-455A-9EB0-E59E5A2FBF0AQ47071014-3D3DC8C1-D8AD-4E19-8DF8-69465F28A185
P2860
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on August 2000
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@en
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@nl
type
label
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@en
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@nl
prefLabel
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@en
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@nl
P2093
P2860
P356
P1476
Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
@en
P2093
P2860
P304
P356
10.1073/PNAS.180328897
P407
P577
2000-08-01T00:00:00Z