Persius/hicric huggingface dataset:
Supima
Supima is a non-profit organisation in the United States whose main objective is to promote the use of American Pima cotton around the world and is involved in quality assurance and research programs. Founded in 1954, it derived its name from superior pima.
Supima licenses over 300 selected high-quality mills, textile and clothing manufacturers, and retailers to use the Supima trademark. Members finance the activities of Supima by payments calculated on a "per bale" basis.
Its other activities include:
- research programs to improve the quality of American Pima cotton
- timely crop and market information to its grower-members and licensees
- advertisements in both consumer and trade publications
- presentations to customers both in the USA and abroad
- participation in major international exhibitions and events
The Board of Directors of Supima is made up of Pima growers from Arizona, California, New Mexico and Texas.
Production of Supima cotton has risen from about 100,000 bales per year in the 1980s to over 800,000 bales in 2006. More than 90% of Supima cotton is exported from the United States, the majority of this being for the overseas manufacture of finished fabrics, clothing, sheets and towels which are re-exported to the United States for sale. The top five importers of Supima cotton are China, Pakistan, India, Japan and Indonesia.
Syngas

# Overview
Syngas (from synthesis gas) is the name given to a gas mixture that contains varying amounts of carbon monoxide and hydrogen generated by the gasification of a carbon containing fuel to a gaseous product with a heating value.  Examples include steam reforming of natural gas or liquid hydrocarbons to produce hydrogen, the gasification of coal and in some types of waste-to-energy gasification facilities. The name comes from their use as intermediates in creating synthetic natural gas (SNG) and for producing ammonia or methanol. Syngas is also used as an intermediate in producing  synthetic petroleum for use as a fuel or lubricant via Fischer-Tropsch synthesis and previously the Mobil methanol to gasoline process.
Syngas consists primarily of carbon monoxide, carbon dioxide and hydrogen, and has less than half the energy density of natural gas. Syngas is combustible and often used as a fuel source or as an intermediate for the production of other chemicals. Syngas for use as a fuel is most often produced by gasification of coal or municipal waste mainly by the following paths:
When used as an intermediate in the large-scale, industrial synthesis of hydrogen and ammonia, it is also produced from natural gas (via the steam reforming reaction) as follows:
The syngas produced in large waste-to-energy gasification facilities is used as fuel to generate electricity.
Coal gasification processes are reasonably efficient and were used for many years to manufacture illuminating gas (coal gas) for gas lighting, before electric lighting became widely available.
When syngas contains a significant amount of nitrogen, the nitrogen must be removed.  Cryogenic processing has great difficulty in recovering pure carbon monoxide when relatively large volumes of nitrogen are present due to carbon monoxide and nitrogen having very similar boiling points which are -191.5 C and -195.79 C respectively. Certain process technology  selectively removes carbon monoxide by complexation/decomplexation of carbon monoxide with cuprous aluminum chloride (CuAlCl4), dissolved in an organic liquid such as toluene. The purified carbon monoxide can have a purity greater than 99%, which makes it a good feedstock for the chemical industry. The reject gas from the system can contain carbon dioxide, nitrogen, methane, ethane and hydrogen.  The reject gas can be further processed on a pressure swing absorption system to remove hydrogen and the hydrogen and carbon dioxide can be recombined in the proper ratio for methanol production, Fischer-Tropsch diesel etc. However, the total energy efficiency is not very high, if the gas is used to make fuel, meaning that the purification processes are very energy intensive.
Syntex
Laboratorios Syntex SA was a pharmaceutical company formed in Mexico City in 1944 by Russell Marker to manufacture therapeutic steroids from the Mexican yam. Syntex was integrated into the Roche group in 1994.

# Prominent researchers
- Russell Marker left the company and took his notebooks in a disagreement over compensation.
- George Rosenkranz had studied at the Swiss Federal Institute of Technology and was conducting pharmaceutical research in Cuba. He joined Syntex to replace Marker and hired Djerassi.
- Carl Djerassi went to work at Syntex in 1949 as the associate director of chemical research. He oversaw the research resulting in the first synthesis of norethindrone, the first orally active progestin, which led to the development of some of the first oral contraceptives.
- Luis E. Miramontes moved from UNAM to Syntex in 1950 as a researcher under the direction of Djerassi. He performed the first synthesis of an orally active progestin on October 15, 1951. The steroid was 19-nor-17 alpha-ethynyltestosterone, with the generic name of norethistrone or norethindrone, which led to the development of some of the first oral contraceptives.

# Birth control pill
Syntex submitted their compound to a laboratory in Madison, Wisconsin, for biological evaluation, and found it was the most active, orally-effective progestational hormone of its time. Syntex submitted a patent application in November of 1951. G.D. Searle & Co. filed for a patent for the synthesis of the double bond isomer 13 of norethindrone called norethynodrel in August of 1953. Norethynodrel is converted into norethindrone under acidic conditions, and their new patent didn't infringe on Syntex's. Searle obtained approval to market norethynodrel before Syntex received their approval. By 1964, 3 companies including Syntex were marketing 2 mg doses of Syntex's norethindrone. Syntex chemists synthesized cortisone from diosgenin, a phytosteroid contained in Mexican yams. This synthesis was a more economical than the previous Merck & Co. synthesis.
TADA2L
Transcriptional adapter 2-alpha is a protein that in humans is encoded by the TADA2A gene.

# Function
Many DNA-binding transcriptional activator proteins enhance the initiation rate of RNA polymerase II-mediated gene transcription by interacting functionally with the general transcription machinery bound at the basal promoter. Adaptor proteins are usually required for this activation, possibly to acetylate and destabilize nucleosomes, thereby relieving chromatin constraints at the promoter. The protein encoded by this gene is a transcriptional activator adaptor and has been found to be part of the PCAF histone acetylase complex. Two transcript variants encoding different isoforms have been identified for this gene.

# Interactions
TADA2L has been shown to interact with GCN5L2, TADA3L and Myc.
TARBP2
RISC-loading complex subunit TARBP2 is a protein that in humans is encoded by the TARBP2 gene.

# Function
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene binds between the bulge and the loop of the HIV-1 TAR RNA regulatory element and activates HIV-1 gene expression in synergy with the viral Tat protein. Alternative splicing results in multiple transcript variants encoding different isoforms. This gene also has a pseudogene.

# Interactions
TARBP2 has been shown to interact with Protein kinase R and RBM14.
TAS1R2
Taste receptor type 1 member 2 is a protein that in humans is encoded by the TAS1R2 gene.

# Structure
The protein encoded by the TAS1R2 gene is a G protein-coupled receptor with seven trans-membrane domains and is a component of the heterodimeric amino acid taste receptor T1R2+3. This receptor is formed as a dimer of the TAS1R2 and TAS1R3 proteins. Moreover, the TAS1R2 protein is not functional without formation of the 2+3 heterodimer. 
Another interesting quality of the TAS1R2 and TAS1R1 genes is their spontaneous activity in the absence of the extracellular domains and binding ligands. This may mean that the extracellular domain regulates function of the receptor by preventing spontaneous action as well as binding to activating ligands such as sucrose.

# Ligands
The TAS1R2+3 receptor has been shown to respond to natural sugars sucrose and fructose, and to the artificial sweeteners saccharin, acesulfame potassium, dulcin, and guanidinoacetic acid.  Research initially suggested that rat receptors did not respond to many other natural and artificial sugars, such as glucose and aspartame, leading to the conclusion that there must be more than one type of sweet taste receptor. Contradictory evidence, however, suggested that cells expressing the human TAS1R2+3 receptor showed sensitivity to both aspartame and glucose but cells expressing the rat TAS1R2+3 receptor were only slightly activated by glucose and showed no aspartame activation. These results are inconclusive about the existence of another sweet taste receptor, but show that the TAS1R2+3 receptors are responsible for a wide variety of different sweet tastes.

# Signal transduction
TAS1R2 and TAS1R1 receptors have been shown to bind to G proteins, most often the gustducin G subunit, although a gusducin knock-out has shown small residual activity. TAS1R2 and TAS1R1 have also been shown to activate Go and Gi protein subunits. This suggests that TAS1R1 and TAS1R2 are G protein-coupled receptors that inhibit adenylyl cyclases to decrease cyclic guanosine monophosphate (cGMP) levels in taste receptors. 
Research done by creating knock-outs of common channels activated by sensory G-protein second messenger systems has also shown a connection between sweet taste perception and the phosphatidylinositol (PIP2) pathway.  The nonselecive cation Transient Receptor Potential channel TRPM5 has been shown to correlate with both umami and sweet taste.  Also, the phospholipase PLC2 was shown to similarly correlate with umami and sweet taste.  This suggests that activation of the G-protein pathway and subsequent activation of PLC 2 and the TRPM5 channel in these taste cells functions to activate the cell.

# Location and innervation
TAS1R2+3 expressing cells are found in circumvallate papillae and foliate papillae near the back of the tongue and palate taste receptor cells in the roof of the mouth.  These cells are shown to synapse upon the chorda tympani and glossopharyngeal nerves to send their signals to the brain.
TAS1R and TAS2R (bitter) channels are not expressed together in taste buds.
TAS1R3
Taste receptor type 1 member 3 is a protein that in humans is encoded by the TAS1R3 gene. The TAS1R3 gene encodes the human homolog of mouse Sac taste receptor, a major determinant of differences between sweet-sensitive and -insensitive mouse strains in their responsiveness to sucrose, saccharin, and other sweeteners.

# Structure
The protein encoded by the TAS1R3 gene is a G protein-coupled receptor with seven trans-membrane domains and is a component of the heterodimeric amino acid taste receptor TAS1R1+3 and sweet taste receptor TAS1R2+3. This receptor is formed as a protein dimer with either TAS1R1 or TAS1R2.
Experiments have also shown that a homo-dimer of TAS1R3 is also sensitive to natural sugar substances.  This has been hypothesized as the mechanism by which sugar substitutes do not have the same taste qualities as natural sugars.

# Ligands
The G protein-coupled receptors for sweet and umami taste are formed by dimers of the TAS1R proteins. 
The TAS1R1+3 taste receptor is sensitive to the glutamate in MSG as well as the synergistic taste-enhancer molecules inosine monophosphate (IMP) and guanosine monophosphate (GMP).  These taste-enhancer molecules are unable to activate the receptor alone, but are rather used to enhance receptor responses many to L-amino acids. The TAS1R2+3 receptor has been shown to respond to natural sugars sucrose and fructose, and to artificial sweeteners saccharin, acesulfame potassium, dulcin, guanidinoacetic acid.

# Signal transduction
TAS1R2 and TAS1R1 receptors have been shown to bind to G proteins, most often the gustducin G subunit, although a gusducin knock-out has shown small residual activity. TAS1R2 and TAS1R1 have also been shown to activate Go and Gi protein subunits. This suggests that TAS1R1 and TAS1R2 are G protein-coupled receptors that inhibit adenylyl cyclases to decrease cyclic guanosine monophosphate (cGMP) levels in taste receptors. The TAS1R3 protein, however, has been shown in vitro to couple with G subunits at a much lower rate than the other TAS1R proteins.  While the protein structures of the TAS1R proteins are similar, this experiment shows that the G protein-coupling properties of TAS1R3 may be less important in the transduction of taste signals than the TAS1R1 and TAS1R2 proteins.

# Location and innervation
TAS1R1+3 expressing cells are found in fungiform papillae at the tip and edges of the tongue and palate taste receptor cells in the roof of the mouth.  These cells are shown to synapse upon the chorda tympani nerves to send their signals to the brain. TAS1R2+3 expressing cells are found in circumvallate papillae and foliate papillae near the back of the tongue and palate taste receptor cells in the roof of the mouth.  These cells are shown to synapse upon the glossopharyngeal nerves to send their signals to the brain. TAS1R and TAS2R (bitter) channels are not expressed together in any taste buds.
TAS2R9
Taste receptor type 2 member 9 is a protein that in humans is encoded by the TAS2R9 gene.

# Function
This gene product belongs to the family of candidate taste receptors that are members of the G-protein-coupled receptor superfamily. These proteins are specifically expressed in the taste receptor cells of the tongue and palate epithelia. They are organized in the genome in clusters and are genetically linked to loci that influence bitter perception in mice and humans. In functional expression studies, they respond to bitter tastants. This gene maps to the taste receptor gene cluster on chromosome 12p13.
Polymorphisms in this gene have been associated with the perceived bitterness of sweetener acesulfame potassium.
TBC1D4
AS160 (Akt substrate of 160 kDa), which was originally known as TBC1 domain family member 4 (TBC1D4), is a Rab GTPase-activating protein that in humans is encoded by the TBC1D4 gene.
The 160 kD protein product was first discovered in a screen for novel substrates of the serine-threonine kinase Akt2, which phosphorylates AS160 at Thr-642 and Ser-588 after insulin stimulation.  Insulin stimulation of fat and muscle cells results in translocation of the glucose transporter GLUT4 to the plasma membrane, and this translocation process is dependent on phosphorylation of AS160.  The role of AS160 in GLUT4 translocation is mediated by its GTPase activating domain and interactions with Rab proteins in vesicle formation, increasing GLUT4 translocation when its GTPase activity is inhibited by Akt phosphorylation. Specifically, this inhibition activates RAB2A, RAB8A, RAB10 and RAB14.
AS160 also contains a calmodulin-binding domain, and this domain mediates phosphorylation-independent glucose uptake in muscle cells.
TCF7L1
Transcription factor 7-like 1 (T-cell specific, HMG-box), also known as TCF7L1, is a human gene.
This gene encodes a member of the T cell factor/lymphoid enhancer factor family of transcription factors. These transcription factors are activated by beta catenin, mediate the Wnt signaling pathway and are antagonized by the transforming growth factor beta signaling pathway. The encoded protein contains a high mobility group-box DNA binding domain and participates in the regulation of cell cycle genes and cellular senescence.

# Model organisms
Model organisms have been used in the study of TCF7L1 function. A conditional knockout mouse line, called Tcf7l1tm1a(EUCOMM)Wtsi was generated as part of the International Knockout Mouse Consortium program  a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on mutant mice and two significant abnormalities were observed. Few homozygous mutant embryos were identified during gestation, and those that did survive had a severe craniofacial defect. None survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.
TFAP2B
Transcription factor AP-2 beta also known as AP2-beta is a protein that in humans is encoded by the TFAP2B gene.

# Function
AP-2 beta is a member of the AP-2 family of transcription factors. AP-2 proteins form homo- or hetero-dimers with other AP-2 family members and bind specific DNA sequences. They are thought to stimulate cell proliferation and suppress terminal differentiation of specific cell types during embryonic development. Specific AP-2 family members differ in their expression patterns and binding affinity for different promoters. This protein functions as both a transcriptional activator and repressor.

# Clinical significance
Mutations in this gene result in autosomal dominant Char syndrome, suggesting that this gene functions in the differentiation of neural crest cell derivatives.
TMEM18
Transmembrane protein 18 also known as TMEM18 is a protein which in humans is encoded by the TMEM18 gene.

# Function
TMEM18 seems to affect energy levels through insulin and glucagon signaling, and in flies, its downregulation induces a metabolic state resembling type-II diabetes
Overexpression of the TMEM18 protein increases the migration capacity of neural stem cells while inactivation of TMEM18 results in almost complete loss of migration activity.
The TMEM18 gene is ubiquitously expressed in both mammalian and fly tissues, which suggests a basic cellular function. In the mouse brain, it is found in the majority of all cells, but is more abundant in neurons than other cell types.

# Clinical significance
Genetic variants in the proximity of the TMEM18 gene are associated with obesity, insulin levels, and blood sugar levels 

# Evolutionary history
The TMEM18 gene  has a long evolutionary history as it is present in both plants and animals. The TMEM18 protein's amino acid sequence is well conserved, which suggests that it has retained its function since the divergence of human and plants. The gene seems to have been lost in two separate lineages, but is not found duplicated in any analyzed genomes. Hence, it is not essential for eukaryotic organisms, but there appears to be selection against multiple copies of the TMEM18 gene.
TMEM67
Meckelin is a protein that in humans is encoded by the TMEM67 gene.

# Function
The protein encoded by this gene localizes to the primary cilium and to the plasma membrane. The gene functions in centriole migration to the apical membrane and formation of the primary cilium. Multiple transcript variants encoding different isoforms have been found for this gene.

# Clinical significance
Defects in this gene are a cause of Meckel syndrome type 3 (MKS3), nephronophthisis and Joubert syndrome type 6 (JBTS6).
TMEM70
Transmembrane protein 70 is a protein that in humans is encoded by the TMEM70 gene. It is a transmembrane protein located in the mitochondrial inner membrane involved in the assembly of the F1 and Fo structural subunits of ATP synthase. Mutations in this gene have been associated with neonatal mitochondrial encephalo-cardiomyopathy due to ATP synthase (Complex V) deficiency, causing a wide variety of symptoms including 3-methylglutaconic aciduria, lactic acidosis, mitochondrial myopathy, and cardiomyopathy.

# Structure
The TMEM70 gene has 4 exons and is located on the q arm of chromosome 8 in position 21.11 and spans 6,642 base pairs. The gene produces a 29 kDa protein composed of 260 amino acids. The encoded protein is a multi-pass transmembrane protein localized to the mitochondrial inner membrane. It contains two putative transmembrane regions and the conserved domain DUF1301.

# Function
The encoded protein is involved in the assembly of the F1 and Fo structural subunits of ATP synthase.

# Clinical significance
Mutations in the TMEM70 gene have been associated with neonatal mitochondrial encephalocardiomyopathy due to nuclear type 2 Complex V (ATP synthase) deficiency. There are a wide variety of possible symptoms depending on the mutation, including 3-methylglutaconic aciduria, dysmorphic features, psychomotor retardation, hypotonia, growth retardation, mitochondrial myopathy and cardiomyopathy, hepatomegaly, hypoplastic kidneys, and elevated lactate levels in urine, plasma, and cerebrospinal fluid.
Most notably, a c.317-2AG mutation in the splice site of intron 2 of this gene caused aberrant splicing and the loss of the TMEM70 transcript. This resulted in ATP synthase deficiency symptomized by apneoic spells, hypertrophic cardiomyopathy, profound lactic acidosis, hyperammonaemia, psychomotor retardation, 3-methylglutaconic aciduria, failure to thrive, and severe muscular hypotonia. Also noted in some patients were hypospadias, intrauterine growth retardation, microcephaly and cryptorchidism, but most patients did not survive the neonatal period.
Another mutation (c.366A>T) in the second exon of this gene caused an amino acid substitution (Y112X), resulting in Nuclear Type 2 Mitochondrial Complex V deficiency symptomized by lactic acidosis, psychomotor retardation, facial dysmorphism, hypertrophic cardiomyopathy, and hypospadia.
A study of mitochondrial morphology in patients with mutations in this gene revealed disorganization of the mitochondrial nucleoid. Mitochondria were abnormal, with whorled cristae and disrupted nucleoid clusters of mtDNA. The nucleoids and mitochondrial respiratory chain complexes were confined to the outer rings of the whorls.

# Interactions
The encoded protein has protein-protein interactions with RAB2A, PHC2, NDUFAF8, NDUFS5, COX6B1, ECSIT, NDUFAF4, and COA3.
TNNI3K
TNNI3 interacting kinase is a protein that in humans is encoded by the TNNI3K gene.

# Function
This gene encodes a protein that belongs to the MAP kinase kinase kinase (MAPKKK) family of protein kinases. The protein contains ankyrin repeat, protein kinase and serine-rich domains and is thought to play a role in cardiac physiology.

# Clinical significance
Mutations in TNNI3K are associated to                 cardiomyopathies            .
TOLLIP
Toll interacting protein, also known as TOLLIP, is an inhibitory adaptor protein that in humans is encoded by the TOLLIP gene.

# Function
It is an inhibitory adaptor protein within Toll-like receptors (TLR). The TLR pathway is a part of the innate immune system that recognizes structurally conserved molecular patterns of microbial pathogens, leading to an inflammatory immune response.

# Clinical significance
Polymorphisms in TLR genes have been implicated in various diseases like atopic dermatitis. Recently, variations in the TOLLIP gene have been associated with tuberculosis and idiopathic pulmonary fibrosis.

# Interactions
TOLLIP has been shown to interact with TOM1, TLR 2, TLR 4 and IL1RAP.