Mad1 Function Is Regulated through Elements within the Carboxy Terminus

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Molecular and Cellular Biology

• Publication date

  2000-06-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1128/MCB.20.12.4253-4264.2000PMID 10825189PMCID PMC85793
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Expression and regulation of protein kinase CK2 during the cell cycle

  2004cited by this paper
• Murine protein kinase CK2: Gene and oncogene

  2004cited by this paper
• Mxi1 Is a Repressor of the c-myc Promoter and Reverses Activation by USF*

  1999cited by this paper
• Targeted disruption of the MYC antagonist MAD1 inhibits cell cycle exit during granulocyte differentiation

  1998cited by this paper
• CBP Alleviates the Intramolecular Inhibition of ATF-2 Function*

  1998cited by this paper
• Function of the c-Myc antagonist Mad1 during a molecular switch from proliferation to differentiation

  1997cited by this paper
• Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression

  1997cited by this paper
• Regulated expression and function of the c-Myc antagonist, Mad1, during a molecular switch from proliferation to differentiation.

  1997cited by this paper
• Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression.

  1997cited by this paper
• Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non‐canonical E box and acts as a transcriptional repressor

  1997influential reference
• Histone deacetylase activity is required for full transcriptional repression by mSin3A.

  1997cited by this paper
• Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites.

  1997influential reference
• Expression of Mad, an antagonist of Myc oncoprotein function, in differentiating keratinocytes during tumorigenesis of the skin.

  1996cited by this paper
• Optimization of Dnase I removal of contaminating DNA from RNA for use in quantitative RNA-PCR.

  1996cited by this paper
• The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb.

  1996cited by this paper
• Inhibition of cell proliferation by the Mad1 transcriptional repressor

  1996cited by this paper
• Proteins of the Myc network: essential regulators of cell growth and differentiation.

  1996cited by this paper
• Effects of the MYC oncogene antagonist, MAD, on proliferation, cell cycling and the malignant phenotype of human brain tumour cells

  1995cited by this paper
• Repression of Myc-Ras cotransformation by Mad is mediated by multiple protein-protein interactions.

  1995influential reference
• Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro

  1995cited by this paper
• Erratum: Effects of the MYC oncogene antagonist, MAD, on proliferation, cell cycling and the malignant phenotype of human brain tumour cells (Nature Medicine (1995) 1 (638-643))

  1995cited by this paper
• Mad3 and Mad4: novel Max‐interacting transcriptional repressors that suppress c‐myc dependent transformation and are expressed during neural and epidermal differentiation.

  1995influential reference
• Contrasting roles for Myc and Mad proteins in cellular growth and differentiation.

  1995cited by this paper
• Regulation of Myc and Mad during epidermal differentiation and HPV-associated tumorigenesis.

  1995cited by this paper
• Differential effects by Mad and Max on transformation by cellular and viral oncoproteins.

  1995influential reference
• Differential regulation of Max and role of c-Myc during erythroid and myelomonocytic differentiation of K562 cells.

  1995cited by this paper
• Mapping of two genes encoding members of a distinct subfamily of MAX interacting proteins: MAD to human chromosome 2 and mouse chromosome 6, and MXI1 to human chromosome 10 and mouse chromosome 19.

  1994cited by this paper
• Inducing differentiation of transformed cells with hybrid polar compounds: a cell cycle-dependent process.

  1994cited by this paper
• Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1.

  1994cited by this paper
• Assignment of the human MAD and MXI1 genes to chromosomes 2p12-p13 and 10q24-q25.

  1994cited by this paper
• Expression of mad, mxi1, max and c-myc during induced differentiation of hematopoietic cells: opposite regulation of mad and c-myc.

  1994cited by this paper
• NF-kappa B sites function as positive regulators of expression of the translocated c-myc allele in Burkitt's lymphoma

  1994cited by this paper
• Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity.

  1993cited by this paper
• Differential patterns of DNA binding by myc and max proteins.

  1993cited by this paper
• Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites.

  1993cited by this paper
• Opposite regulation of gene transcription and cell proliferation by c-Myc and Max.

  1993cited by this paper
• Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62.

  1993cited by this paper
• Oncogenic activity of the c-Myc protein requires dimerization with Max.

  1993influential reference
• A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation.

  1993cited by this paper
• Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers.

  1993cited by this paper
• Sequence-specific transcriptional activation by Myc and repression by Max

  1993cited by this paper
• Max and c-Myc/Max DNA-binding activities in cell extracts.

  1992cited by this paper
• Myc family oncoproteins function through a common pathway to transform normal cells in culture: cross-interference by Max and trans-acting dominant mutants.

  1992cited by this paper
• Regions within the c-Myc protein that are necessary for transformation are also required for inhibition of differentiation of murine erythroleukemia cells.

  1992cited by this paper
• Myc and Max proteins possess distinct transcriptional activities

  1992cited by this paper
• Mutational analysis of Max: role of basic, helix-loop-helix/leucine zipper domains in DNA binding, dimerization and regulation of Myc-mediated transcriptional activation.

  1992cited by this paper
• Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.

  1992influential reference
• Association of Myn, the murine homolog of max, with c-Myc stimulates methylation-sensitive DNA binding and ras cotransformation.

  1991cited by this paper
• Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.

  1991cited by this paper
• Construction of defined deletion mutants by thermal cycled fusion: applications to protein kinase C.

  1990cited by this paper
• The leucine zipper domain of avian cMyc is required for transformation and autoregulation.

  1990cited by this paper
• An amino-terminal c-myc domain required for neoplastic transformation activates transcription

  1990cited by this paper
• c-myc antisense transcripts accelerate differentiation and inhibit G1 progression in murine erythroleukemia cells

  1988cited by this paper
• Enforced expression of the c-myc oncogene inhibits cell differentiation by precluding entry into a distinct predifferentiation state in G0/G1

  1988cited by this paper
• Expression of a transfected human c-myconcogene inhibits differentiation of a mouse erythroleukaemia cell line

  1986cited by this paper
• Microinjected c-myc as a competence factor.

  1985cited by this paper
• Close link between reduction of c-myc expression by interferon and G0/G1 arrest

  1985cited by this paper
• Differentiation and Control of Malignancy of Tumor Cells

  1976cited by this paper

• Direct HPV E6/Myc interactions induce histone modifications, Pol II phosphorylation, and hTERT promoter activation

  2017influential citation
• The suppression of MAD1 by AKT‐mediated phosphorylation activates MAD1 target genes transcription

  2009cites this paper
• The Mad side of the Max network: antagonizing the function of Myc and more.

  2006cites this paper
• Mnt transcriptional repressor is functionally regulated during cell cycle progression

  2005cites this paper
• Assessing the impact of alternative splicing on domain interactions in the human proteome.

  2004cites this paper
• In Vivo Chromatin Remodeling Events Leading to Inflammatory Gene Transcription under Diabetic Conditions*

  2004cites this paper
• Signaling disrupts mSin3A binding to the Mad1‐like Sin3‐interacting domain of TIEG2, an Sp1‐like repressor

  2002cites this paper
• Regulation and function of the Mad/Max/Myc network during neuronal and hematopoietic differentiation.

  2001cites this paper