c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells. (Q32084062)

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5 November 2019

title

c-myc overexpression activates alternative pathways for intracellular proteolysis in lymphoma cells (English)

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5 November 2019

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5 November 2019

Teresa Frisan

2

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5 November 2019

Maria Masucci

5

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5 November 2019

author name string

Vertuani S

3

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5 November 2019

Bornkamm GW

4

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5 November 2019

publication date

1 March 2001

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5 November 2019

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5 November 2019

volume

3

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5 November 2019

issue

3

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5 November 2019

page(s)

283-288

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A proteolytic system that compensates for loss of proteasome function

5 November 2019

cites work

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Differences in B cell growth phenotype reflect novel patterns of Epstein-Barr virus latent gene expression in Burkitt's lymphoma cells

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Down-regulation of class I HLA antigens and of the Epstein-Barr virus-encoded latent membrane protein in Burkitt lymphoma lines

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Variations in proteasome subunit composition and enzymatic activity in B-lymphoma lines and normal B cells

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Restoration of endogenous antigen processing in Burkitt's lymphoma cells by Epstein-Barr virus latent membrane protein-1: coordinate up-regulation of peptide transporters and HLA-class I antigen expression

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c-myc activation renders proliferation of Epstein-Barr virus (EBV)-transformed cells independent of EBV nuclear antigen 2 and latent membrane protein 1.

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Cell cycle activation by c-myc in a burkitt lymphoma model cell line.

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Ubiquitin-dependent protein degradation

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The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene

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DUB-1, a deubiquitinating enzyme with growth-suppressing activity

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The level of C/EBP protein is critical for cell migration during Drosophila oogenesis and is tightly controlled by regulated degradation

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Characterization and inhibition of a cholecystokinin-inactivating serine peptidase

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Basal and human papillomavirus E6 oncoprotein-induced degradation of Myc proteins by the ubiquitin pathway

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Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc.

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c-Myc proteolysis by the ubiquitin-proteasome pathway: stabilization of c-Myc in Burkitt's lymphoma cells

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Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas

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Release of infectious Epstein-Barr virus by transformed marmoset leukocytes

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Sensitivity of Epstein-Barr virus (EBV) producer and non-producer human lymphoblastoid cell lines to superinfection with EB-virus

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7 January 2021

Endemic Burkitt's lymphoma: phenotypic analysis of tumor biopsy cells and of derived tumor cell lines

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7 January 2021

Activation of the cell death program by inhibition of proteasome function

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7 January 2021

Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes

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7 January 2021

Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes

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7 January 2021

Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

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7 January 2021

MHC-linked LMP gene products specifically alter peptidase activities of the proteasome

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7 January 2021

Identifiers

DOI

10.1038/35060076

1 reference

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Dimensions Publication ID

5 November 2019

1008599136

0 references

1 reference