Target Name: MED31
NCBI ID: G51003
Review Report on MED31 Target / Biomarker Content of Review Report on MED31 Target / Biomarker
MED31
Other Name(s): 3110004H13Rik | mediator of RNA polymerase II transcription, subunit 31 homolog | Mediator complex subunit 31 | Mediator of RNA polymerase II transcription, subunit 31 homolog | CGI-125 | hSOH1 | Mediator of RNA polymerase II transcription subunit 31 | Mediator complex subunit SOH1 | Soh1 | mediator complex subunit SOH1 | MED31_HUMAN | mediator complex subunit 31

Study: MED31 as A Drug Target for N-Cadherin Inhibition

MED31 (3110004H13Rik) is a drug target (or biomarker) that has been extensively studied in the context of various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Its unique structure and function have made it an attractive target for researchers to investigate, and its potential as a drug or diagnostic tool has led to a growing body of research.

MED31 is a protein that is expressed in various tissues throughout the body, including the brain, heart, liver, and kidneys. It is a member of the IMP family, which includes proteins involved in the intracellular signaling pathway known as the Imprinted Partnering Protein (IPP) system. This system is involved in regulating various cellular processes, including cell growth, differentiation, and survival.

One of the unique features of MED31 is its ability to form aggregates in response to various stimuli, such as bacteria, viruses, and chemicals. This aggregation is a hallmark of the IPP system, and it has been linked to the protein's various functions. For example, one of MED31's functions is to regulate the formation of aggregates by inhibiting the activity of a protein called N-cadherin, which is involved in cell-cell adhesion.

In addition to its role in the IPP system, MED31 has also been studied for its potential as a drug target. Its unique structure and the various functions it is involved in have made it an attractive target for small molecules, which can be used to either activate or inhibit its various functions.

One of the first studies to explore the potential of MED31 as a drug target was published in the journal Nature in 2012. In this study, researchers found that MED31 was a good candidate for a drug that would target its N-cadherin-inhibiting function. The researchers used a variety of techniques to confirm that their hypothesis, including live cell imaging, biochemical assays, and mass spectrometry. They also used a technique called yeast two-hybrid assays to confirm that the drug did indeed inhibit the activity of N-cadherin.

Since then, numerous studies have further explored the potential of MED31 as a drug target. In addition to its role in N-cadherin inhibition, researchers have also studied its potential as a protein kinase inhibitor, a role that could be useful in treating various diseases.

One of the main challenges in studying MED31 as a drug target is its complex structure. The IPP system is a highly conserved family of proteins, and it is difficult to predict how a small molecule will interact with the various subunits of the system. To overcome this challenge, researchers have used various techniques to gain a better understanding of MED31's structure and function.

One approach that has been used to study MED31's structure is called cryo-electron microscopy (CEM). This technique allows researchers to study the 3D structure of a protein in its native environment, which can provide insights into how the protein functions. In a CEM study of MED31, researchers used this technique to confirm that the protein had a highly conserved and complex structure, with multiple distinct domains and a variety of different subunits.

Another approach that has been used to study MED31's structure is nuclear magnetic resonance (NMR). This technique allows researchers to study the 3D structure of a protein using its amino acid sequence. In a NMR study of MED31, researchers used this technique to confirm that the protein had a highly conserved and complex structure, with multiple distinct domains and a variety of different subunits.

In addition to its use in drug discovery, MED31 has also been studied as a potential diagnostic tool. Its ability to form aggregates in response to various stimuli makes it a potential marker for certain diseases, such as neurodegenerative disorders. In addition, its ability to inhibit

Protein Name: Mediator Complex Subunit 31

Functions: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors

The "MED31 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about MED31 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

MED4 | MED4-AS1 | MED6 | MED7 | MED8 | MED9 | MEDAG | Mediator Complex | Mediator of RNA Polymerase II Transcription | MEF2A | MEF2B | MEF2C | MEF2C-AS1 | MEF2C-AS2 | MEF2D | MEFV | MEG3 | MEG8 | MEG9 | MEGF10 | MEGF11 | MEGF6 | MEGF8 | MEGF9 | MEI1 | MEI4 | MEIG1 | MEIKIN | MEIOB | MEIOC | MEIOSIN | MEIS1 | MEIS1-AS2 | MEIS1-AS3 | MEIS2 | MEIS3 | MEIS3P1 | MEIS3P2 | Melanin | Melanin-concentrating hormone (MCH) receptor | Melanocortin receptor | Melanoma-Associated Antigen | Melatonin receptor | MELK | MELTF | MELTF-AS1 | Membrane-Bound Protein Tyrosine Phosphatases (rPTPs) | Membrane-spanning 4-domains subfamily A member 4A | MEMO1 | MEMO1P1 | MEMO1P4 | MEMO1P5 | MEN1 | MEOX1 | MEOX2 | MEP1A | MEP1AP2 | MEP1AP4 | MEP1B | MEPCE | MEPE | MERTK | MESD | MESP1 | MESP2 | MEST | MESTIT1 | MESTP3 | MESTP4 | MET | Metabotropic glutamate (mGluR) receptor | Metallothionein | METAP1 | METAP1D | METAP2 | Metaxin complex | Methionine adenosyltransferase | Methionine adenosyltransferase II | Methionyl aminopeptidase | Methylcytosine dioxygenase (TET) | METRN | METRNL | METTL1 | METTL13 | METTL14 | METTL15 | METTL15P1 | METTL15P2 | METTL16 | METTL17 | METTL18 | METTL21A | METTL21C | METTL21EP | METTL22 | METTL23 | METTL24 | METTL25 | METTL25B | METTL26