Persius/hicric huggingface dataset:
Furan

# Overview
Furan, also known as furane and furfuran, is a heterocyclic organic compound.  It is typically derived by the thermal decomposition of pentose-containing materials,  cellolosic solids especially pine-wood.  Furan is a colorless, flammable, highly volatile liquid with a boiling point close to room temperature.  It is toxic and may be carcinogenic. Catalytic hydrogenation (see redox) of furan with a palladium catalyst gives tetrahydrofuran.
Furan is aromatic because one of the lone pairs of electrons on the oxygen atom is delocalized into the ring, creating a 4n+2 aromatic system (see Huckel's rule) similar to benzene.  Because of the aromaticity, the molecule is flat and lacks discrete double bonds. The other lone pair of electrons of the oxygen atom extends in the plane of the flat ring system.  The sp2 hybridization is to allow one of the lone pairs of oxygen to reside in a p orbital and thus allow it to interact within the pi-system.
The name furan comes from the Latin furfur, which means bran. The first furan derivative to be described was 2-furoic acid, by Carl Wilhelm Scheele in 1780. Another important derivative, furfural, was reported by Johann Wolfgang Dobereiner in 1831 and characterised nine years later by John Stenhouse. Furan itself was first prepared by Heinrich Limpricht in 1870, although he called it tetraphenol.

# Synthesis and isolation
- Furan can be obtained from furfural by oxidation and decarboxylation of the resulting furan-2-carboxylic acid, the furfural being derived by destructive distillation of corn cobs in the presence of sulfuric acid.
- A classic furan organic synthesis is the Feist-Benary synthesis.
- One of the most simple synthesis methods for furans is the reaction of 1,4-diketones with phosphorus pentoxide  (P2O5) in the Paal-Knorr Synthesis. It is interesting that the thiophene formation reaction of 1,4-diketones with Lawesson's reagent also forms furans as side products.

# Reactions
Due to its aromaticity, furan's behavior is quite dissimilar to that of the more typical heterocyclic ethers such as tetrahydrofuran. It is considerably more reactive than benzene in electrophilic substitution reactions. Furan serves as a diene in Diels-Alder reactions with electron-deficient dienophiles such as ethyl (E)-3-nitroacrylate. The reaction product is a mixture of isomers with preference for the endo isomer:
Hydrogenation of furans affords sequentially dihydrofurans and tetrahydrofurans.
Furin
Furin is a protein that in humans is encoded by the FURIN gene. Some proteins are inactive when they are first synthesized, and must have sections removed in order to become active. Furin cleaves these sections and activates the proteins. It was named furin because it was in the upstream region of an oncogene known as FES. The gene was known as FUR (FES Upstream Region) and therefore the protein was named furin. Furin is also known as PACE (Paired basic Amino acid Cleaving Enzyme).

# Function
The protein encoded by this gene is an enzyme which belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. Some of its substrates are: proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor. A furin-like pro-protein convertase has been implicated in the processing of RGMc (also called hemojuvelin), a gene involved in a severe iron-overload disorder called juvenile hemochromatosis. Both the Ganz and Rotwein groups demonstrated that furin-like proprotein convertases (PPC) are responsible for conversion of 50 kDa HJV to a 40 kDa protein with a truncated COOH-terminus, at a conserved polybasic RNRR site.  This suggests a potential mechanism to generate the soluble forms of HJV/hemojuvelin (s-hemojuvelin) found in the blood of rodents and humans.
Furin is one of the proteases responsible for the proteolytic cleavage of HIV envelope polyprotein precursor gp160 to gp120 and gp41 prior to viral assembly. This gene is thought to play a role in tumor progression. The use of alternate polyadenylation sites has been found for this gene.
Furin is enriched in the Golgi apparatus, where it functions to cleave other proteins into their mature/active forms. Furin cleaves proteins just downstream of a basic amino acid target sequence (canonically, Arg-X-(Arg/Lys) -Arg'). In addition to processing cellular precursor proteins, furin is also utilized by a number of pathogens. For example, the envelope proteins of viruses such as HIV, influenza, dengue fever and several filoviruses including ebola and marburg virus  must be cleaved by furin or furin-like proteases to become fully functional. Anthrax toxin, pseudomonas exotoxin, and papillomaviruses must be processed by furin during their initial entry into host cells. Inhibitors of furin are under consideration as therapeutic agents for treating anthrax infection.
The furin substrates and the locations of furin cleavage sites in protein sequences can be predicted by two bioinformatics methods: ProP  and PiTou.
Expression of furin in T-cells is required for maintenance of peripheral immune tolerance.

# Interactions
Furin has been shown to interact with PACS1.
G-LOC

# Overview
G-LOC, abbreviated from G-force induced Loss Of Consciousness, is a term generally used in aerospace physiology to describe a loss of consciousness arising from excessive and sustained g-forces draining blood away from the brain causing cerebral hypoxia.  The condition is most likely to affect pilots of high performance fighter and aerobatic aircraft or astronauts but is possible on some extreme amusement park rides.  G-LOC incidents have caused fatal accidents in high performance aircraft capable of sustaining high g for extended periods.  High-G training for pilots of high performance aircraft or spacecraft often includes the simulation of G-LOC in special centrifuges.  Such man-rated centrifuges are made by AMST Systemtechnik in Austria (Austria Metall SystemTechnik), Latacoere in France, the Environmental Tectonics Corporation (ETC) and Wyle Laboratories in the USA.

# Effects of g-forces
As g-force increases, or the longer it is sustained, the victim may suffer progressively:
- Brownout- a loss of colour vision
- Tunnel vision - loss of peripheral vision, retaining only the centre vision
- Blackout a complete loss of vision  but retaining consciousness.
- G-LOC where consciousness is lost.
Recovery is usually prompt following removal of g-force but a period of several seconds of disorientation may occur.  Brief but vivid dreams have been reported to follow G-LOC.
The human body is much more tolerant of g-force when it is applied laterally (across the body) than when applied longitudinally (along the length of the body).  Unfortunately most sustained g-forces incurred by pilots is applied longitudinally. This has led to experimentation with prone pilot aircraft designs which lies the pilot face down or (more successfully) reclined positions for astronauts.

# Thresholds
The g thresholds at which these effects occur depend on the training, age and fitness of the individual.  An un-trained individual not used to the g-straining manoeuvre, can black out between 4 and 6 g, particularly if this is pulled suddenly.  A trained, fit individual wearing a g suit and practising the straining manoeuvre, can, with some difficulty, sustain up to 9g without loss of consciousness.  Prone position designs in aircraft have not proved successful and the problem has been addressed largely by the development of the G-suit.
G6PC3
Glucose-6-phosphatase 3, also known as glucose-6-phosphatase beta, is an enzyme that in humans is encoded by the G6PC3 gene.

# Function
This gene encodes the catalytic subunit of glucose 6-phosphatase (G6Pase). G6Pase is located in the endoplasmic reticulum (ER) and catalyzes the hydrolysis of glucose 6-phosphate to glucose and phosphate in the last step of the gluconeogenic and glycogenolytic pathways.

# Clinical significance
Mutations in this gene result in autosomal recessive severe congenital neutropenia.
G6PC3 deficiency results in a phenotypic continuum.  At one end the affected individuals have only neutropenia and related complications but no other organ is affected. This is sometimes referred to as non-syndromic or  isolated severe congenital neutropenia. Most affected individuals have a classic form of the disease with severe congenital neutropenia and cardiovascular and/or urogenital abnormalities. Some individuals have severe G6PC3 deficiency (also known as Dursun syndrome) and they have all the features of classic G6PC3 deficiency but in addition show involvement of non-myeloid hematopoietic cell lines, some other extra-hematologic features and pulmonary hypertension.
GABPA
GA-binding protein alpha chain is a protein that in humans is encoded by the GABPA gene.

# Function
This gene encodes one of three GA-binding protein transcription factor subunits which functions as a DNA-binding subunit.  Since this subunit shares identity with a subunit encoding the nuclear respiratory factor 2 gene, it is likely involved in activation of cytochrome oxidase expression and nuclear control of mitochondrial function.  This subunit also shares identity with a subunit constituting the transcription factor E4TF1, responsible for expression of the adenovirus E4 gene.  Because of its chromosomal localization and ability to form heterodimers with other polypeptides, this gene may play a role in the Down Syndrome phenotype.

# Interactions
GABPA has been shown to interact with Host cell factor C1, Sp1 transcription factor and Sp3 transcription factor.
GABRD
Gamma-aminobutyric acid receptor subunit delta is a protein that in humans is encoded by the GABRD gene.

# Function
-Aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABAA receptors, which are ligand-gated chloride channels. The  GABAA receptor is generally pentameric. Its five subunits are alpha, beta, gamma, delta, and rho. The GABRD gene encodes the delta subunit. Specifically, the -subunit is usually expressed in GABAA receptors associated with extrasynaptic activity. The most common  GABAA receptors have the gamma subunit, which allows the receptor to bind benzodiazepines. For this reason, receptors containing -subunits are sometimes referred to as benzodiazepine insensitive  GABAA receptors. The -subunit containing receptors are also known to be involved in the ventral tegmental area (VTA) pathway in the brain's hippocampus, which means that they may have implications in learning, memory, and reward.

# Cell type-specific expression
In a technical comparison between quantitative reverse transcriptase PCR and digital PCR, the expression of the rat gabrd gene was examined across three cell types in the somatosensory cortex: neurogliaform cells, fast spiking basket cells and pyramidal cells.  Gene expression was detected in all three cell types, but showed marked enrichment in neurogliaform cells versus the other cell types examined.
GABRE
Gamma-aminobutyric acid receptor subunit epsilon is a protein that in humans is encoded by the GABRE gene.
The product of this gene belongs to the ligand-gated ionic channel (TC 1.A.9) family. It encodes the gamma-aminobutyric acid (GABA) A receptor which is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes an epsilon subunit. It is mapped to chromosome Xq28 in a cluster of genes encoding alpha 3, beta 4 and theta subunits of the same receptor. Alternatively spliced transcript variants encoding different isoforms have been identified.
Brainstem expression of  subunit-containing GABAA receptors is upregulated during pregnancy, particularly in the ventral respiratory group.
GATA5
Transcription factor GATA-5 is a protein that in humans is encoded by the GATA5 gene.

# Function
The protein encoded by this gene is a transcription factor that contains two GATA-type zinc fingers. The encoded protein is known to bind to hepatocyte nuclear factor-1alpha (HNF-1alpha), and this interaction is essential for cooperative activation of the intestinal lactase-phlorizin hydrolase promoter. In other organisms, similar proteins may be involved in the establishment of cardiac smooth muscle cell diversity.

# Role in development
Gata5 is a transcription factor. Gata5 regulates the proper development of the heart. Early in embryo development, Gata5 helps in making sure that there are enough heart muscle precursor cells produced to differentiate into the final myocardial cells. It also regulates other genes that are crucial to successful heart development. As pregnancy progresses, Gata 5 is involved in the specification of the heart tissue that becomes the ventricles. Problems can arise when Gata5 is overexpressed. This overexpression can lead to ectopic foci. Ectopic foci are also known as ectopic pacemakers. They are bundles of cells that can cause cardiac pacing that are located in places in the heart where theyre not supposed to be. These cells can become excited before the heart is supposed to be excited. This causes the heart to beat and thus contract before it should. Oftentimes, this is not a big deal and the heart naturally reverts to its normal pacing. However, if its caused by problems with development in the heart  if Gata5 did not express properly in the embryo- then this can lead to constant ectopic foci problems. These problems include tachycardia (the heart beating too fast), bradycardia (the heart beating too slow), or ventricular fibrillation which is a serious condition where the ventricles of the heart arent pumping consistently and cant get blood out to the body.
GATA6
Transcription factor GATA-6, also known as GATA-binding factor 6 (GATA6), is protein that in humans is encoded by the GATA6 gene. The gene product preferentially binds (A/T/C)GAT(A/T)(A) of the consensus binding sequence.

# Clinical significance
Mutations in the gene have been linked with pancreatic agenesis and congenital heart defects.

## Lung Endodermal Epithelial Development
GATA-6, a zinc finger transcription factor, is important in the endodermal differentiation of organ tissues. It is also indicated in proper lung development by controlling the late differentiation stages of alveolar epithelium and aquaporin-5 promoter activation. Furthermore, GATA-6 has been linked to the production of LIF, a cytokine that encourages proliferation of endodermal embryonic stem cells and blocks early epiblast differentiation. If left unregulated in the developing embryo, this cytokine production and chemical signal contributes to the phenotypes discussed further below.
Upon the disruption of GATA-6 in an embryo, the distal lung epithelial development is stunted in transgenic mice models The progenitor cells, or stem cells, for alveolar epithelial tissues develop and are specified appropriately, however further differentiation does not occur. Also the distal-proximal bronchiole development is affected, resulting in a reduced quantity of airway exchange sites.
This branching deficit, which will cause bilateral pulmonary hypoplasia after birth, has been locally associated with areas lacking differentiated alveolar epithelium, implicating this phenotype as inherent to endodermal function, and thus may be indirectly linked to improper GATA-6 expression. That is, a deficit of bronchiole branching may not be a result of direct transcriptional error in GATA-6, but rather a side effect of such an error.
GDF10
Growth differentiation factor 10 (GDF10) also known as bone morphogenetic protein 3B (BMP-3B) is a protein that in humans is encoded by the GDF10 gene.
GDF10 belongs to the transforming growth factor beta superfamily that is closely related to bone morphogenetic protein-3 (BMP3). It plays a role in head formation and may have multiple roles in skeletal morphogenesis. GDF10 is also known as BMP-3b, with GDF10 and BMP3 regarded as a separate subgroup within the TGF-beta superfamily.
In mice, GDF10 mRNA is abundant in the brain, inner ear, uterus, prostate, neural tissues, blood vessels and adipose tissue with low expression in spleen and liver. It is also present in bone of both adults and neonatal mice. Human GDF10 mRNA is found in the cochlea and lung of foetuses, and in testis, retina, pineal gland, and other neural tissues of adults.
GDF15
Growth/differentiation factor 15 (GDF15) was first identified as Macrophage inhibitory cytokine-1 or MIC-1.
It is a protein belonging to the transforming growth factor beta superfamily. Under normal conditions, GDF-15 is expressed in low concentrations in most organs and upregulated because of injury of organs such as such as liver, kidney, heart and lung.
The function of GDF-15 is not fully cleared but it seems to have a role in regulating inflammatory pathways and to be involved in regulating apoptosis, cell repair and cell growth, which are biological processes observed in cardiovascular and neoplastic disorders. GDF-15 has shown to be a strong prognostic protein in patients with different diseases such as heart diseases and cancer.
GFRA1
GDNF family receptor alpha-1 (GFR1), also known as the GDNF receptor, is a protein that in humans is encoded by the GFRA1 gene.

# Function
Glial cell line-derived neurotrophic factor (GDNF) and neurturin (NTN) are two structurally related, potent neurotrophic factors that play key roles in the control of neuron survival and differentiation. The protein encoded by this gene is a member of the GDNF receptor family. It is a glycosylphosphatidylinositol(GPI)-linked cell surface receptor for both GDNF and NTN, and mediates activation of the RET tyrosine kinase receptor. This gene is a candidate gene for Hirschsprung disease. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.

# Interactions
GDNF family receptor alpha 1 has been shown to interact with GDNF and RET proto-oncogene.
GGPS1
Geranylgeranyl pyrophosphate synthase is an enzyme that in humans is encoded by the GGPS1 gene.

# Function
This gene is a member of the prenyltransferase family and encodes a protein with geranylgeranyl diphosphate (GGPP) synthase activity. The enzyme catalyzes the synthesis of GGPP from farnesyl diphosphate and isopentenyl diphosphate. GGPP is an important molecule responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Much like its homolog farnesyl diphosphate synthase, GGPS1 is inhibited by bisphosphonate compounds.
GIPC3
PDZ domain-containing protein GIPC3 is a protein that in humans is encoded by the GIPC3 gene. GIPC3 is a member of the GIPC (GAIP-interacting protein C terminus) gene family that also includes GIPC1 and GIPC2. The encoded protein, GIPC3, features a centrally located PDZ domain, which is flanked on each side by a single GIPC-homology domain.

# Function
GIPC3 is thought to be important for acoustic signal acquisition and propagation in hair cells of the mammalian cochlea.

# Gene
The human GIPC3 gene is located on the short arm of chromosome 19 at p13.3. The locus extends over about 8 kbp and contains the six coding exons that give rise to an open reading frame of 639 nucleotides encoding the GIPC3 protein of 312 amino acids. A single PDZ domain is located at amino acid position 122-189.  
In the mouse, Gipc3 is located on chromosome 10 at cytogenetic band qC1. The genomic region covers a distance of 5.5 kbp. The six coding exons encode a protein of 297 amino acids. The PDZ domain is located at amino acid position 107-174.

# Genetics
In the mouse, a missense mutation in Gipc3 (c.343G>A) leads to a non-synonymous amino acid replacement (p.G115R) in the loop connecting two beta strands of the PDZ domain.  Glycine 115 is conserved in all GIPC proteins.
Missense (c.785C>T; p. L262R) and nonsense (c.903G>A, p.W301X) mutations in human GIPC3 cause congenital sensorineural hearing impairment in families segregating non-syndromic hearing loss DFNB15 and DFNB95.

# Phenotypes
Mice of the Black Swiss strain develop early-onset slowly progressing sensorineural hearing loss.  A genetic study identified two quantitative trait loci (QTL) that control hearing function.   One QTL, named age-related hearing loss 5 (ahl5) localizes to chromosome 10 and accounted for ca. 60% of the variation in hearing thresholds.  A second QTL, ahl6, localized to chromosome 18 and has a smaller effect size.  Besides their hearing impairment, Black Swiss mice also are hypersensitive to acoustic stimulation, reacting with seizures (audiogenic seizures) to loud white noise.  A genetic locus conferring susceptibility was identified (juvenile audiogenic monogenic seizures1, jams1) on chromosome 10.  A positional cloning approach aimed to decipher the genetic basis of both the hearing loss and audiogenic seizure susceptibility subsequently identified the glycine to arginine substitution in Gipc3 as the underlying cause.
In humans, individuals with the p.W301X missense mutation (DFNB95) exhibit bilateral sensorineural hearing loss with threshold shifts of 70-80 dB hearing levels as early as 11 months of age.

# Interactions
The PDZ domain of GIPC family proteins interact with:
- Frizzled-3 (FZD3) class of WNT receptor,
- insulin-like growth factor-I receptor (IGF1R),
- receptor tyrosine kinase TrkA,
- TGF-beta type III receptor (TGF-beta RIII),
- integrin alpha6A (ITGA6),
- transmembrane glycoprotein TPBG, and
- RGS19/RGS-GAIP.
GLE1L
Nucleoporin GLE1 is a protein that in humans is encoded by the GLE1 gene on chromosome 9.

# Function
This gene encodes a predicted 75-kDa polypeptide with high sequence and structure homology to yeast Gle1p, which is nuclear protein with a leucine-rich nuclear export sequence essential for poly(A)+RNA export. Inhibition of human GLE1L by microinjection of antibodies against GLE1L in HeLa cells resulted in inhibition of poly(A)+RNA export. Immunoflourescence studies show that GLE1L is localized at the nuclear pore complexes. This localization suggests that GLE1L may act at a terminal step in the export of mature RNA messages to the cytoplasm. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.

# Clinical significance
A genome-wide screening and linkage analysis assigned the disease locus of lethal congenital contracture syndrome, one of 40 Finnish heritage diseases, to a defined region of 9q34, where the GLE1 gene is located. Mutations in GLEI have been identified in families with foetal motoneuron disease.

# Interactions
GLE1L has been shown to interact with NUP155.
GLIS2
GLIS family zinc finger 2 also known as GLIS2 is a human gene.

# Function
The protein encoded by this gene is a Kruppel-like transcription factor which functions depending on the gene and promoter context as an activator or repressor of gene transcription. GLIS2 plays a role in kidney development and neurogenesis.
Glis2 knockout mice display decreased size and weight.  The kidneys in these mice show progressive kidney atrophy and display symptoms similar to human nephronophthisis. Glis2 plays an essential role in the maintenance of renal tissue through prevention of apoptosis and fibrosis.

# Clinical significance
Mutations in the GLIS2 gene are associated with nephronophthisis.