Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase.
about
cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasomeNewly identified pair of proteasomal subunits regulated reciprocally by interferon gammaEvolutionary families of peptidasesMolecular and biotechnological aspects of microbial proteasesAnalysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysisArchaea and the prokaryote-to-eukaryote transitionOrthoParaMap: distinguishing orthologs from paralogs by integrating comparative genome data and gene phylogeniesThe active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing.Proteasome assemblyThe major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processingPhosphorylation of ATPase subunits of the 26S proteasomeIn vivo assembly of the proteasomal complexes, implications for antigen processingInhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystinChemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasomeBiochemical analysis of the 20 S proteasome of Trypanosoma brucei.alpha5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings.Why does threonine, and not serine, function as the active site nucleophile in proteasomes?Cloning and sequence analysis of a cDNA clone from Arabidopsis thaliana homologous to a proteasome alpha subunit from Drosophila.Archaebacteria then ... Archaes now (are there really no archaeal pathogens?)The proteasome: a macromolecular assembly designed for controlled proteolysisThe proteasome activator 11 S REG (PA28) and class I antigen presentationHalophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysisPuromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization.Purification and Characterization of a Proteasome from the Hyperthermophilic Archaeon Pyrococcus furiosus.Delineation of the subunit composition of human proteasomes using antisera against the major histocompatibility complex-encoded LMP2 and LMP7 subunitsMutations in PRG1, a yeast proteasome-related gene, cause defects in nuclear division and are suppressed by deletion of a mitotic cyclin geneThe second capsule gene of cryptococcus neoformans, CAP64, is essential for virulence.Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus.Regulation by proteolysis: energy-dependent proteases and their targets.Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors.Experimental studies defining omega-3 fatty acid antiinflammatory mechanisms and abrogation of tumor-related syndromes.Protein Expression of Proteasome Subunits in Elderly Patients with Schizophrenia.cDNA cloning of rat proteasome subunit RC10-II, assumed to be responsible for trypsin-like catalytic activity.The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.The roles of the proteasome pathway in signal transduction and neurodegenerative diseases.ATP-dependent proteases differ substantially in their ability to unfold globular proteinsArchaeal proteasomes and sampylation.A voyage to the inner space of cells.Proteasomes: multicatalytic proteinase complexesDisplacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex.
P2860
Q22253889-4DAE2608-A88F-4F15-BD43-884EE27F5EFDQ24322943-79D75AB7-1E07-4A66-A05C-472F67D752CFQ24527684-063D6C43-D8A0-4A10-8C0B-68093CF33E42Q24548591-625BC0FD-8999-4627-8F07-1A8D3AD03A9FQ24561722-CE0E4B05-E869-4382-B21A-55B5EC82F03DQ24643523-FA590078-324D-4C84-8C44-5EAA345105D0Q24801185-34FADADE-5E7B-408C-82B2-E2E10044329BQ27939678-53594B79-B2A3-4F32-A4BB-21D5F1B92FA9Q28245575-B427110A-BB5C-42E6-9E81-123ED6A7D5F0Q28267460-006B1DD8-49C1-4A9E-8D2E-FDF9C4321244Q28278235-A76EECAD-8E69-41A3-855B-D2D4864E633DQ28285019-CE54CD20-BA86-4479-BE79-C3080D777CCEQ28300614-A8583265-0FF9-473C-8FEB-0F6395A8B48BQ28346508-2AA188B7-3579-46C9-B7EC-6D9EBFEEC8CDQ30724510-0FDE5A0A-1F2F-4D87-A722-762FD0C897C6Q30814900-70BDBF77-C8CF-448C-9565-695851CF419CQ30870481-77E50DED-53F7-4746-9AD6-AED820868D3EQ33203244-FEA7A6A7-F83E-42D8-8B58-059CF237A97AQ33658157-7516096D-CE02-4773-B287-3A4CBE72C5F4Q33785021-EA17C996-6361-428E-ABD0-74DFB4CEA04DQ33796158-778312F0-7200-4F0D-8C4C-EFAB11008DFBQ33993001-2467CD19-B8E8-45C0-B573-6DDC94F6C08CQ34298336-757626F3-EE04-454A-9D1C-DCD5EA06FBFAQ34424057-6BCCF8C5-81BA-4B88-92B6-0C3C4707C4FBQ34946059-A7C9C0C0-9849-4BE7-B785-52EC9FDFA07BQ35088782-84FD90A8-8854-4122-8D68-189A3E054C46Q35495143-63B584E2-351E-464C-99E5-67A8CE781587Q35606572-806B16BE-0D74-4A02-A265-FB82EAA89BA6Q35655403-9E355A7A-F4D7-42F4-9DB2-532BF700151DQ36237082-C6ABA91B-024B-48E6-9E14-008347F163D8Q36278315-2D1CC261-6E76-468C-BE37-42CDB96B5DE4Q36449744-77184FE1-598F-495E-AE96-37B83B2EB7F2Q36759968-5954276B-90F0-48FE-9F5F-3DBCAD666DDAQ36862775-62582F9D-4154-418E-9852-0C1A7C4AE08CQ37171851-DC4D4DF0-95B0-4C30-BDAD-049154A2D18AQ37254059-25EB6AC6-0368-4C6A-956D-21A118667867Q37606188-76550D4C-E847-4B84-B450-14D7DC3AA135Q38575440-7D1B783A-978A-4812-8B3A-79D77608FF1BQ40486138-3C678EA5-578B-4B38-A342-1E0BC9969287Q40792545-87461501-349D-4D55-A49A-5ADDFC4CF747
P2860
Primary structure of the Thermoplasma proteasome and its implications for the structure, function, and evolution of the multicatalytic proteinase.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
Primary structure of the Therm ...... the multicatalytic proteinase.
@en
Primary structure of the Therm ...... the multicatalytic proteinase.
@nl
type
label
Primary structure of the Therm ...... the multicatalytic proteinase.
@en
Primary structure of the Therm ...... the multicatalytic proteinase.
@nl
prefLabel
Primary structure of the Therm ...... the multicatalytic proteinase.
@en
Primary structure of the Therm ...... the multicatalytic proteinase.
@nl
P2093
P356
P1433
P1476
Primary structure of the Therm ...... the multicatalytic proteinase.
@en
P2093
P304
P356
10.1021/BI00119A004
P407
P577
1992-02-01T00:00:00Z