26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide.
about
PI31 is a modulator of proteasome formation and antigen processingEthanol-induced oxidant stress modulates hepatic autophagy and proteasome activityAlternative Antigen Processing for MHC Class I: Multiple Roads Lead to RomeMechanisms of HIV protein degradation into epitopes: implications for vaccine designAntigenic peptide trimming by ER aminopeptidases--insights from structural studiesHepatitis C virus and ethanol alter antigen presentation in liver cellsRationally designed inhibitor targeting antigen-trimming aminopeptidases enhances antigen presentation and cytotoxic T-cell responsesThe immunoproteasome and viral infection: a complex regulator of inflammationERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulumThe ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residuesRegulation of CD8+ T cell development by thymus-specific proteasomesRequirement of the proteasome for the trimming of signal peptide-derived epitopes presented by the nonclassical major histocompatibility complex class I molecule HLA-EERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulumMajor histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidaseThe transporter associated with antigen processing: function and implications in human diseasesProteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97A ubiquitin independent degradation pathway utilized by a hepatitis B virus envelope protein to limit antigen presentationProgressively impaired proteasomal capacity during terminal plasma cell differentiation.Computational prediction of cleavage using proteasomal in vitro digestion and MHC I ligand data.CTL escape mediated by proteasomal destruction of an HIV-1 cryptic epitopeThe caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.EpiJen: a server for multistep T cell epitope prediction.N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation.The internal sequence of the peptide-substrate determines its N-terminus trimming by ERAP1.The distribution of CTL epitopes in HIV-1 appears to be random, and similar to that of other proteomes.Pathways of antigen processing.Cutting Edge: Coding single nucleotide polymorphisms of endoplasmic reticulum aminopeptidase 1 can affect antigenic peptide generation in vitro by influencing basic enzymatic properties of the enzymeThe specificity of trimming of MHC class I-presented peptides in the endoplasmic reticulum.Characterizing the specificity and cooperation of aminopeptidases in the cytosol and endoplasmic reticulum during MHC class I antigen presentationThe antiviral efficacy of HIV-specific CD8⁺ T-cells to a conserved epitope is heavily dependent on the infecting HIV-1 isolate.PA28αβ: the enigmatic magic ring of the proteasome?Modelling proteasome and proteasome regulator activities.Placental leucine aminopeptidase efficiently generates mature antigenic peptides in vitro but in patterns distinct from endoplasmic reticulum aminopeptidase 1Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes.Deletion of immunoproteasome subunits imprints on the transcriptome and has a broad impact on peptides presented by major histocompatibility complex I molecules.Enhanced delivery of exogenous peptides into the class I antigen processing and presentation pathway.Unexpected role for the immunoproteasome subunit LMP2 in antiviral humoral and innate immune responses.The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism.Study of antigen-processing steps reveals preferences explaining differential biological outcomes of two HLA-A2-restricted immunodominant epitopes from human immunodeficiency virus type 1.Nature of pharmacophore influences active site specificity of proteasome inhibitors.
P2860
Q24540374-61C85F1F-778E-463C-A24D-6B4AD660D303Q26852284-FDB7FB02-C054-48AF-A911-AD22A40DAF2DQ26864074-E9EDBD12-ACE0-403A-B8B5-AD2A82BB65ADQ26866505-997DEB99-EC60-4E6B-92FE-7FF2B6B9059CQ27009465-9504540C-A797-4C0C-B01D-33E55CC8BCABQ27488237-AB96BFB2-E556-4AD9-8134-3DD42501052DQ27680633-8B37939F-2124-4B21-8C30-E03780F2EFE2Q27694656-B16B3C4B-2C3D-48F0-837E-55CD675A055BQ28115045-BA083297-B809-4E9C-AE3F-7294A244630CQ28115737-A99489C0-04EF-4CA2-8DF5-B84E9F8C34ABQ28116400-EC4B7F5D-E576-4BEA-907B-F5A81DB24670Q28181479-5A00386F-E7CC-4C70-893E-C7AF97F781DEQ28205720-2F1D97FB-2BD0-41C0-BA13-EF6FAA194489Q28209972-6119EC74-6BDB-47C5-987F-329DFA202F0EQ28214433-E3144C4F-289D-4B93-BC93-835100B620ECQ28243388-98BAAA64-CC9F-40AE-B507-6DD5FB1748E5Q28744484-FA4D6E24-5332-48FA-90FB-2BA9D7698DCEQ30476988-B1BB3AE2-8B89-46C8-B690-17E6703A7406Q30665275-3CDF4367-DDD2-4A42-8076-0EB4278A241BQ31010282-C9EDC2F9-8DB8-4D1B-9B9A-40273460BB82Q33187465-BC7FA92B-9315-49A1-AC4C-6339CBD937FCQ33236277-2472C0FD-DC0A-4E41-8049-268897F67010Q33303325-76B19ACD-2189-4D9D-8EDE-105F81A30490Q33382992-7D003C14-8759-4FA0-8B81-062BD4D7918FQ33490243-CB468FB1-3A2D-4C87-8F13-42EE4FE016A9Q33631854-31C39A8F-B20E-476F-BF27-0E4DC1776475Q33688037-2B62424D-FB96-42EC-825F-094C286A6C46Q33791476-57B44580-A9BA-482F-A64D-C1BA58B3AD3BQ33807043-EAF1B7AD-92CC-4C99-9CA0-6130BCE52EFDQ33904028-24775DFA-8C0E-4F4C-B5A3-37A0A9119453Q33912635-F57555BC-E239-4A04-AC82-BFAF22A3EE8AQ33912642-B845AAE8-C602-43FB-BFF2-93B91FAB0E7CQ34023384-67FFEE72-FD68-42B2-A6BC-5CDE0B6294F5Q34088438-4C83513D-5F6A-4F8E-8C64-C6A0A8A22816Q34122227-3A2ADA4D-0D0D-4680-A1D1-A6BA1DC55244Q34124112-F4DEFBED-A968-4BB9-BE7E-D06E44BE7948Q34135115-DAC00588-042B-496B-B3DB-41B665B8EAE9Q34144506-913C5CE4-AF0C-4100-8AFF-0F1E07942F5EQ34348731-C8117CBD-367D-4ECE-B272-C32DB306B4B4Q34401062-AA2B1C02-BF37-4BF9-BB7C-7000EAB82F37
P2860
26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
26S proteasomes and immunoprot ...... rsions of an antigenic peptide
@nl
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@ast
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en-gb
type
label
26S proteasomes and immunoprot ...... rsions of an antigenic peptide
@nl
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@ast
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en-gb
prefLabel
26S proteasomes and immunoprot ...... rsions of an antigenic peptide
@nl
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@ast
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en-gb
P2093
P2860
P356
P1433
P1476
26S proteasomes and immunoprot ...... sions of an antigenic peptide.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/20.10.2357
P407
P577
2001-05-01T00:00:00Z