gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

MYC associated factor X

MAX, Max protein
The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Multiple alternatively spliced transcript variants have been described for this gene but the full-length nature for some of them is unknown. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: c-Myc, CAN, HAD, ACID, OUT
Papers using MAX antibodies
Establishment and characterization of an immortalized human sebaceous gland cell line (SZ95)
Supplier
Peirano Reto Ivo et al., In Dermato-endocrinology, 1998
... Oasis MAX u-elution plates (Waters, WAT058943) were used for extraction and washed with 5% NH4OH solution (Merck, 105428) and 10% methanol ...
Papers on MAX
Bioinformatics analyses of differentially expressed genes associated with acute myocardial infarction.
New
Sun et al., Shenyang, China. In Cardiovasc Ther, Feb 2016
Besides, 4 transcription factors (TFs), including nuclear receptor subfamily 2, group C, member 2 (NR2C2), MYC associated factor X (MAX), general transcription factor IIIC, polypeptide 2, beta 110 kDa (GTF3C2), and B-cell CLL/lymphoma 3 (BCL3) were identified.
TCP10L synergizes with MAD1 in transcriptional suppression and cell cycle arrest through mutual interaction.
New
Wu et al., Shanghai, China. In Bmb Rep, Jan 2016
MAX dimerization protein 1 (MAD1) is a key transcription suppressor that is involved in regulating cell cycle progression and Myc-mediated cell transformation.
Integrative omics reveals MYCN as a global suppressor of cellular signalling and enables network-based therapeutic target discovery in neuroblastoma.
New
Kolch et al., Dublin, Ireland. In Oncotarget, Jan 2016
MYCN's oncogenic functions are likely independent of its classical heterodimerisation partner, MAX.
Complex MAX rearrangement in a family with malignant pheochromocytoma, renal oncocytoma and erythrocytosis.
New
Dinjens et al., Rotterdam, Netherlands. In J Clin Endocrinol Metab, Jan 2016
RESULTS: The index patient's germline DNA revealed a large complex genomic alteration encompassing the intragenic and promoter regions of Myc-Associated Factor X (MAX) and alpha-(1,6)-fucosyltransferase (FUT8).
Prospective comparison of (68)Ga-DOTATATE and (18)F-FDOPA PET/CT in patients with various pheochromocytomas and paragangliomas with emphasis on sporadic cases.
New
Taïeb et al., Marseille, France. In Eur J Nucl Med Mol Imaging, Jan 2016
DESIGN: (68)Ga-DOTATATE, (18)F-FDOPA PET/CT, and conventional imaging (contrast-enhanced CT and MRI with MR angiography sequences) were prospectively performed in 30 patients (8 with SDHD mutations, 1 with a MAX mutation and 21 sporadic cases) with PHEO/PGL at initial diagnosis or relapse.
The MYC-WDR5 Nexus and Cancer.
Review
New
Tansey et al., Nashville, United States. In Cancer Res, Nov 2015
The ability of MYC to regulate transcription depends on its dimerization with MAX, which creates a DNA-binding domain that recognizes specific sequences in the regulatory elements of MYC target genes.
Impact of MYC in regulation of tumor cell metabolism.
Review
New
Henriksson et al., Stockholm, Sweden. In Biochim Biophys Acta, May 2015
The MYC proto-oncoproteins including c-MYC, MYCN and MYCL exert their functions as heterodimers with MAX, which in turn binds to E-box sequences at target promoters to regulate gene expression.
Functional interactions among members of the MAX and MLX transcriptional network during oncogenesis.
Review
New
Eisenman et al., Hutchinson, United States. In Biochim Biophys Acta, May 2015
Notably, MYC is part of a network of bHLHLZ proteins centered on the MYC heterodimeric partner MAX and its counterpart, the MAX-like protein MLX.
[Hereditary pheochromocytoma-associated syndromes. Part 1].
Review
Beltsevich et al., In Ter Arkh, 2014
New EGLN1/PHD2, KIF1B, SDH5/SDHAF2, IDH1, TMEM127, SDHA, MAX, and HIF2A gene mutations have been recently discovered.
Paragangliomas/Pheochromocytomas: clinically oriented genetic testing.
Review
Bugalho et al., Faro, Portugal. In Int J Endocrinol, 2013
Additionally to the genes involved in the classical syndromic forms: VHL gene (von Hippel-Lindau), RET gene (Multiple Endocrine Neoplasia type 2), and NF1 gene (Neurofibromatosis type 1), 10 novel genes have so far been implicated in the occurrence of paragangliomas/pheochromocytomas: SDHA, SDHB, SDHC, SDHD, SDHAF2, TMEM127, MAX, EGLN1, HIF2A, and KIF1B.
New structural determinants for c-Myc specific heterodimerization with Max and development of a novel homodimeric c-Myc b-HLH-LZ.
GeneRIF
Lavigne et al., Sherbrooke, Canada. In J Mol Recognit, 2012
New structural determinants for c-Myc specific heterodimerization with Max and development of a novel homodimeric c-Myc b-HLH-LZ.
MAX mutations cause hereditary and sporadic pheochromocytoma and paraganglioma.
GeneRIF
Robledo et al., Paris, France. In Clin Cancer Res, 2012
germline mutations in MAX are responsible for 1.12% of hereditary and sporadic pheochromocytoma and paraganglioma in patients without evidence of other known mutations
Mutation and association analyses of the candidate genes ESR1, ESR2, MAX, PCNA, and KAT2A in patients with unexplained MSH2-deficient tumors.
GeneRIF
Propping et al., Bonn, Germany. In Fam Cancer, 2012
Genetic variants in MAX does not contribute to the development of Lynch syndrome.
The Max b-HLH-LZ can transduce into cells and inhibit c-Myc transcriptional activities.
GeneRIF
Lavigne et al., Sherbrooke, Canada. In Plos One, 2011
Max b-HLH-LZ can transduce into cells and inhibit c-Myc transcriptional activities
E-box-independent regulation of transcription and differentiation by MYC.
Impact
Di Croce et al., Barcelona, Spain. In Nat Cell Biol, 2011
MYC can either activate or repress target genes by forming a complex with MAX (ref.
The E-box binding factors Max/Mnt, MITF, and USF1 act coordinately with FoxO to regulate expression of proapoptotic and cell cycle control genes by phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3 signaling.
GeneRIF
Cooper et al., Boston, United States. In J Biol Chem, 2011
The E-box binding factors Max/Mnt, MITF, and USF1 act coordinately with FoxO to regulate expression of proapoptotic and cell cycle control genes by phosphatidylinositol 3-kinase/Akt/glycogen synthase kinase 3 signaling.
Impact of KRAS and BRAF Gene Mutation Status on Outcomes From the Phase III AGITG MAX Trial of Capecitabine Alone or in Combination With Bevacizumab and Mitomycin in Advanced Colorectal Cancer.
Impact
Tebbutt et al., Elizabeth, United States. In J Clin Oncol, 2011
This analysis was performed to assess the predictive and prognostic impact of KRAS and BRAF gene mutation status in patients receiving capecitabine with bevacizumab (CG) or capecitabine without bevacizumab in the phase III AGITG MAX (Australasian Gastrointestinal Trials Group MAX) study.
Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma.
Impact
GeneRIF
Cascón et al., Madrid, Spain. In Nat Genet, 2011
MAX mutations are associated with hereditary pheochromocytoma.
PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation.
Impact
Oliviero et al., Siena, Italy. In Nat Cell Biol, 2007
Here we show that, after stimulation with growth factor, PIM1 forms a complex with the dimer of MYC with MAX (Myc-associated factor X) via the MYC BoxII (MBII) domain.
Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity.
Impact
Eisenman et al., Seattle, United States. In Cell, 1993
To determine whether Max mediates the function of regulatory proteins other than Myc, we screened a lambda gt11 expression library with radiolabeled Max protein.
share on facebooktweetadd +1mail to friends