Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation (Q28140363)

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scientific article (publication date: 7 April 2000)

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English	Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation	scientific article (publication date: 7 April 2000)

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scholarly article

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Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation (English)

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author name string

J Lewis

1

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A Devin

2

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A Miller

3

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Y Lin

4

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Y Rodriguez

5

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L Neckers

6

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Z G Liu

7

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language of work or name

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publication date

7 April 2000

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Journal of Biological Chemistry

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275

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14

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10519-26

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Two tumour necrosis factor receptors: structure and function.

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https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The Fas death factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Two TNF receptors

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https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

A novel domain within the 55 kd TNF receptor signals cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The death domain kinase RIP mediates the TNF-induced NF-kappaB signal

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

NF-kappa B: ten years after

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https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Identification and characterization of an IkappaB kinase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

An essential role for NF-kappaB in preventing TNF-alpha-induced cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Requirement of NF-kappaB activation to suppress p53-independent apoptosis induced by oncogenic Ras.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Suppression of TNF-alpha-induced apoptosis by NF-kappaB

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kappaB

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Aberrant nuclear factor-kappaB/Rel expression and the pathogenesis of breast cancer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Molecular chaperones in cellular protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Hsp90 as a capacitor for morphological evolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The Hsp90 complex--a super-chaperone machine as a novel drug target

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Regulation of interleukin-8 production in a human colon epithelial cell line (HT-29).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Helicobacter pylori induces interleukin-8 expression in endothelial cells and the signal pathway is protein tyrosine kinase dependent

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras Association

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Hop modulates Hsp70/Hsp90 interactions in protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Inhibition of TNF-induced apoptosis by NF-kappa B.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Steroid receptor interactions with heat shock protein and immunophilin chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

The complexity of Raf-1 regulation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Involvement of the CD95 (APO–1/Fas) receptor/ligand system in drug–induced apoptosis in leukemia cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.14.10519

21 January 2018

Identifiers

10.1074/JBC.275.14.10519

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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