T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
about
Maturation of human cyclin E requires the function of eukaryotic chaperonin CCTHuman TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroA 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteinsElucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gammaStructure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 betaTwo yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivoEukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteinsComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsPrefoldin-nascent chain complexes in the folding of cytoskeletal proteinsContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisFormation and function of the Rbl2p-beta-tubulin complex.Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNAProteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasisAntibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testisThe proteome landscape of Giardia lamblia encystationThe chaperonin containing TCP1 complex (CCT/TRiC) is involved in mediating sperm-oocyte interactionLarge-scale proteome comparative analysis of developing rhizomes of the ancient vascular plant equisetum hyemaleDopamine-induced recruitment of dopamine D1 receptors to the plasma membrane.Erianthus arundinaceus HSP70 (EaHSP70) Acts as a Key Regulator in the Formation of Anisotropic Interdigitation in Sugarcane (Saccharum spp. hybrid) in Response to Drought Stress.Multigene expression of protein complexes by iterative modification of genomic Bacmid DNAChaperone rings in protein folding and degradation.Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Type D retrovirus Gag polyprotein interacts with the cytosolic chaperonin TRiC.An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytesFunction in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunitsExpression of mRNA for the t-complex polypeptide-1, a subunit of chaperonin CCT, is upregulated in association with increased cold hardiness in Delia antiqua.Heat shock proteins: molecular chaperones of protein biogenesis.Heat shock proteins and cardiovascular pathophysiology.Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro.Autoantibodies against chaperonin CCT in human sera with rheumatic autoimmune diseases: comparison with antibodies against other Hsp60 family proteins.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.A yeast TCP-1-like protein is required for actin function in vivoChaperone-assisted folding of newly synthesized proteins in the cytosol.Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulinA eukaryotic cytosolic chaperonin is associated with a high molecular weight intermediate in the assembly of hepatitis B virus capsid, a multimeric particle.A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin.MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains.The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
P2860
Q22008018-142FDC03-A3B2-4E18-89CB-DCC4A59492D6Q24299586-E4E35A97-022F-4D64-AD5C-C560EAC6E0ACQ24310269-76E9BA80-9DA2-48E3-BF9A-77C3765AB862Q24532436-5C2152EE-527E-491E-A811-8CB40CB438F1Q24534148-40566A72-CA11-48A8-9468-4A1177D3A1D3Q24539197-5479132B-6633-49FA-A400-1451152C671BQ24563795-5680158E-2AE9-45C0-8F97-A5EE731D1E58Q24563986-48041F3B-12A2-4B73-B0D2-5C646A6EEF62Q24622449-78463197-0551-4458-B4EA-2888FE4BA0C0Q24653464-E0501679-153C-4797-B306-2AC7B99E2AD4Q24682236-ECAE0095-0058-4CD6-8A86-738E1CBF78EEQ26777412-DA197B41-49B7-477D-85A5-59EBCAEE1271Q27931582-A6D35DBA-83F3-40CF-A552-1C8958AEC07BQ28116110-7F5BCD48-16E4-4582-8C89-7785A5A35DEEQ28286034-BBDB5EC6-1140-483F-ADAE-E96820FF76B8Q28511008-148A4723-242C-4DFD-9F5E-26F5D241E701Q28538118-412F40A6-695A-4704-973E-42EDFEF45E07Q28586695-29D9C28B-49EC-4FCB-96EB-20082B31F0E5Q28727999-E9C27336-15FC-4994-A4AB-862C04527F1AQ30454416-5014BBAC-036F-404C-8754-990E6693DFD5Q30999743-85F48735-294F-4681-88E7-7AA1114AC7E9Q33499534-98CF80C1-DAB2-436F-B479-1C1E1321D440Q33740150-3C47C610-0CE8-4781-BC0F-13406D242B70Q33807906-AD43D3A4-15D1-47BE-AA3C-74E56765E15AQ33865019-27A8A8C2-2D3F-4170-AD49-ED531443D9D3Q33899922-374B4E0F-B389-4805-A007-45E620055DF2Q33938572-9AE7A7E3-5578-44FE-A2AF-BC76D3201CE5Q34020322-5CE5E74F-6DF5-4C4F-B7A5-E3FF13127177Q34351628-D9E3164B-5CD7-41E2-AE99-CEC5D567BCD8Q34388079-B4758DEA-A852-48BA-8148-A7649D7654D2Q34487798-80AF267D-ADB9-47A6-9F4B-6C018BFA3A6EQ35083722-4BF120EA-0C27-4FF7-BE25-D543E0D6B94EQ35706831-6E15DF86-C4F8-4150-A861-8DB77D5CC20DQ35763868-B8C5C6C5-AA6A-483A-B623-B3C729201E47Q36069355-C8EFE0A3-4E69-4DF7-A92F-552128EF5182Q36233504-C74EA82E-E851-4B88-AC29-460AD5C19817Q36234085-FE10262C-9AB3-43F9-90BF-2BF2DBA9BA47Q36234218-255213A7-C833-46D5-97F3-D287DF2F72F3Q36281080-2F86DAD6-8C61-4E26-ACB8-65B94611037CQ36327627-A8D4E623-AAA6-40AE-9556-D23E061FB6BD
P2860
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
description
1992 nî lūn-bûn
@nan
1992 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@ast
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@en
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@nl
type
label
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@ast
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@en
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@nl
prefLabel
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@ast
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@en
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@nl
P2093
P356
P1433
P1476
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
@en
P2093
P2888
P304
P356
10.1038/358249A0
P407
P577
1992-07-01T00:00:00Z
P6179
1048280434