The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo. - Wikidata - awgldk - TriplyDB

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

http://www.wikidata.org/entity/Q36591894

about

Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT Transcriptional activation of mouse cytosolic chaperonin CCT subunit genes by heat shock factors HSF1 and HSF2 Insertional mutation of the murine kisimo locus caused a defect in spermatogenesis Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT micro-complexes.Structure 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 beta Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells Activities of the chaperonin containing TCP-1 (CCT): implications for cell cycle progression and cytoskeletal organisation Chaperonin filaments: the archaeal cytoskeleton?Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin Chaperonin-mediated folding of actin and tubulin Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins Identification and functional analysis of healing regulators in Drosophila Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system Modulation of tubulin polypeptide ratios by the yeast protein Pac10p A novel protein complex promoting formation of functional alpha- and gamma-tubulin.Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells Slow axonal transport of the cytosolic chaperonin CCT with Hsc73 and actin in motor neurons Chaperonin contributes to cold hardiness of the onion maggot Delia antiqua through repression of depolymerization of actin at low temperatures.Growth hormone and gene expression of in vitro-matured rhesus macaque oocytes Gene expression profile in hereditary transthyretin amyloidosis: differences in targeted and source organs Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics.Identification of obscure yet conserved actin-associated proteins in Giardia lamblia.Chaperonin containing T-complex polypeptide subunit eta (CCT-eta) is a specific regulator of fibroblast motility and contractility CCT chaperonin complex is required for the biogenesis of functional Plk1.Tubulin folding cofactor D is a microtubule destabilizing protein.A systematic screen for tube morphogenesis and branching genes in the Drosophila tracheal system.Expression of mRNA for the t-complex polypeptide-1, a subunit of chaperonin CCT, is upregulated in association with increased cold hardiness in Delia antiqua.MALAT-1 enhances cell motility of lung adenocarcinoma cells by influencing the expression of motility-related genes.Caenorhabditis elegans chaperonin CCT/TRiC is required for actin and tubulin biogenesis and microvillus formation in intestinal epithelial cells Exchange of genetic markers at extremely high temperatures in the archaeon Sulfolobus acidocaldarius Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro.Cloning and expression of rabbit CCT subunits eta and beta in healing cutaneous wounds.Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain.The cytosolic chaperonin CCT/TRiC and cancer cell proliferation.Proteomic profiling of rabbit embryonic stem cells derived from parthenotes and fertilized embryos.Structure and function of a protein folding machine: the eukaryotic cytosolic chaperonin CCT.

P2860

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P2860

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

http://www.wikidata.org/entity/Q36591894

description

1993 nî lūn-bûn

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1993年の論文

@ja

1993年論文

@yue

1993年論文

@zh-hant

1993年論文

@zh-hk

1993年論文

@zh-mo

1993年論文

@zh-tw

1993年论文

@wuu

1993年论文

@zh

1993年论文

@zh-cn

name

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@ast

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@en

type

label

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@ast

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@en

prefLabel

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@ast

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

@en

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P356

PNAS.90.20.9422

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo

@en

P2093

G W Farr

http://www.w3.org/2001/XMLSchema#string

H Sternlicht

http://www.w3.org/2001/XMLSchema#string

J K Driscoll

http://www.w3.org/2001/XMLSchema#string

M B Yaffe

http://www.w3.org/2001/XMLSchema#string

M L Sternlicht

http://www.w3.org/2001/XMLSchema#string

P2860

The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes

TCP1 complex is a molecular chaperone in tubulin biogenesis

T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

The t complex polypeptide 1 (TCP-1) is associated with the cytoplasmic aspect of Golgi membranes

Protein folding in the cell

Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

Mitochondria, molecular chaperone proteins and the in vivo assembly of microtubules.

Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells.

Assembly associated with the cytomatrix.

Sequence and structural homology between a mouse T-complex protein TCP-1 and the 'chaperonin' family of bacterial (GroEL, 60-65 kDa heat shock antigen) and eukaryotic proteins.

P304

9422-9426

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scholarly article

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10.1073/PNAS.90.20.9422

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20

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90

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15092728

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8105476

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P932

47580

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