(Q37608575)

English

Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineries

scientific article published on 06 January 2014

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scholarly article

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PMC publication ID

21 August 2017

Drosophila Spag is the homolog of RNA polymerase II-associated protein 3 (RPAP3) and recruits the heat shock proteins 70 and 90 (Hsp70 and Hsp90) during the assembly of cellular machineries (English)

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21 August 2017

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5

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13 June 2020

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13 June 2020

Edouard Bertrand

12

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13 June 2020

Andrey V Kajava

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Andrey V Kajava

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13 June 2020

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Nour El Houda Benbahouche

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13 June 2020

Ioannis Iliopoulos

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13 June 2020

István Török

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13 June 2020

Joachim Marhold

4

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13 June 2020

Robert Farkaš

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13 June 2020

Tore Kempf

8

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13 June 2020

István Kiss

11

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13 June 2020

Bernard M Mechler

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13 June 2020

Bérengère Pradet-Balade

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13 June 2020

Martina Schnölzer

9

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13 June 2020

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6 January 2014

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21 August 2017

Journal of Biological Chemistry

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13 June 2020

289

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13 June 2020

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13 June 2020

6236-6247

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13 June 2020

High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex

1 reference

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Drosophila Tel2 is expressed as a translational fusion with EpsinR and is a regulator of wingless signaling

1 reference

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Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition

1 reference

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Hsp110 is required for spindle length control

1 reference

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23 August 2017

C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances

1 reference

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23 August 2017

Structure of Minimal Tetratricopeptide Repeat Domain Protein Tah1 Reveals Mechanism of Its Interaction with Pih1 and Hsp90

1 reference

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CRM1 controls the composition of nucleoplasmic pre-snoRNA complexes to licence them for nucleolar transport

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CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for mTOR and SMG1 stability

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High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes

1 reference

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Molecular cloning of novel Monad binding protein containing tetratricopeptide repeat domains

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Drosophila Uri, a PP1alpha binding protein, is essential for viability, maintenance of DNA integrity and normal transcriptional activity.

1 reference

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Chaperone ligand-discrimination by the TPR-domain protein Tah1.

1 reference

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23 August 2017

The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery

1 reference

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Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation

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A genome-wide transgenic RNAi library for conditional gene inactivation in Drosophila

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Melanotic mutants in Drosophila: pathways and phenotypes

1 reference

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23 August 2017

Hsp90: a chaperone for protein folding and gene regulation

1 reference

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23 August 2017

Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone

1 reference

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A protein interaction map of Drosophila melanogaster

1 reference

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23 August 2017

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

1 reference

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Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments

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23 August 2017

Regulation of cellular growth by the Drosophila target of rapamycin dTOR

1 reference

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1 reference

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23 August 2017

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions

1 reference

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23 August 2017

Down-regulation of RpS21, a putative translation initiation factor interacting with P40, produces viable minute imagos and larval lethality with overgrown hematopoietic organs and imaginal discs

1 reference

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12 December 2020

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10.1074/JBC.M113.499608

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24394412%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

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Europe PubMed Central

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13 June 2020

PubMed publication ID

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:24394412%20AND%20SRC:MED&resulttype=core&format=json

13 June 2020

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