UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.

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Gene Expression of Pneumocystis murina after Treatment with Anidulafungin Results in Strong Signals for Sexual Reproduction, Cell Wall Integrity, and Cell Cycle Arrest, Indicating a Requirement for Asci Formation for Proliferation.

P2860

Q49791958-7F3BE518-FC7B-40AC-B739-56AE4B13E8B5

P2860

UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.

Item

http://www.wikidata.org/entity/Q41176558

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

UBL/BAG-domain co-chaperones c ...... nstitutive activation of Hsf1.

@en

type

Item

label

UBL/BAG-domain co-chaperones c ...... nstitutive activation of Hsf1.

@en

prefLabel

UBL/BAG-domain co-chaperones c ...... nstitutive activation of Hsf1.

@en

P1476

UBL/BAG-domain co-chaperones c ...... nstitutive activation of Hsf1.

@en

P2093

Caroline Kampmeyer

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

Esben G Poulsen

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

Franziska Kriegenburg

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

Kay Hofmann

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

P2860

Hsp70-Hsp40 chaperone complex functions in controlling polarized growth by repressing Hsf1-driven heat stress-associated transcription

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines

Whole-genome microarrays of fission yeast: characteristics, accuracy, reproducibility, and processing of array data

BAG-1 haplo-insufficiency impairs lung tumorigenesis

The nucleotide exchange factors of Hsp70 molecular chaperones

Protein quality control in the nucleus

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors

Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.

P2888

s12192-016-0751-z

P304

143-154

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

P31

scholarly article

P356

10.1007/S12192-016-0751-Z

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

P433

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

P478

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

P50

Rasmus Hartmann-Petersen

Jens V. Johansen

Christian Holmberg

P577

2016-12-14T00:00:00Z

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

P698

27966061

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

P921

molecular chaperones

overexpression

P932

5225068

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

UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.

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P2860

P2860

UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.

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type

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prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P921

P932