Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.
about
Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactorHuman TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroMechanism of folding chamber closure in a group II chaperoninContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangementCrystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding CycleCrystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulinDual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin ChamberCryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.Mechanism of nucleotide sensing in group II chaperoninsThe molecular architecture of the eukaryotic chaperonin TRiC/CCTA ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesisDefining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesDynamics, flexibility, and allostery in molecular chaperoninsThe structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCTAssisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteinsxTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometryJADAS: a customizable automated data acquisition system and its application to ice-embedded single particles.Multiscale natural moves refine macromolecules using single-particle electron microscopy projection imagesStructure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy.Archaeal-like chaperonins in bacteria.Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solutionSequential action of ATP-dependent subunit conformational change and interaction between helical protrusions in the closure of the built-in lid of group II chaperonins.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling.Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT.A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin.Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCTHuman CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Hardware-based anti-Brownian electrokinetic trap (ABEL trap) for single molecules: Control loop simulations and application to ATP binding stoichiometry in multi-subunit enzymes.Chaperonin-Dendrimer Conjugates for siRNA Delivery.Insights into chaperonin function from studies on archaeal thermosomes.The Mechanism and Function of Group II Chaperonins.The human mitochondrial Hsp60 in the APO conformation forms a stable tetradecameric complex.Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.p90 ribosomal S6 kinase and p70 ribosomal S6 kinase link phosphorylation of the eukaryotic chaperonin containing TCP-1 to growth factor, insulin, and nutrient signaling.
P2860
Q24293412-059CEE89-76AA-4A05-9216-4790E4439686Q24299586-5638F37D-982D-42D9-8086-8DA0F1DAAB83Q24631877-CF68C9E7-CBA5-49FF-89F5-8F66261F35B1Q26777412-9105378C-8B6A-477E-ACC9-89B546A454E6Q27319527-4EE18A74-C398-44F7-8802-20C3C7481423Q27660079-D3A48B1A-E787-4B67-9806-D81EFD17DC1AQ27662675-58AFB931-C300-454B-8A63-7FBD416F0E94Q27666364-B4C244E6-58DA-4AAF-96CD-E889DD7B0C69Q27666606-63B69078-4F1B-4798-B684-1D58FD86EBA5Q27667812-5CCAB03B-F145-43B6-8637-C6BA9D4A9D58Q27675341-8959DCCC-6EDD-4E59-9176-96D46D20AF0EQ27676366-307BB935-18D7-4B5C-9956-18594EEC8A0BQ27678510-B255539F-6832-401A-B36F-E263926A5ADFQ27931602-44FD5E81-77F3-4FB2-929F-377F89B06686Q27967631-760908E6-88F4-4E35-8CD1-E2D868A242ADQ28087481-ED22CDEC-B1A4-47D6-9E9E-F5E98B3F1A3BQ28590650-D24C89EB-E9EF-4107-9F2F-8C9ABF0D4675Q28659980-D4344024-80A3-46C8-B73F-BCFCFBCBC65FQ28828370-A0DC630F-0488-4B7E-9946-8F2FAA7A65B4Q30485768-060F2916-1747-4255-BD4B-51F574C5988CQ30517942-90A841A7-2A17-4F97-9546-5B08EB81FF88Q33807906-0CE1BE5E-EB60-4BC8-BE8E-E3384F01D3D5Q34283382-A7412333-6BC5-4AAF-982A-64B6CE0BA2E3Q34377701-E3B15253-CEE0-4406-B283-A4EB4DFF0083Q35345051-A56FF5D2-8DDD-4123-A2C0-4837993D2B48Q35676893-1831CAE7-E497-467F-A2FC-79E42EF4C32CQ35706831-9E678FA0-0C9D-47F5-B684-0D3B45CC3B04Q35779424-C3878168-0285-42DF-B012-7D4F4940A347Q36504252-7CC2570E-6625-46B6-8F3B-16A7FCD6AC34Q36528641-BE24D006-10CF-4444-8220-14878C6776E2Q36772307-678695CE-E587-4300-AB4D-B24CB2951DA4Q36897533-96477476-2A27-426D-A6F6-9872403FF51DQ36929097-F4463ECB-22A3-4990-A138-860DEBD2E7D7Q37380508-19183EBE-88E2-4436-9663-FC502859F93FQ37394496-ABF3498F-215A-48CE-AB62-CB80E04980D7Q37832255-7391A6F6-FD60-4321-BA85-8FA6E61BAEC5Q38455984-1035DB03-2C66-4584-A338-ED1B775A81F3Q38736673-C051BBFB-F45E-4766-BB49-C89C7C24B2FAQ39586605-C6D3E15A-4077-4360-8515-7363BF1EAB36Q39866337-8EDE3C79-899C-447C-8C15-E41466775B9B
P2860
Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Essential function of the buil ...... otic and archaeal chaperonins.
@ast
Essential function of the buil ...... otic and archaeal chaperonins.
@en
type
label
Essential function of the buil ...... otic and archaeal chaperonins.
@ast
Essential function of the buil ...... otic and archaeal chaperonins.
@en
prefLabel
Essential function of the buil ...... otic and archaeal chaperonins.
@ast
Essential function of the buil ...... otic and archaeal chaperonins.
@en
P2093
P2860
P356
P1476
Essential function of the buil ...... otic and archaeal chaperonins.
@en
P2093
Charles Parnot
Christopher R Booth
Stefanie Reissmann
P2860
P2888
P304
P356
10.1038/NSMB1236
P577
2007-04-29T00:00:00Z