MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
about
The immunoproteasome and viral infection: a complex regulator of inflammationThe active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing.The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residuesIn vivo assembly of the proteasomal complexes, implications for antigen processingHLA class I binding motifs derived from random peptide libraries differ at the COOH terminus from those of eluted peptides.Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes.Identification and linkage of the proteasome activator complex PA28 subunit genes in zebrafish.Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors.IFN-beta mediates coordinate expression of antigen-processing genes in RSV-infected pulmonary epithelial cells.TAP1 down-regulation in primary melanoma lesions: an independent marker of poor prognosis.Mechanisms of antigen presentation.Human pathogen subversion of antigen presentation.The specificity of proteasomes: impact on MHC class I processing and presentation of antigens.Proteolysis and class I major histocompatibility complex antigen presentation.Proteasome inhibitors: from in vitro uses to clinical trials.Conformational constraints in protein degradation by the 20S proteasome.Beta 2 subunit propeptides influence cooperative proteasome assembly.Impaired expression of proteasome subunits and human leukocyte antigens class I in human colon cancer cells.Peptide motifs of the single dominantly expressed class I molecule explain the striking MHC-determined response to Rous sarcoma virus in chickens.Molecular characterization and expressional affirmation of the beta proteasome subunit cluster in rock bream immune defense.Resistance to malaria by enhanced phagocytosis of erythrocytes in LMP7-deficient mice.Tumor-specific shared antigenic peptides recognized by human T cells.Distinct proteasome subpopulations in the alveolar space of patients with the acute respiratory distress syndromeGeneration of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII.Association of LMP/TAP gene polymorphisms with tuberculosis susceptibility in Li population in ChinaThymoproteasomes produce unique peptide motifs for positive selection of CD8(+) T cells.Molecular machines for protein degradation.Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing.The production of a new MAGE-3 peptide presented to cytolytic T lymphocytes by HLA-B40 requires the immunoproteasomePotential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system.The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking peptide epitope.Antigen presentation machinery (APM) modulation and soluble HLA molecules in the tumor microenvironment: do they provide tumor cells with escape mechanisms from recognition by cytotoxic T lymphocytes?Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptideDiversity of proteasomal missions: fine tuning of the immune response.Genetics of proteasome diseases.TAA polyepitope DNA-based vaccines: a potential tool for cancer therapyInsights into the processing of MHC class I ligands gained from the study of human tumor epitopes.The role of the proteasome in the generation of MHC class I ligands and immune responses.Isolation and purification of proteasomes from primary cells.Standard and immunoproteasomes show similar peptide degradation specificities.
P2860
Q27694656-C413A775-8507-464F-9DB2-04C350488B5AQ27939678-03A748AE-520A-46DE-BC05-B4CCA77C33CBQ28115737-53C4475E-5999-4585-A7DC-F2078C05B326Q28285019-14BD1D2D-7317-414B-A18A-0A37FD4D78E9Q30442842-D2BFD9C4-675C-446C-980F-A54757A33075Q30598957-5BA7C81A-67B4-4495-BEEE-1408373F7CDEQ30878098-4B74BFE6-524C-421A-8135-82604A1F5230Q30983359-7D314472-DD9F-4D6A-B3AD-0A6DEEB938D7Q31834062-3CA46E79-B5E2-4217-BA42-BAD9E6305B14Q32159956-1D533873-7E56-4AA7-8078-B70ADE135B57Q33649805-05CCCF7B-D7AB-4198-8FD9-1805DB8F64CAQ33683402-0C3495EB-BD9F-4277-ADDD-3AFDC0BA25D5Q33815363-11F07118-CC2C-44AD-9F81-2F212484DC22Q33815369-6E4F1D31-11EF-4F86-8FDC-D34ECACA5615Q34052405-60321B51-BD19-4A8E-B077-C0052C6411CBQ34058982-6698C704-7D1C-4110-AF01-56F7155B2CABQ34161423-BAA37B0B-AC0F-498F-9E82-9F71A26DFAB3Q34169329-95525986-174A-4A07-8D79-64E1D706E6F4Q34334820-2C45D023-EEC6-4199-BCDE-93FD9CEDB2E6Q34421574-32047625-3735-4DB4-B00F-210619C7FB03Q34635361-FA86116C-AFF5-4463-A081-64D2CF073C1DQ35005926-A140878E-A085-49BC-8E67-097AF0052C9AQ35738931-BBF4D53D-B35E-4A06-B41A-15826F0EA924Q35821221-52A17FB0-353D-41C2-8E8D-B0EC57EDF99BQ35822689-0A0EFD28-BF57-429B-8ABB-779BE7291B1DQ36018570-D9F234ED-9447-4EF5-9DBA-2F40DE4E833EQ36023030-7A93B7DE-0A64-49D4-8E82-A434A099E894Q36266425-AC44CC6E-E19E-4F67-B0DC-5CA253018980Q36369920-3F60FBAB-7472-4182-8AB0-FC0F78E37703Q36380352-DC153F01-C7A7-433C-BEC3-F7D2B072C933Q36401780-AA0DC012-7115-467B-80D3-F74FA4FA681AQ36569023-F7F4DBF3-13FF-46A7-8DF7-6256A917DF74Q36597620-11B66C8E-9102-4CBD-A9B5-C842930AEB71Q36909248-A6BFBCB4-25F0-4838-B0BA-E18DA74F5D4BQ37483040-86009399-9A56-4B08-B8B1-69C1CD772E17Q37771268-EC8943A7-CAB8-4773-A002-2B7D02BE73FDQ37851050-223D7885-0E49-463B-9DEA-22E9355504BEQ37851052-83E1E234-3320-498F-8471-F8DB522981BFQ38264766-7B7AAEA5-2147-4FB3-96B5-01EBECBCD342Q38268527-5B6895BA-0651-4E48-A5C5-07BCF4CB6C3C
P2860
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature у вересні 1993
@uk
name
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@en
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@nl
type
label
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@en
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@nl
prefLabel
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@en
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@nl
P2093
P356
P1433
P1476
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
@en
P2093
P2888
P304
P356
10.1038/365262A0
P407
P577
1993-09-01T00:00:00Z
P6179
1035838378