Persius/hicric huggingface dataset:
miR-296
miR-296 is a family of microRNA precursors found in mammals, including humans. The ~22 nucleotide mature miRNA sequence is excised from the precursor hairpin by the enzyme Dicer. This sequence then associates with RISC which effects RNA interference.
miR-296 has been named an "angiomiR" due to being characterised as a microRNA which regulates angiogenesis, the process of growth and creation of new blood vessels. miR-296 is thought to have a specific role in cancer in promoting tumour angiogenesis. It achieves this by targeting HGS mRNA, reducing its expression in endothelial cells which then results in  greater number of VEGF receptors.
miR-296 has predicted target sites in the transcription factor NANOG and may also contribute to carcinogenesis by dysregulating p53.
miR-338
miR-338 is a family of brain-specific microRNA precursors found in mammals, including humans. The ~22 nucleotide mature miRNA sequence is excised from the precursor hairpin by the enzyme Dicer. This sequence then associates with RISC which effects RNA interference.
miR-338 is located in an intronic region within the gene for apoptosis-associated tyrosine kinase (AATK). It has been predicted that it may downregulate genes which have a downstream negative effect on AATK expression.

# Function
miR-338 is a brain-specific miRNA which regulates the expression of cytochrome c oxidase IV (COX4). The mature miR-338 miRNA sequence is complementary to a short section of the 3' untranslated region of COX4 mRNA. This mRNA sequence is presented atop a stem-loop structure, indicating it is accessible to miRNA processing.

# Applications
miR-338 is dysregulated in neuroblastoma, and could potentially be implemented as a biomarker or future therapeutic agent. miR-338 has also been linked with hepatocellular carcinoma, and a large-scale diagnostic test has been suggested involving measurement of miR-338 expression in tissue samples. Furthermore, miR-338 is one of seven microRNAs whose expression profiles can be combined to give a prediction of the probability of survival of a patient with gastric cancer.
mir-145
In molecular biology, mir-145 microRNA is a short RNA molecule that in humans is encoded by the MIR145 gene. MicroRNAs function to regulate the expression levels of other genes by several mechanisms.

# Targets
MicroRNAs are involved in down-regulation of a variety of target genes. Gotte et al. have shown that experimental over-expression of mir-145 down-regulates the junctional cell adhesion molecule JAM-A as well as the actin bundling protein fascin. Larsson et al. showed that miR-145 targets the 3' UTR of the FLI1 gene, a finding that was later supported by Zhang et al.

# Role in cancer
miR-145 is hypothesised to be a tumor suppressor. miR-145 has been shown to be down-regulated in breast cancer. miR-145 is also involved in colon cancer  and acute myeloid leukemia.
Monomer
A monomer (from Greek mono "one" and meros "part") is a small molecule that may become chemically bonded to other monomers to form a polymer.
Examples of monomers are hydrocarbons such as the alkene and arene homologous series.
Here hydrocarbon monomers such as phenylethene and ethene form polymers used as plastics like polyphenylethene (commonly known as polystyrene) and polyethene (commonly known as polyethylene or polythene).  Other commercially important monomers include acrylic monomers such as acrylic acid, methyl methacrylate, and acrylamide.
Amino acids are natural monomers, and polymerize to form proteins. Glucose monomers can also polymerize to form starches, amylopectins and glycogen polymers. In this case the polymerization reaction is known as a dehydration or condensation reaction (due to the formation of water (H2O) as one of the products) where a hydrogen atom and a hydroxyl (-OH) group are lost to form H2O and an oxygen molecule bonds between each monomer unit.
The lower molecular weight compounds built from monomers are also referred to as dimers, trimers, tetramers, quadramers, pentamers, octamers, 20-mers, etc. if they have 2, 3, 4, 5, 8, or 20 monomer units, respectively.  Any number of these monomer units may be indicated by the appropriate prefix, eg, decamer, being a 10-unit monomer chain or polymer.  Larger numbers are often stated in English in lieu of Greek.  Polymers with relatively low number of units are called oligomers.
Movicol
A drug used in the treatment of constipation, Movicol comes in the form of a dissolvable sachet and is marketed outside the US by Norgine Ltd
The active ingredient is polyethylene glycol '3350' (also known as macrogol), which belongs to a class of drugs called osmotic laxatives.  These drugs work by binding to water in the gut, thereby moistening stools making them easier to pass.
For more detailed information, including side effects and contra-indications of the drug see the British National Formulary or the references.
Mucin 2
Mucin 2, oligomeric mucus gel-forming, also known as MUC2, is a protein that in humans is encoded by the MUC2 gene.

# Function
This gene encodes a member of the mucin protein family. The protein encoded by this gene, also called mucin 2, is secreted onto mucosal surfaces.
Mucin 2 is particularly prominent in the gut where it is secreted from goblet cells in the epithelial lining into the lumen of the large intestine. There, mucin 2, along with small amounts of related-mucin proteins, polymerizes into a gel of which 80% by weight is oligosaccharide side-chains that are added as post-translational modifications to the mucin proteins. This gel provides an insoluble mucous barrier that serves to protect the intestinal epithelium.

# Genetics
The mucin 2 protein features a central domain containing tandem repeats rich in threonine and proline that varies between 50 and 115 copies in different individuals. Alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known.
Mucin 7
Mucin-7 is a protein that in humans is encoded by the MUC7 gene. In animals, the MUC7 gene is found in most placental mammals, but not marsupials.

# Human variations
Humans carry either a five or six tandem repeat version of the gene. In other primates, the number of repeats found is 4-5 for gorillas, 5 for chimpanzees, 6-7 for orangutans, 8-10 for macaques, 10-11 for baboons and 11-12 for green monkeys.
Some modern people from Sub-Saharan Africa were found to carry a five tandem repeat variation of the MUC7 gene that is highly divergent from other, modern humans. The estimated coalescence age for the human variations of the MUC7 gene is estimated to be around 4.5 million years ago, which predates the human-Neanderthal split. Neanderthals and Denisovans also carry variants that are much closer to those of other, modern humans; thus, researcers postulate that this divergent Sub-Saharan variant most likely introgressed from a currently yet-unknown archaic human ghost population.
Mullein
The Mulleins (Verbascum) are a genus of about 250 species of flowering plants in the figwort family (Scrophulariaceae). They are native to Europe and Asia, with the highest species diversity in the Mediterranean region.
They are biennial or perennial plants, rarely annuals or subshrubs, growing to 0.5-3 m tall. The plants first form a dense rosette of leaves at ground level, subsequently sending up a tall flowering stem. The leaves are spirally arranged, often densely hairy, though glabrous (hairless) in some species. The flowers have five symmetrical petals; petal colours in different species include yellow (most common), orange, red-brown, purple, blue or white. The fruit is a capsule containing numerous minute seeds.

# Cultivation and uses
Various species have been introduced (and in some case naturalised) in the Americas, Australia and Hawaii.
Since the year 2000 a number of new hybrid cultivars have come out that have increased flower size with shorter heights and tend to be longer lived plants. A number have new colors for this genus. Many are raised from seed, both the short lived perennial and biennial types. In the landscape they are valued for their tall narrow stature and for flowering over a long period of time, even in dry soils.
One of the best known species is Verbascum thapsus (Great mullein), which is used as a herbal remedy for sore throat, cough and lung diseases.
Mullein is also the active ingredient in many alternative smoking blends.
Murrain
Murrain (Pronounced "mur'in") is a highly infectious disease of cattle and sheep.  It literally means "disease" and was used in medieval times to represent just that.  The population of that era had no way of identifying specific diseases in their livestock so they simply put all illnesses under one heading.  There were major sheep and cattle murrains in Europe during the 14th century, which combined with the Little Ice Age resulted in widespread famine during the Great Famine of 1315-1317, weakening the population of Europe before the onset of the Black Death in 1348.
Murrain is also mentioned once in the Bible relating to the fifth plague brought upon Egypt.
Exodus 9:3: "Behold, the hand of the LORD is upon thy cattle which is in the field, upon the horses, upon the asses, upon the camels, upon the oxen, and upon the sheep: there shall be a very grievous murrain."
In some parts of Scotland, force-fire was believed to cure it.
NAV-CO2
Non-flammable Alcohol Vapor in Carbon Dioxide (NAV-CO2) systems were developed in Japan in the 1990s to sanitize hospitals and ambulances. These systems were developed to respond to a need for a safe, effective, and environmentally sound way to sanitizing without the use of toxic or corrosive chemicals.

# Theory of operation
NAV-CO2 systems use liquid CO2 as a propellant. NAV-CO2 systems combine Alcohol-based sanitizing solutions with a heated stream of CO2 liquid to create a vapor capable of penetrating small crevices and gaps. As CO2 and atomized Alcohol evaporate completely at room temperature, no residue remains. CO2 displaces oxygen, eliminating one of the elements needed to support combustion. Sanitizing chemicals such as quaternary ammonium can be added to alcohol based sanitizers to extend the killing time on surfaces. NAV-CO2 systems are used to sanitize contact surfaces where individuals may become infected. Hand washing and sanitizing surfaces with Alcohol-based solutions are effective methods for the prevention of nosocomial infection.

# Application
Hospitals, Ambulances, Nursing Homes, Public Waiting Areas and Food Processing Plants are likely places where disease causing bacteria and viruses are known to colonize. NAV-CO2 eliminates the use and disposal of toxic chemicals  such as bleach and other commercial products.

# Effectiveness against Pathogens
Alcohol-based solutions Tuberculosis, MRSA, Listeria, Salmonella, Pseudonomas aeruginosa, Hepatitis B, Norovirus
NDUFA12
NADH dehydrogenase  1 alpha subcomplex subunit 12 is an enzyme that in humans is encoded by the NDUFA12 gene. The NDUFA12 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in subunits of NADH dehydrogenase (ubiquinone), also known as Complex I, frequently lead to complex neurodegenerative diseases such as Leigh's syndrome that result from mitochondrial complex I deficiency.

# Structure
The NDUFA12 gene is located on the q arm of chromosome 12 in position 22 and spans 32,386 base pairs. The gene produces a 17 kDa protein composed of 145 amino acids. NDUFA12 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane. NDUFA12 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I, but it is an accessory subunit that is believed not to be involved in catalysis. The predicted secondary structure is primarily alpha helix, but the carboxy-terminal half of the protein has high potential to adopt a coiled-coil form. The amino-terminal part contains a putative beta sheet rich in hydrophobic amino acids that may serve as mitochondrial import signal.

# Function
The human NDUFA12 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.

# Clinical significance
Mutations to NDUFA12 are not frequently found to cause complex I deficiency on their own. NDUFA12 is an accessory subunit and the complex can still be found assembled and enzymatically active in its absence, though in reduced amounts and activity. However, a cytosine to tyrosine mutation at position 178 that leads to a premature stop codon has been found in place of arginine at amino acid 60, leading to delayed early development, loss of motor abilities, and basal ganglia lesions typical of Leigh's syndrome.
NDUFAB1
NADH dehydrogenase (ubiquinone) 1 beta subcomplex, 5, 16kDa is a protein that in humans is encoded by the NDUFAB1 gene. The NDUFAB1 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain.

# Structure
The NDUFAB1 gene is located on the p arm of chromosome 16 at position 12.2 and it spans 15,327 base pairs. The NDUFAB1 gene produces a 17.4 kDa protein composed of 156 amino acids. NDUFAB1 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site. NDUFAB1 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.

# Function
The human NDUFAB1 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. However, NDUFAB1 is an accessory subunit of the complex that is believed not to be involved in catalysis. Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.

# Clinical Significance
In a genome-wide association study (GWAS) meta-analysis conducted across European and African American populations, the NDUFAB1 gene and two other genes (MFAP3L and PALB2) were identified as genetic loci significantly associated with anxiety disorders (ADs). Since the comorbidity of ADs arises from their shared genetic basis, these candidate genetic loci may become therapeutic targets for AD treatments. Moreover, a study to identify small molecule drug targets for Tetralogy of Fallot (TOF), a congenital malformation of the heart, found the NDUFAB1 gene to be a major hub gene of differentially expressed genes in TOF.
NDUFAF2
NADH:ubiquinone oxidoreductase complex assembly factor 2  (NDUFAF2), also known as B17.2L or NDUFA12L is a protein that in humans is encoded by the NDUFAF2, or B17.2L, gene. The NDUFAF2 protein is a chaperone involved in the assembly of NADH dehydrogenase (ubiquinone) also known as complex I, which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in this gene have been associated with progressive encephalopathy and Leigh disease resulting from mitochondrial complex I deficiency.

# Structure
NDUFAF2 is located on the q arm of chromosome 5 in position 12.1. The NDUFAF2 gene produces a 20 kDa protein composed of 169 amino acids. The protein is a chaperone of the complex I NDUFA12 subunit family.

# Function
NADH:ubiquinone oxidoreductase (complex I) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the first step of the mitochondrial respiratory chain, resulting in the translocation of protons across the inner mitochondrial membrane. The NDUFAF2 gene encodes a complex I assembly factor, B17.2L, that is important for the correct function of the mitochondrial respiratory chain. Specifically, B17.2L acts as a molecular chaperone, associating with an 830 kDa subassembly in the late stages of complex I assembly.

# Clinical significance
Mutations in NDUFAF2 have been associated with complex I deficiency and mitochondrial diseases. These disorders are a result of the dysfunction of the mitochondrial respiratory chain and can cause a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. Clinically, NDUFAF2 mutations have been associated with progressive encephalopathy and Leigh disease.

# Interactions
In addition to co-complexes, NDUFAF2 has protein-protein interactions with CYB5B SEC22B, TMEM97, TMEM201, SPG21, LPAR3, STX8,OPTN.
NDUFAF3
NADH dehydrogenase  1 alpha subcomplex assembly factor 3, also known as 2P1, E3-3, or C3orf60, is a protein that in humans is encoded by the NDUFAF3 gene. NDUFAF3 is a mitochondrial assembly protein involved in the assembly of NADH dehydrogenase (ubiquinone) also known as complex I, which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in this gene have been associated severe complex I deficiency and Leigh syndrome.

# Structure
NDUFAF3 is located on the p arm of chromosome 3 in position 21.31 and has 7 exons. The NDUFAF3 gene produces a 20.4 kDa protein composed of 184 amino acids. NDUFAF3 encodes two isoforms which have a common DUF498 domain. Predictions indicate that isoform A contains an additional 35 amino acid N-terminal sequence and is thus longer than isoform B. The extra sequence may be involved in mitochondrial targeting, supporting NDUFAF3's function in mitochondrial assembly.

# Function
NADH:ubiquinone oxidoreductase (complex I) catalyzes the transfer of electrons from NADH to ubiquinone (coenzyme Q) in the first step of the mitochondrial respiratory chain, resulting in the translocation of protons across the mitochondrial inner membrane. The NDUFAF3 gene encodes a mitochondrial complex I assembly protein that localizes to the mitochondrial inner membrane and interacts with complex I subunits and is important for the correct function of the mitochondrial respiratory chain.
NDUFAF3 colocalizes, comigrates to several assembly intermediates, and is codependent with NDUFAF4 from the early to late stages of complex I assembly. In addition to their close interactions with each other, NDUFAF3 and NDUFAF4 interact with NDUFS2, NDUFS3, NDUFS8, and NDUFA5 in a translation-dependent early assembly mechanism. It is also suggested that NDUFAF3 is involved in coupling mitochondrial translation with membrane insertion in the process of complex I assembly.

# Clinical Significance
Mutations in NDUFAF3 have been associated with complex I deficiency and mitochondrial diseases. These disorders are a result of the dysfunction of the mitochondrial respiratory chain and can cause a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. Mutations have included the homozygous variants c.494C > T; p.(Ala165Val), c.365 GC resulting in R122P, and c.2 TC resulting in M1T. Clinically, NDUFAF3 mutations have been associated with Leigh syndrome and severe complex I deficiency. Some common signs and symptoms include lactic acidosis, nystagmus, hypotonia, and cerebral lesions.

# Interactions
In addition to co-complexes, NDUFAF3 has protein-protein interactions with NDUFAF4 and SNRPA.