Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
about
Estrogen receptor of primary breast cancers: evidence for intracellular proteolysisClioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells.Regulation of IkappaBalpha function and NF-kappaB signaling: AEBP1 is a novel proinflammatory mediator in macrophagesA mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell divisionHuman Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysisCritical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portionCbl-mediated degradation of Lyn and Fyn induced by constitutive fibroblast growth factor receptor-2 activation supports osteoblast differentiationThe conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell deathPhosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-induced RAR gamma degradation and transactivation.CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3pYeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent activation of transcription by human progesterone and glucocorticoid receptorscDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativityNewly identified pair of proteasomal subunits regulated reciprocally by interferon gammaMammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexesCharacterization of a human ubiquitin-conjugating enzyme gene UBE2L3Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalphaUBPY: a growth-regulated human ubiquitin isopeptidase.The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factorPhosphorylation of nuclear MyoD is required for its rapid degradation.Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virusA novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory proteinConjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus.Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradationSupramolecular complex formation between Rad6 and proteins of the p53 pathway during DNA damage-induced responseAnalysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysisActivation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin EDifferential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IkappaBalpha and beta-catenin and stimulates IkappaBalpha ubiquitination in vitroThe N-end rule: functions, mysteries, usesEGCG, green tea polyphenols and their synthetic analogs and prodrugs for human cancer prevention and treatmentNp95 is a histone-binding protein endowed with ubiquitin ligase activityYeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review seriesDNA immunization: ubiquitination of a viral protein enhances cytotoxic T-lymphocyte induction and antiviral protection but abrogates antibody inductionThe Ras target AF-6 is a substrate of the fam deubiquitinating enzymeMolecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope associationCharacterization of alternatively spliced products and tissue-specific isoforms of USP28 and USP25
P2860
Q21195159-E4685084-1626-4550-9377-DAAA4E1D0C2DQ21195237-24DE5023-6375-45A5-A18C-94384B782640Q21296830-F93FACDA-638F-4155-BC8C-2AA5E6AAEA77Q22009029-48C0B35E-A436-4FAC-9475-A75B7B7B3A1DQ22010136-1B2423B0-4A32-42E9-97F6-A033E4169F7EQ24293712-076B3766-03B7-46CB-9D69-4A520C64A7D3Q24296414-8F4C29D9-7063-42E4-8E6F-C680B96DFE40Q24297104-40C530E1-4B0F-4045-BC18-D58AC5D73EF6Q24298384-26CCCC65-F5C1-413D-8945-923C336ED6D0Q24301267-6D297192-370A-44AB-88A9-F2062F5D68BAQ24308679-AF642E92-7DE5-4DAD-ABA7-E38E1D30E6C8Q24316214-620A7DF2-AF4F-418D-B95E-962D8982137EQ24318067-C3B66EE5-EB19-455E-810F-5B644D795691Q24321751-32AEC541-A08C-437A-80E5-D790BDE87042Q24322943-8330C010-737F-4695-97E4-E9C8D9F3B0ABQ24324511-B6B0EC2C-AA83-4501-B33E-E79B572405B9Q24324671-CCC0F7EA-ACD9-479D-A1AD-A01232516995Q24329214-82A97A20-81D9-4BC6-A914-CEFE2751E2E6Q24336064-37CC6B86-C88E-4939-B2C3-3811FFD4CC2DQ24336424-4E18EB15-A441-4BB0-A9F7-730C2DBE1D8DQ24522630-876EBD89-1027-466E-9704-B7ED49991A9CQ24523226-595D94AF-3BC7-4976-8738-BD3447A7DD24Q24532134-8E646072-37B0-4E9C-930D-4F6748CAAF2EQ24532901-2D7C6C8B-0748-46C8-8B8B-46F3E3BF649DQ24533384-4EEE9499-9202-4727-889D-DE4219F0AA23Q24551106-75002548-C617-4D98-B933-2F0794C262D4Q24561722-476A9697-2AA2-4636-971E-F529E6E2EEE3Q24562111-0CA6F395-5B38-45D1-A396-B44B8BC96E7CQ24563324-3DA2EFAB-31CF-44ED-B834-BB59D623B00BQ24597101-83A21FAE-1E78-4169-A2E8-0AE939A97B8AQ24608829-3A04FD5B-0143-4D36-A1E4-E66BEA166E25Q24609395-792DAD68-9EA1-4EAE-BF49-B5DF7EB33AB7Q24616455-B683DC39-8047-4523-BB24-EF662FB3FEA8Q24629660-76123D57-D0C1-4D8E-8171-39537CA5648FQ24654196-5AB05396-7E05-4ABF-BD22-E620FE8F0BEAQ24655287-D72B435A-F63F-4169-98A8-E2005EEE52C2Q24671114-328D8E01-E1CB-422A-8937-027CE6D851ACQ24682859-FFED67B0-8F9B-4FEE-B2D2-5D93DA5383ACQ24683718-0357CFF9-8044-4021-86AB-71AC8C8CB0C1Q24805911-E464A06E-5566-4C09-95AA-6AB9FD0C2FDD
P2860
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
@en
type
label
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
@en
prefLabel
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
@en
P1476
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation.
@en
P2093
Hochstrasser M
P304
P356
10.1016/0955-0674(95)80031-X
P577
1995-04-01T00:00:00Z