The proteasome, a novel protease regulated by multiple mechanisms.
about
Ubiquitin-proteasome system involvement in Huntington's diseasecDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasomeIdentification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteinsIdentification of two proteins, S14 and UIP1, that interact with UCH37Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RAR gamma degradation and transactivation.Cells adapted to the proteasome inhibitor 4-hydroxy- 5-iodo-3-nitrophenylacetyl-Leu-Leu-leucinal-vinyl sulfone require enzymatically active proteasomes for continued survivalThe aryl hydrocarbon receptor mediates degradation of estrogen receptor alpha through activation of proteasomesPrediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approachDevelopmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomesDocking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entryNew Insights into the Function of the Immunoproteasome in Immune and Nonimmune CellsThe immunoproteasome and viral infection: a complex regulator of inflammationMultiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysisRPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit.Physical association of ubiquitin ligases and the 26S proteasome.Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and is required for its proteolytic cleavage.Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeastControl of CREB expression in tumors: from molecular mechanisms and signal transduction pathways to therapeutic targetTargeting of NEDD8 and its conjugates for proteasomal degradation by NUB1Pathogenesis of colorectal carcinoma and therapeutic implications: the roles of the ubiquitin-proteasome system and Cox-2Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1Differential roles of the COOH termini of AAA subunits of PA700 (19 S regulator) in asymmetric assembly and activation of the 26 S proteasomeConstruction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathwayModulation of p53 degradation via MDM2-mediated ubiquitylation and the ubiquitin-proteasome system during reperfusion after stroke: role of oxidative stressAltered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathwayDynamics of protein turnover, a missing dimension in proteomics.A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms.A yeast two-hybrid screen reveals that osteopontin associates with MAP1A and MAP1B in addition to other proteins linked to microtubule stability, apoptosis and protein degradation in the human brain.Randomized phase II trial of concurrent versus sequential bortezomib plus docetaxel in advanced non-small-cell lung cancer: a California cancer consortium trial.Proteasome activator enhances survival of Huntington's disease neuronal model cellsIdentification of a peptoid inhibitor of the proteasome 19S regulatory particle.Patented small molecule inhibitors in the ubiquitin proteasome systemProteasomes remain intact, but show early focal alteration in their composition in a mouse model of amyotrophic lateral sclerosis.Stress genes and proteins in the archaea.Aging is not associated with proteasome impairment in UPS reporter mice.Usa1 protein facilitates substrate ubiquitylation through two separate domainsNew targets for the treatment of follicular lymphoma.Mild heat stress stimulates 20S proteasome and its 11S activator in human fibroblasts undergoing aging in vitro.How cells use proteolysis to control their growth.
P2860
Q21129327-E1E49F53-0CC4-42A1-A768-5C553A6E017DQ22253889-FED78F27-051B-452C-86CD-D155193E2DBAQ22254027-A05E504A-4ABD-444C-9A08-85C8954906EAQ24290789-85CD774D-3FC3-4FC5-A4C4-452E5C93D0B4Q24301267-6863A726-3556-4E6F-974D-3D7AF9923C45Q24542503-3A0014AD-8EED-4EB5-89E2-5742D0671222Q24550565-482E3816-36C3-4127-AE2D-C0B3410322FBQ24621595-D9C074CC-00A9-4053-BC04-80FF465D5565Q24630449-BBBA861C-A8CA-4921-9DA4-8E4C8F3CFBC2Q24674433-4340813A-71ED-451C-B050-2B2849871AE9Q26774372-1974E43C-063D-4847-9BAA-FE377E315E2CQ27694656-52B91AF1-D394-4349-B5A7-5331D172C8D5Q27931879-56A438BB-462E-4724-9CEA-5C9EE3030231Q27933746-845F9F23-7455-47A4-8B87-C33E97912D53Q27935257-A432A612-4200-43B1-A601-4954511990EEQ27935670-87C32120-CAE7-46F3-8E3C-F60F066945E3Q27938567-D4E7207D-0682-430A-9577-FCF15AD4415DQ28070887-55260844-28E8-4271-9452-01B278CA6130Q28190234-443DCC54-ED02-4CED-974D-F6CB8E55CE20Q28209990-D04697A0-2C89-4AC7-A28B-B8ACD079E2E1Q28261510-4EC8AB8C-6E87-42F1-93E8-A9A9CE92DA84Q28294192-D4202C88-C8C2-442F-8F64-945DA3E21182Q28590671-0693F55E-B0CD-4698-806F-493841357CA7Q28593530-96829D41-998C-43BC-97DF-1A49CE517D99Q28593574-5D75CD56-DC45-48CE-8216-198D5B9E6F80Q30862513-864278FB-04C9-4975-BC4A-487012008B54Q30883536-D537887A-60B1-42F1-A502-78F14D74A763Q31026772-0A865D8A-2518-49C1-8259-362709E3E389Q31071712-77AA5097-9328-49BF-9333-61753F5D073EQ33159653-D9DD3662-A453-4639-A199-5F7AD18F8424Q33275949-19479392-24CC-48D4-B5C3-DCFC3967DE90Q33286169-8706BDC9-5687-403F-BA71-4F9A58EEB3DBQ33307875-BB077F28-3BFD-40A6-B967-B56272E03798Q33322191-62C570D7-F2CA-41A2-B4A9-F69A5CC57A73Q33334155-1963C82C-25D3-46C8-BBF6-4F477E08DE39Q33466066-079A684A-AFA4-43D6-9D74-70E953C79E64Q33515572-65A29C4C-B59D-41FF-9093-1F1DDD1E3336Q33587396-7E876C66-FF38-4C40-8D0F-773BD236A307Q33716925-5DA4E86B-4D39-4903-9F5C-A92C8CE851F4Q33833006-A5DC15F3-0C2B-41A5-B164-D1D5EB223452
P2860
The proteasome, a novel protease regulated by multiple mechanisms.
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The proteasome, a novel protease regulated by multiple mechanisms.
@ast
The proteasome, a novel protease regulated by multiple mechanisms.
@en
type
label
The proteasome, a novel protease regulated by multiple mechanisms.
@ast
The proteasome, a novel protease regulated by multiple mechanisms.
@en
prefLabel
The proteasome, a novel protease regulated by multiple mechanisms.
@ast
The proteasome, a novel protease regulated by multiple mechanisms.
@en
P2860
P356
P1476
The proteasome, a novel protease regulated by multiple mechanisms.
@en
P2093
DeMartino GN
Slaughter CA
P2860
P304
22123-22126
P356
10.1074/JBC.274.32.22123
P407
P577
1999-08-01T00:00:00Z