MXD4

MXD4

MAX dimerization protein 4, also known as MXD4, is a human gene.cite web | title = Entrez Gene: MXD4 MAX dimerization protein 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10608| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene is a member of the MAD gene family . The MAD genes encode basic helix-loop-helix-leucine zipper proteins that heterodimerize with MAX protein, forming a transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.cite web | title = Entrez Gene: MXD4 MAX dimerization protein 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10608| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Marcotte R, Chen JM, Huard S, Wang E |title=c-Myc creates an activation loop by transcriptionally repressing its own functional inhibitor, hMad4, in young fibroblasts, a loop lost in replicatively senescent fibroblasts. |journal=J. Cell. Biochem. |volume=96 |issue= 5 |pages= 1071–85 |year= 2006 |pmid= 16167342 |doi= 10.1002/jcb.20503
*cite journal | author=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203–8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007
*cite journal | author=Hillier LW, Graves TA, Fulton RS, "et al." |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Jiang DJ, Yu HX, Hexige SY, "et al." |title=Human liver specific transcriptional factor TCP10L binds to MAD4. |journal=J. Biochem. Mol. Biol. |volume=37 |issue= 4 |pages= 402–7 |year= 2004 |pmid= 15469726 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Kime L, Wright SC |title=Mad4 is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc. |journal=Biochem. J. |volume=370 |issue= Pt 1 |pages= 291–8 |year= 2003 |pmid= 12418961 |doi= 10.1042/BJ20021679
*cite journal | author=Cairo S, Merla G, Urbinati F, "et al." |title=WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network. |journal=Hum. Mol. Genet. |volume=10 |issue= 6 |pages= 617–27 |year= 2001 |pmid= 11230181 |doi=
*cite journal | author=Billin AN, Eilers AL, Queva C, Ayer DE |title=Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36344–50 |year= 2000 |pmid= 10593926 |doi=
*cite journal | author=Hurlin PJ, Quéva C, Koskinen PJ, "et al." |title=Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5646–59 |year= 1996 |pmid= 8521822 |doi=

External links

*

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем решить контрольную работу

Look at other dictionaries:

  • Receptor (biochemistry) — For other uses, see Receptor (disambiguation). In biochemistry, a receptor is a molecule found on the surface of a cell, which receives specific chemical signals from neighbouring cells or the wider environment within an organism. These signals… …   Wikipedia

  • CREB — redirects here. For other uses, see Clean Renewable Energy Bonds. CREB (top) is a transcription factor capable of binding DNA (bottom) and regulating gene expression. CREB (cAMP response element binding) is a cellular transcription factor. It… …   Wikipedia

  • MyoD — Myogenic differentiation 1 PDB rendering based on 1mdy …   Wikipedia

  • Oct-4 — POU class 5 homeobox 1 Identifiers Symbols POU5F1; MGC22487; OCT3; OCT4; OTF 3; OTF3; OTF4; Oct 3; Oct 4 External IDs …   Wikipedia

  • Estrogen receptor — 1 (ER alpha) A dimer of the ligand binding region of ERα (PDB rendering based on 3erd). Identifi …   Wikipedia

  • Progesterone receptor — PDB rendering based on 1a28 …   Wikipedia

  • Androgen receptor — Structure of the ligand binding domain of the androgen receptor (rainbow cartoon) complexed with testosterone (white sticks).[1] …   Wikipedia

  • NF-κB — Mechanism of NF κB action. In this figure, the NF κB heterodimer between Rel and p50 proteins is used as an example. While in an inactivated state, NF κB is located in the cytosol complexed with the inhibitory protein IκBα. Through the… …   Wikipedia

  • Homeobox protein NANOG — See NANOG (computing) for the network operators group. Nanog homeobox Identifiers Symbols NANOG; External IDs …   Wikipedia

  • Glucocorticoid receptor — Nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor) Crystallographic structures of the glucocorticoid receptor DNA binding domain (DBD, left, PDB 1R4O bound to DNA) and ligand bindin …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”