Persius/hicric huggingface dataset:
Iboga
Iboga (Tabernanthe iboga), also known as Black bugbane, is a perennial rainforest shrub and hallucinogen, native to western Africa. Iboga stimulates the central nervous system when taken in small doses and induces visions in larger doses.
Normally growing to a height of 2 m, T. iboga may eventually grow into a small tree up to 10 m tall, given the right conditions. It has small green leaves. Its flowers are white and pink, while the elongated, oval-shaped fruit are orange. Its yellow-coloured roots contains a number of indole alkaloids, most notably ibogaine, which is found in the highest concentration in the root-bark. The root material, bitter in taste, causes an anaesthetic sensation in the mouth as well as systemic numbness to the skin.

# Traditional use
The Iboga tree is the central pillar of the Bwiti religion practiced in West-Central Africa, mainly Gabon, Cameroon and the Republic of the Congo, which utilises the alkaloid-containing roots of the plant in a number of ceremonies. Iboga is taken in massive doses by initiates when entering the religion, and on a more regular basis is eaten in smaller doses in connection with rituals and tribal dances, which is usually performed at night time. Bwitists have been subject to persecution by Catholic missionaries, who to this day are thoroughly opposed to the growing religious movement of Bwiti. Leon M'ba, before becoming the first President of Gabon in 1960, defended the Bwiti religion and the use of iboga in French colonial courts. On June 6, 2000, the Council of Ministers of the Republic of Gabon declared Tabernanthe iboga to be a national treasure.

# Addiction treatment
Outside Africa, iboga extracts as well as the purified alkaloid ibogaine are used in treating opiate addiction. The therapy may last several days and upon completion the subject is generally no longer physically dependent. One methadone patient said in the Dutch behind-the-news show Twee Vandaag that in just four days he reached a state that normally would have taken him three months, but without the agony. Evidence suggests that ibogaine may also help to interrupt addiction to alcohol and nicotine.  The pharmacological effects are rather undisputed with hundreds of peer reviewed papers in support but formal clinical studies have not been completed.

# Legal status
Iboga is outlawed or restricted in Belgium, Denmark,  France, Sweden, Switzerland and the United States. Root material and extracts thereof is obtainable through various European smart shops.

# Quotations
- "The Catholic church is a beautiful theory for Sunday, the iboga on the contrary is the practice of everyday living. In church, they speak of God, with iboga, you live God" (Nengue Me Ndjoung Isidore, ecumenical Bwitist religious leader)
Ichor
In Greek mythology, ichor (Greek Template:Polytonic) is the mineral that is the Greek gods' blood, sometimes said to have been present in ambrosia or nectar.  When a god was injured and bled, the ichor made his or her blood poisonous to mortals.
Ichor has also been used to mean the blood in a vampire's veins.  Whereas many vampire stories and movies describe them as having reddish or dark red blood, others describe vampire blood as being different from human blood altogetheran ichor that is traditionally dark green in color.
H. P. Lovecraft often used ichor in his descriptions of other-worldly creatures, most prominently in his nightmarish detail of the chimeric remains of Wilbur Whateley, in "The Dunwich Horror".
The term ichor is often misused in fantasy contexts by authors trying to find a different word for "blood" or "ooze", to the point that it has become cliche.  Author Ursula LeGuin, in "From Elfland to Poughkeepsie", calls the term "the infallible touchstone of the seventh-rate."
Ichor has also been used in science fiction as an alien substitute for blood, as in Garth Nix's book Shade's Children. Additionally, in the Dragonriders of Pern novel series, Anne McCaffrey refers to the blood of the alien (but genetically enhanced by humans) Pernese dragons as ichor.
Ileum

# Overview
In anatomy of the digestive system, the ileum is the final section of the small intestine.  It is about 2-4 m long in humans, follows the duodenum and jejunum, and is separated from the cecum by the ileocecal valve (ICV). The pH in the ileum is usually between 7 and 8 (neutral or slightly alkaline).

# Function
Its function is mainly to absorb vitamin B12 and bile salts and whatever products of digestion that were not absorbed by the jejunum. The wall itself is made up of folds, each of which has many tiny finger-like projections known as villi, on its surface. In turn, the epithelial cells which line these villi possess even larger numbers of microvilli. Therefore the ileum has an extremely large surface area both for the adsorption (attachment) of enzyme molecules and for the absorption of products of digestion. The DNES (diffuse neuroendocrine system)cells that line the ileum contain the protease and carbohydrase enzymes (gastrin, secretin, cholecystokinin) responsible for the final stages of protein and carbohydrate digestion. These enzymes are present in the cytoplasm of the epithelial cells. The villi contain large numbers of capillaries which take the amino acids and glucose produced by digestion to the hepatic portal vein and the liver.
Lacteals are small lymph vessels, and are present in villi. They absorb fatty acid and glycerol, the products of fat digestion. Layers of circular and longitudinal smooth muscle enable the digested food to be pushed along the ileum by waves of muscle contractions called peristalsis.

# Differences between jejunum and ileum
There is no line of demarcation between the jejunum and the ileum. There are, however, subtle differences between the two.
- The ileum has more fat inside the mesentery than the jejunum.
- The ileum is a paler color, and tends to be of a smaller caliber as well.
- While the length of the intestinal tract contains lymphoid tissue, only the ileum has abundant Peyer's patches.
These unencapsulated lymphoid nodules contain large amounts of lymphocytes and other cells of the immune system.

# Embryology
In the fetus the ileum is connected to the navel by the vitelline duct. In roughly 3% of humans, this duct fails to close during the first seven weeks after birth, causing a condition called Meckel's diverticulum.

# Veterinary anatomy
In veterinary anatomy, the ileum is distinguished from the jejunum by being that portion of the jejunoileum that is connected to the caecum by the ileocaecal fold.

# Additional images
- Inferior ileocecal fossa.
- Arteries of cecum and vermiform process.
- Goblet cell in ileum
Joule
The joule (Template:PronEng or Template:IPA) (symbol: J) is the SI unit of energy. It was named after James Prescott Joule for his work on the relationship between heat, electricity and mechanical work.

# Description
One joule is the work done, or energy expended, by a force of one newton moving  one meter along the direction of the force. This quantity is also denoted as a newton-meter with the symbol Nm.  Note that torque also has the same units as work, but the quantities are not identical.  In elementary units:
One joule is also:
- The work required to move an electric charge of one coulomb through an electrical potential difference of one volt; or one coulomb volt, with the symbol CV.
- The work done to produce power of one watt continuously for one second; or one watt second (compare kilowatt-hour), with the symbol Ws. Thus a kilowatt-hour is 3,600,000 joules or 3.6 megajoules

# History
A joule is the mechanical equivalent of heat meaning the number of units of work in which the unit of heat can perform.. Its value was found by James Prescott Joule in experiments that showed the mechanical energy Joule's equivalent, and represented by the symbol J. The term was first introduced by Dr. Mayer of Heilbronn.

# Conversions
1 joule is exactly 107 ergs.
1 joule is approximately equal to:
- 6.24150636309 Template:E eV (electronvolts)
- 0.238845896628 cal (calorie) (small calories, lower case c)
- 2.390 Template:E kilocalorie, Calories (food energy, upper case C)
- 9.47817120313 Template:E BTU (British thermal unit)
- 0.737562149277 ftlbf (foot-pound force)
- 23.7 ftpdl (foot poundals)
- 2.7778 Template:E kilowatt-hour
- 2.7778 Template:E watt-hour
- 9.8692 Template:E litre-atmosphere
Units defined in terms of the joule include:
- 1 thermochemical calorie = 4.184 J
- 1 International Table calorie = 4.1868 J
- 1 watt-hour = 3600 J
- 1 kilowatt-hour = 3.6 Template:E J (or 3.6 MJ)
Useful to remember:
- 1 joule = 1 newton-metre = 1 watt-second
1 joule in everyday life is approximately:
- the energy required to lift a small apple one meter straight up.
- the energy released when that same apple falls one meter to the ground.
- the amount of energy, as heat, that a quiet person produces every hundredth of a second.
- the energy required to heat one gram of dry, cool air by 1 degree Celsius.
- one hundredth of the energy a person can get by drinking a single drop of beer.

## SI multiples
KCNA2
Potassium voltage-gated channel subfamily A member 2 also known as Kv1.2 is a protein that in humans is encoded by the KCNA2 gene.

# Function
Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, members of which allow nerve cells to efficiently repolarize following an action potential. The coding region of this gene is intronless, and the gene is clustered with genes KCNA3 and KCNA10 on chromosome 1.

# Interactions
KCNA2 has been shown to interact with KCNA4, DLG4, PTPRA, KCNAB2, RHOA and Cortactin.

# Clinical
Mutations in this gene have been associated with hereditary spastic paraplegia.
KCNA4
Potassium voltage-gated channel subfamily A member 4 also known as Kv1.4 is a protein that in humans is encoded by the KCNA4 gene. It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.

# Description
Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the A-type potassium current class, the members of which may be important in the regulation of the fast repolarizing phase of action potentials in heart and thus may influence the duration of cardiac action potential. The coding region of this gene is intronless, and the gene is clustered with genes KCNA3 and KCNA10 on chromosome 1 in humans.
KCNA4 (Kv1.4) contains a tandem inactivation domain at the N terminus. It is composed of two subdomains. Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N terminus anchored at a 5-turn helix, and is thought to work by occluding the ion pathway, as is the case with a classical ball domain. Inactivation domain 2 (ID2, residues 40-50) is a 2.5 turn helix with a high proportion of hydrophobic residues that probably serves to attach ID1 to the cytoplasmic face of the channel. In this way, it can promote rapid access of ID1 to the receptor site in the open channel. ID1 and ID2 function together to bring about fast inactivation of the Kv1.4 channel, which is important for the role of the channel in short-term plasticity.

# Interactions
KCNA4 has been shown to interact with DLG4, KCNA2 and DLG1.
KCNA5
Potassium voltage-gated channel, shaker-related subfamily, member 5, also known as KCNA5 or Kv1.5, is a protein that in humans is encoded by the KCNA5 gene.

# Function
Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. KCNA5 encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, the function of which could restore the resting membrane potential of beta cells after depolarization, thereby contributing to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12. Mutations in this gene have been related to both atrial fibrillation  and sudden cardiac death. KCNA5 are also key players in pulmonary vascular function, where they play a role in setting the resting membrane potential and its involvement during hypoxic pulmonary vasoconstriction.

# Interactions
KCNA5 has been shown to interact with DLG4 and Actinin, alpha 2.
KCNC1
Potassium voltage-gated channel subfamily C member 1 is a protein that in humans is encoded by the KCNC1 gene.
The Shaker gene family of Drosophila encodes components of voltage-gated potassium channels and comprises four subfamilies. Based on sequence similarity, this gene is similar to one of these subfamilies, namely the Shaw subfamily. The protein encoded by this gene belongs to the delayed rectifier class of channel proteins and is an integral membrane protein that mediates the voltage-dependent potassium ion permeability of excitable membranes.

# Expression pattern
Kv3.1 and Kv3.2 channels are prominently expressed in neurons that fire at high frequency. Kv3.1 channels are prominently expressed in brain (cerebellum > globus pallidus, subthalamic nucleus, substantia nigra > reticular thalamic nuclei, cortical and hippocampal interneurons > inferior colliculi, cochlear and vestibular nuclei), and in retinal ganglion cells.

# Physiological role
Kv3.1/Kv3.2 conductance is necessary and kinetically optimized for high-frequency action potential generation. Kv3.1 channels are important for the high-firing frequency of auditory and fast-spiking GABAergic interneurons, retinal ganglion cells; regulation of action potential duration in presynaptic terminals.

# Pharmacological properties
Kv3.1 currents in heterologous systems are highly sensitive to external tetraethylammonium (TEA) or 4-aminopyridine (4-AP) (IC50 values are 0.2 mM and 29 M respectively). This can be useful in identifying native channels. The overlapping sensitivity of potassium current to both 0.5 mM TEA and 30 M 4-AP strongly suggest an action on Kv3.1 subunits.

# Transcript variants
There are two transcript variants of Kv3.1 gene: Kv3.1a and Kv3.1b. Kv3.1 isoforms differ only in their C-terminal sequence.

# Clinical significance
A missense mutation c.959G>A (p.Arg320His) in KCNC1 causes progressive myoclonus epilepsy.
KCNC2
Potassium voltage-gated channel subfamily C member 2 is a protein that in humans is encoded by the KCNC2 gene. The protein encoded by this gene is a voltage-gated potassium channel subunit (Kv3.2).

# Expression pattern
Kv3.1 and Kv3.2 channels are prominently expressed in neurons that fire at high frequency. Kv3.2 channels are prominently expressed in brain (fast-spiking GABAergic interneurons of the neocortex, hippocampus, and caudate nucleus; terminal fields of thalamocortical projections), and in retinal ganglion cells.

# Physiological role
Kv3.1/Kv3.2 conductance is necessary and kinetically optimized for high-frequency action potential generation. Sometimes in heteromeric complexes with Kv3.1; important for the high-frequency firing of fast spiking GABAergic interneurons and retinal ganglion cells; and GABA release via regulation of action potential duration in presynaptic terminals.

# Pharmacological properties
Kv3.2 currents in heterologous systems are highly sensitive to external tetraethylammonium (TEA) or 4-aminopyridine (4-AP) (IC50 values are 0.1 mM for both of the drugs). This can be useful in identifying native channels.

# Transcript variants
There are four transcript variants of Kv3.2 gene: Kv3.2a, Kv3.2b, Kv3.2c, Kv3.2d. Kv3.2 isoforms differ only in their C-terminal sequence.
KCND3
Potassium voltage-gated channel subfamily D member 3 also known as Kv4.3 is a protein that in humans is encoded by the KCND3 gene. It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.

# Function
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes  shaker, shaw, shab, and shal  have been identified in Drosophila, and each has been shown to have human homolog(s).
Kv4.3 is a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This member includes two isoforms with different sizes, which are encoded by alternatively spliced transcript variants of this gene.

# Clinical significance
Gain of function is believed to cause Brugada Syndrome although only indirectly shown by mutations in the beta subunit KCNE3 which causes gain of function of Kv4.3.
KCNH1
Potassium voltage-gated channel subfamily H member 1 is a protein that in humans is encoded by the KCNH1 gene.
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. It is activated at the onset of myoblast differentiation. The gene is highly expressed in brain and in myoblasts. Overexpression of the gene may confer a growth advantage to cancer cells and favor tumor cell proliferation. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms.

# Interactions
KCNH1 has been shown to interact with KCNB1.

# Pathologies
A recent study has shown that de novo missense mutations in the KCNH1 gene results in deleterious gain of function, resulting in a multisystem developmental disorder known as Temple-Baraitser syndrome (TBS). TBS is categorized by intellectual disabilities, epilepsy, and aplasia of the nails. Simons et al. suggested that mutational mosaicism present in the mothers of some probands was responsible for their children's TBS phenotype. This is further evidence of the role that genetic mosaicism plays in the etiology of neurological disorders.
KCNH5
Potassium voltage-gated channel, subfamily H (eag-related), member 5, also known as KCNH5, is a human gene encoding the Kv10.2 protein.
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. This gene is not expressed in differentiating myoblasts. Alternative splicing results in three transcript variants encoding distinct isoforms.
Mutations in this gene have been linked to cases of early onset Epilepsy.(10.1111/epi.12201)
KCNJ5
G protein-activated inward rectifier potassium channel 4 is a protein that in humans is encoded by the KCNJ5 gene and is a type of G protein-gated ion channel.

# Function
Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins. It may associate with other G-protein-activated potassium channel subunits to form a heterotetrameric pore-forming complex.
In humans KCNJ5 is mainly expressed in adrenal gland and pituitary, although it is also detected at low levels in pancreas, spleen, lung, heart and brain . Consistent with this expression pattern, mutations in KCNJ5/Kir3.4 can cause familial hyperaldosteronism type III and a type of long QT syndrome.

# Interactions
KCNJ5 has been shown to interact with KCNJ3.
KCNK2
Potassium channel subfamily K member 2 is a protein that in humans is encoded by the KCNK2 gene.
This gene encodes K2P2.1, one of the members of the two-pore-domain background potassium channel protein family. This type of potassium channel is formed by two homodimers that create a channel that leaks potassium out of the cell to control resting membrane potential. The channel can be opened, however, by certain anesthetics, membrane stretching, intracellular acidosis, and heat. Three transcript variants encoding different isoforms have been found for this gene.

# Function in neurons
Another name for this channel is TREK-1. TREK-1 is part of the subfamily of mechano-gated potassium channels that are present in mammalian neurons.  They can be gated in both chemical and physical ways and can be opened via both physical stimuli and chemical stimuli.  TREK-1 channels are found in a variety of tissues, but are particularly abundant in the brain and heart and are seen in various types of neurons.  The  C-terminal of TREK-1 channels plays a role in the mechanosensitivity of the channels.
In the neurons of the central nervous system, TREK-1 channels are important in physiological, pathophysiological, and pharmacological processes, including having a role in  electrogenesis, ischemia, and anesthesia. TREK-1 has an important role in neuroprotection against epilepsy and brain and spinal cord ischemia and is being evaluated as a potential target for new developments of therapeutic agents for neurology and anesthesiology.
In the absence of a properly functioning cytoskeleton, TREK-1 channels can still open via mechanical gating.  The cell membrane functions independently of the cytoskeleton and the thickness and curvature of the membrane is able to modulate the activity of the TREK-1 channels. The insertion of certain compounds into the membrane is thought to mediate the opening of TREK-1 by forming a curve in the membrane.