Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins
about
Novel complex integrating mitochondria and the microtubular cytoskeleton with chromosome remodeling and tumor suppressor RASSF1 deduced by in silico homology analysis, interaction cloning in yeast, and colocalization in cultured cellsUXT is a novel and essential cofactor in the NF-kappaB transcriptional enhanceosomeUXT is a novel centrosomal protein essential for cell viabilityStructure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progressionThe Tim8–Tim13 Complex Has Multiple Substrate Binding Sites and Binds Cooperatively to Tim23Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneCrystal structure of an intramolecular chaperone mediating triple-beta-helix foldingThe N-terminal substrate-recognition domain of a LonC protease exhibits structural and functional similarity to cytosolic chaperonesPrefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates.The prefoldin complex regulates chromatin dynamics during transcription elongationSelective contribution of eukaryotic prefoldin subunits to actin and tubulin bindingPrefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin familiesIts substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domainsDEPDC1/LET-99 participates in an evolutionarily conserved pathway for anti-tubulin drug-induced apoptosis.Prefoldin 6 is required for normal microtubule dynamics and organization in Arabidopsis.Chaperone domains convert prolyl isomerases into generic catalysts of protein folding.Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei.Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes.Predicted highly expressed genes in archaeal genomes.Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications.Redox regulation of protein folding in the mitochondrial intermembrane space.Protein folding in the cytoplasm and the heat shock response.Getting a grip on non-native proteinsDynamic protein complexes: insights from mass spectrometry.Arabidopsis thaliana type I and II chaperoninsPrefoldin 5 is required for normal sensory and neuronal development in a murine model.Perspectives on the origin of microfilaments, microtubules, the relevant chaperonin system and cytoskeletal motors--a commentary on the spirochaete origin of flagella.Characterization of HKE2: an ancient antigen encoded in the major histocompatibility complex.Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.Prefoldin subunits are protected from ubiquitin-proteasome system-mediated degradation by forming complex with other constituent subunits.Art27 interacts with GATA4, FOG2 and NKX2.5 and is a novel co-repressor of cardiac genesFunctional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.New insights into the biogenesis of nuclear RNA polymerases?Misato Controls Mitotic Microtubule Generation by Stabilizing the TCP-1 Tubulin Chaperone Complex [corrected].Drosophila Mgr, a Prefoldin subunit cooperating with von Hippel Lindau to regulate tubulin stability.Interactions between folding factors and bacterial outer membrane proteins.
P2860
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P2860
Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins
description
2000 nî lūn-bûn
@nan
2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Structure of the molecular cha ...... ntacles with unfolded proteins
@ast
Structure of the molecular cha ...... ntacles with unfolded proteins
@en
Structure of the molecular cha ...... ntacles with unfolded proteins
@nl
type
label
Structure of the molecular cha ...... ntacles with unfolded proteins
@ast
Structure of the molecular cha ...... ntacles with unfolded proteins
@en
Structure of the molecular cha ...... ntacles with unfolded proteins
@nl
prefLabel
Structure of the molecular cha ...... ntacles with unfolded proteins
@ast
Structure of the molecular cha ...... ntacles with unfolded proteins
@en
Structure of the molecular cha ...... ntacles with unfolded proteins
@nl
P2093
P3181
P1433
P1476
Structure of the molecular cha ...... ntacles with unfolded proteins
@en
P2093
C Scheufler
M R Leroux
P304
P3181
P356
10.1016/S0092-8674(00)00165-3
P407
P577
2000-11-10T00:00:00Z