about
A heterodimeric complex that promotes the assembly of mammalian 20S proteasomesHomeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient miceA novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomesA ubiquitin ligase complex assembles linear polyubiquitin chainsInvolvement of linear polyubiquitylation of NEMO in NF-kappaB activationAssembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperonesProteasome activator PA28gamma-dependent nuclear retention and degradation of hepatitis C virus core proteinCHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic responseA mutation in the immunoproteasome subunit PSMB8 causes autoinflammation and lipodystrophy in humansDevelopmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomesCritical role of PA28 in hepatitis C virus-associated steatogenesis and hepatocarcinogenesisInvolvement of the PA28 -Dependent Pathway in Insulin Resistance Induced by Hepatitis C Virus Core ProteinCrystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomesCrystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domainAn inhibitor of a deubiquitinating enzyme regulates ubiquitin homeostasis.Regulation of CD8+ T cell development by thymus-specific proteasomesLoss of autophagy in the central nervous system causes neurodegeneration in miceImmunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta.PAC1 gene knockout reveals an essential role of chaperone-mediated 20S proteasome biogenesis and latent 20S proteasomes in cellular homeostasisImpairment of starvation-induced and constitutive autophagy in Atg7-deficient miceA human PSMB11 variant affects thymoproteasome processing and CD8+ T cell production.Splice acceptor site mutation of the transporter associated with antigen processing-1 gene in human bare lymphocyte syndromeStructure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targetsDorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity.Activity-based profiling reveals reactivity of the murine thymoproteasome-specific subunit beta5tCooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes.Molecular mechanisms of proteasome assembly.CHIP: a quality-control E3 ligase collaborating with molecular chaperones.Proteasome assembly defect due to a proteasome subunit beta type 8 (PSMB8) mutation causes the autoinflammatory disorder, Nakajo-Nishimura syndrome.Control of AIF-mediated cell death by antagonistic functions of CHIP ubiquitin E3 ligase and USP2 deubiquitinating enzyme.The thymic cortical epithelium determines the TCR repertoire of IL-17-producing γδT cells.Redundant Roles of Rpn10 and Rpn13 in Recognition of Ubiquitinated Proteins and Cellular Homeostasis.Sirt1-deficiency causes defective protein quality controlThymoproteasomes produce unique peptide motifs for positive selection of CD8(+) T cells.Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse developmentTwo distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processingThymic nurse cells provide microenvironment for secondary T cell receptor α rearrangement in cortical thymocytes.Multiple chaperone-assisted formation of mammalian 20S proteasomes.Proteasome dysfunction mediates obesity-induced endoplasmic reticulum stress and insulin resistance in the liverTCR affinity for thymoproteasome-dependent positively selecting peptides conditions antigen responsiveness in CD8(+) T cells.
P50
Q24292874-3843DBB4-F8EF-454F-810B-C859C7E08ED6Q24303752-635B7661-EEA4-447C-BF4E-E7AFA0511188Q24304237-B2AA2E94-44EA-41E1-AC0D-F8640CCA8ABDQ24305030-80661195-1BE1-4EC8-999E-81C0A32BED90Q24315943-00ACABC3-AC8E-4E43-A0F8-582C96300C52Q24316277-5CD03496-B780-43F9-BC27-30DC48F21A8CQ24322067-675C873E-9DCB-49D2-AF67-A68ED470A742Q24336920-68ADF758-FEDE-494E-8B2C-182ACE9B20D0Q24337054-D6B41D5E-729B-4664-A27A-B5346FDC4A46Q24630449-FAF5EED7-6EBA-4042-9CA5-DBB4DFB81030Q27477993-A76836F8-E8A8-4AC1-98DD-DA3BB9161918Q27478049-7F7565CF-9C7E-402E-9E3B-28E0C6321129Q27649865-CC36E536-AE33-4DDD-856C-8535D3ACCCEBQ27657818-9F7DF3B3-65B8-484E-AD4D-EE90D42E3D1AQ27936595-EF57E84F-F9D5-4CB5-A37A-B7410AAB89FDQ28116400-C357764B-1EEE-4428-AE5B-2F4300EC89B7Q28131804-AA0AD66F-D38A-4358-BB68-BB8BCCFEB621Q28363065-4354F2BC-9AD8-48C4-8B41-A24738BDB0E7Q28586356-577CD156-E408-4315-BCCF-6B6552B1D632Q28588080-B4D8A0FA-6195-44F9-8A74-8E6CC6B2C642Q33703233-3DBF9EA1-DC2F-4F22-9F1A-0A17E226428EQ33843690-4ED4ED56-7721-4814-8A58-B534665C041CQ33862782-F022B6FD-36B3-4F70-AE57-487E6D7CE543Q34141572-7AFC128E-59A9-4331-A0E0-CAE02F3FBC7CQ34575522-12D34FDE-E1C2-4ED0-B1FB-B6FCA13E547BQ34594682-6ED1B877-7ABC-4109-9E2D-AB7D648B59A8Q34928594-1BD1FB0C-8522-4E0C-95A3-DB00C07A735BQ35097617-91C1451B-1AA5-41D8-B496-5F44871CF3CAQ35202606-4DE3BF80-6EA4-415C-9AA1-B144F79EA511Q35210599-682C1192-42BB-4DE7-8006-2B7E11BC0400Q35595498-BF0CDCC2-4BF8-4712-A287-911133AD0B97Q35723276-4E68E662-317C-4CBF-B748-7DA37F9CD4DBQ35898247-D4D0EB17-5E0B-4657-AA45-11C65FD03667Q36018570-8E7A262F-8C6C-4503-9395-48A1C77111C2Q36176652-9312BB8C-862F-4C9E-971C-EE6B76C2BDEBQ36370830-F4F4A724-AED7-497E-A693-70098BB5D510Q36483791-DBE0C572-6BA4-41F6-A356-1AB28C6F543CQ36497593-B6571D0B-493F-44A0-9A34-274567CBA76AQ36635369-9B48EB86-3B86-403D-A5F1-7C17BF8F0D01Q36737068-E92CC854-0F88-4C82-B27E-355122CD524E
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Shigeo Murata
@ast
Shigeo Murata
@en
Shigeo Murata
@es
Shigeo Murata
@nl
Shigeo Murata
@sl
type
label
Shigeo Murata
@ast
Shigeo Murata
@en
Shigeo Murata
@es
Shigeo Murata
@nl
Shigeo Murata
@sl
prefLabel
Shigeo Murata
@ast
Shigeo Murata
@en
Shigeo Murata
@es
Shigeo Murata
@nl
Shigeo Murata
@sl
P106
P21
P31
P496
0000-0002-3177-3503