Persius/hicric huggingface dataset:
Hijama
Hijama (Arabic  lit. "sucking") is the name in Arab traditional medicine for wet cupping, where blood is drawn by vacuum from a small skin incision for therapeutic purposes.  Hijama is generally performed by Muslims as it is a form of medicine specifically mentioned and encouraged by the prophet Muhammad. Among other hadith, it is mentioned in that recorded by Imam Bukhari (5263) and Imam Muslim (2952), saying "Hijama is among your best remedies" (    ).

# Procedure
Hijama is normally performed on the head, but can be performed anywhere on the body, often at the site of an ache or pain in order to ease or alleviate it. A more conservative approached outlined at the Broken Earth Cupping Site site warns against over use of cupping and suggests only that six optimal points on the body are all that is required to clean the entire cardiovascular system (The back of the head, two shoulders corresponding to the acupuncture heart position, the tail or small of the back, and the two inner ankles).
The location is first shaved, if necessary, to ensure a tight seal with the cup. The mouth of a cup (metal, glass and plastic cups are generally used, although traditionally horns were used) is placed on the skin at the site chosen for cupping (alternatively leeches can be used). Then a tight seal is created. The old method was to burn a small piece of paper or cotton inside the vessel, so that the mouth of the cup clings to the skin. The new procedure is to use a machine instead. The cup is left to cling to the skin for a few minutes, then it is lifted off and a couple of very small incisions are made in the skin. The cup is then put back as it was before until it is filled with blood.

# Muhammad and hijama
According to various hadith in the Islamic tradition, Muhammad supported hijama. They include:
- Abu Kabsha al-Anmairi gave an eyewitness testimony that Muhammad cupped himself on the head and between his shoulders and then said "Whoever sheds some of this blood will experience no pain in not being treated for a certain (disease) with a certain (cure)".
- Anas's account is more anatomically precise, explaining that Muhammad cupped on two different neck veins and on the upper back.
- According to Jabir, Muhammad also cupped his hip to relieve some pain there.
- According to Abu Hurayra, Muhammad said "If there is good in one thing which cures you it is cupping".
- Also on Abu Hurarya's authority, Muhammad said that "Whoever is cupped on the seventeenth, nineteenth, or twenty-first (of the lunar month) will be healed of every disease".
Hunger
Hunger is a feeling experienced when the glycogen level of the liver falls below a threshold, usually followed by a desire to eat.  The usually unpleasant feeling originates in the hypothalamus and is released through receptors in the liver. Although an average nourished human can survive weeks without food intake, the sensation of hunger typically begins after several hours without eating.
Hunger can also be applied metaphorically to cravings of other sorts, e.g. "hungry for victory."
- Drug causes
Chlorpropamide
Pergolide
- Chlorpropamide
- Pergolide

# Hunger pains
When hunger contractions occur in the stomach, the person sometimes experiences mild pain in the pit of the stomach, called hunger pangs. Hunger pangs usually do not begin until 12 to 24 hours after the last ingestion of food, in starvation. A single hunger contraction lasts about 30 seconds, and pangs continue for around 30-45 minutes, then hunger subsides for around 30-150 minutes. Individual contractions are separated at first, but are almost continuous after a time. Emotional states (anger, joy etc.) may inhibit hunger contractions. Levels of hunger are increased by lower blood sugar levels, and are higher in diabetics. They reach their greatest intensity in 3 to 4 days and may weaken in the succeeding days, though hunger never disappears. Hunger contractions are most intense in young, healthy people who have high degrees of gastrointestinal tonus. Periods between contractions increase with old age.

# Satiety
Satiety, or the feeling of fullness, is the disappearance of hunger after a meal. It is a process mediated by the ventromedial nucleus in the hypothalamus. It is therefore the "satiety center."
Various hormones, first of all cholecystokinin, have been implicated in conveying the feeling of satiety to the brain. Leptin increases on satiety, while ghrelin increases when the stomach is empty.
Therefore, satiety refers to the psychological feeling of "fullness" or satisfaction rather than to the physical feeling of being engorged, i.e. the feeling of physical fullness after eating a very large meal.
Satiety directly influences feelings of appetite that are generated in the limbic system, and hunger that is controlled by neurohormones,  especially serotonin in the lateral hypothalamus.lll

# Behavioral response
Hunger appears to increase activity and movement in many animals - for example an experiment on spiders showed increased activity and predation in starved spiders, resulting in larger weight gain. This pattern is seen in many animals, including humans while sleeping. It even occurs in rats with their cerebral cortex or stomachs completely removed. Increased activity on hamster wheels occurred when rats were deprived not only of food, but also water or B vitamins such as thiamine This response may increase the animal's chance of finding food, though it has also been speculated the reaction relieves pressure on the home population.
Hygeia
In Greek mythology, Hygieia was a daughter of Asclepius.  She was the goddess of health, cleanliness and sanitation and afterwards, the moon. She also played an important part in her father's cult. While her father was more directly associated with healing, she was associated with the prevention of sickness and the continuation of good health.
Hygieia was the subject of a local cult since at least the 7th century BC, (it is highly probable that Greek hygiene and health development began from influences of the Celts and the world's first hospital situated in Armagh Ireland. It was built before 650 BC by Queen Macha.) "Athena Hygieia" was one of the titles given to Athene, as Plutarch recounts:
However, the cult of Hygieia as an independent goddess did not begin to spread out until the Oracle at Delphi recognized her, and after the devastating Athens plague in 429 and 427 BC and in Rome in 293 BC.  Her primary temples were in Epidaurus, Corinth, Cos and Pergamon. Pausanias remarked that, at the asclepieion of Titane in Sicyon (founded by Alexanor, Asclepius' grandson), statues of Hygieia were covered by women's hair and pieces of Babylonian clothes.  According to inscriptions, the same sacrifices were offered at Paros.
Ariphron, a Sicyonian artist from the 4th century BC wrote a well-known hymn celebrating her.  Statues of Hygieia were created by Scopas, Bryaxis and Timotheus, among others. She was often depicted as a young woman feeding a large snake that was wrapped around her body.  Sometimes the snake would be drinking from a jar that she carried. These attributes were later adopted by the Gallo-Roman healing goddess, Sirona. Hygieia was accompanied by her brother, Telesphorus. Her name is the source of the word "hygiene".

# Salus
In Roman mythology, Salus was worshipped extensively by the Romans. Under the name Salus Publica Populi Romani ("goddess of the public welfare of the Roman people"), there was a temple devoted to her on the Quirinal Hill. It was built in 302 BC. She was depicted with snakes and a bowl in many artistic representations of her. Her festival took place on March 30th. Her name is Latin for "health" and is the source of the English words salubrity, salutation etc.
IFITM3
Interferon-induced transmembrane protein 3 (IFITM3) is a protein that in humans is encoded by the IFITM3 gene.  It plays a critical role in the immune system's defense against Swine Flu, where heightened levels of IFITM3 keep viral levels low, and the removal of IFITM3 allows the virus to multiply unchecked. This observation has been further advanced by a recent study that shows that a single nucleotide polymorphism in the human IFITM3 gene purported to increase influenza susceptibility is overrepresented in people hospitalised with pandemic H1N1. The prevalence of this mutation is thought to be approximately 1/400 in European populations.

# Model organisms
Model organisms have been used in the study of IFITM3 function. A conditional knockout mouse line, called Ifitm3tm1Masu 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  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty four tests were carried out on mutant mice, but no significant abnormalities were observed. However, challenge with influenza A virus indicated that these mice display increased viral susceptibility.
IFT140
IFT140, Intraflagellar transport 140 homolog, is a protein that in humans is encoded by the IFT140 gene.

# Clinical significance
Mutations in this gene have been associated to cases of skeletal ciliopathy.

# Model organisms
Model organisms have been used in the study of IFT140 function. A conditional knockout mouse line called Ift140tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Additional screens performed:  - In-depth immunological phenotyping
IGFALS
Insulin-like growth factor binding protein, acid labile subunit, also known as IGFALS, is a protein which in humans is encoded by the IGFALS  gene.

# Function
The protein encoded by this gene is a serum protein that binds insulin-like growth factors, increasing their half-life and their vascular localization. Production of the encoded protein, which contains twenty leucine-rich repeats, is stimulated by growth hormone. Three transcript variants encoding two different isoforms have been found for this gene.

# Clinical significance
Defects in this gene are a cause of acid-labile subunit deficiency, which manifests itself in a delayed and slow puberty.

# Interactions
IGFALS has been shown to interact with IGFBP3.
IGFBP4
Insulin-like growth factor-binding protein 4 is a protein that in humans is encoded by the IGFBP4 gene.

# Function
This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma in both glycosylated and non-glycosylated forms. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors.
IGFBP-4 is a unique protein and it consistently inhibits several cancer cells in vivo and in vitro. Its inhibitory action has been shown in vivo in prostate and colon. It is secreted by all colon cancer cells.

# Clinical significance
The protein itself does not prevent the formation of cancer. However it may reduce the growth of cancer and act as an apoptotic factor.

# Interactions
IGFBP4 has been shown to interact with Insulin-like growth factor 1 and 2.
IL1RAP
Interleukin-1 receptor accessory protein is a protein that in humans is encoded by the IL1RAP gene.
Interleukin 1 induces synthesis of acute phase and proinflammatory proteins during infection, tissue damage, or stress, by forming a complex at the cell membrane with an interleukin 1 receptor and an accessory protein. This gene encodes an interleukin 1 receptor accessory protein. Alternative splicing of this gene results in two transcript variants encoding two different isoforms, one membrane-bound and one soluble.

# Interactions
IL1RAP has been shown to interact with TOLLIP and Interleukin 1 receptor, type I.
IL1RL1
Interleukin 1 receptor-like 1, also known as IL1RL1 and ST2, is a protein that in humans is encoded by the IL1RL1 gene.

# Function
IL1RL1 is a member of the Toll-like receptor superfamily based on the function of its intracelluar TIR domain, but its extracellular region is composed of immunoglobulin domains. Unlike other members of the family IL1RL1 does not induce an inflammatory response through activation of NF-B, although it does activate MAP kinases.
ST2 is a member of the interleukin 1 receptor family. The ST2 protein has two isoforms and is directly implicated in the progression of cardiac disease: a soluble form (referred to as soluble ST2 or sST2) and a membrane-bound receptor form (referred to as the ST2 receptor or ST2L). When the myocardium is stretched, the ST2 gene is upregulated, increasing the concentration of circulating soluble ST2. The ligand for ST2 is the cytokine Interleukin-33(IL-33). Binding of IL-33 to the ST2 receptor, in response to cardiac disease or injury, such as an ischemic event, elicits a cardioprotective effect resulting in preserved cardiac function.  This cardioprotective IL-33 signal is counterbalanced by the level of soluble ST2, which binds IL-33 and makes it unavailable to the ST2 receptor for cardioprotective signaling. As a result, the heart is subjected to greater stress in the presence of high levels of soluble ST2.

# Molecular biology
The gene is found on the long arm of Chromosome 2 (2q12). It is 40,536 bases long and is located on the Watson (plus) strand. It encodes a protein of 556 amino acids (molecular weight 63,358 Da). Both membrane bound and soluble forms are known. The protein is known to interact with MyD88, IRAK1, IRAK4 and TRAF6. It appears to be essential for the normal function of T helper cells type 2 (Th2 cells) .

# Clinical significance
Mutations in this gene have been linked to atopic dermatitis and asthma.
The protein encoded by this gene serves as a cardiac biomarker.
IMMP2L
Inner mitochondrial membrane peptidase subunit 2 (IMMP2L) is an enzyme that in humans is encoded by the IMMP2L gene on chromosome 7. This  protein catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. IMMP2L processes the nuclear encoded protein DIABLO.

# Structure

## Gene
The gene IMMP2L encodes protein Inner mitochondrial membrane peptidase subunit 2 in human. The human IMMP2L gene has 18 exons and locates at chromosome band 7q31.

## Protein
The human protein Inner mitochondrial membrane peptidase subunit 2 has two isoforms due to alternative splicing. One isoform is 19.7 kDa in size and composed of 175 amino acids. The calculated theoretical pI of this protein isoform is 8.66. The other isoform is 12.3kDa in size and composed of 110 amino acids. The calculated theoretical pI of this protein isoform is 9.42.

# Function
As a peptidase, this  protein catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoding DIABLO protein.

# Clinical significance
Gilles de la Tourette syndrome (GTS) is a complex neuropsychiatric disorder characterized by multiple motor and phonic tics. In the clinical characterization of a patient with GTS, Petek et al discovered a breakpoint in chromosome region 7q31. Additional characterization identified that IMMP2L, a novel gene coding for the apparent human homologue of the yeast mitochondrial inner membrane peptidase subunit 2, was found to be disrupted by both the breakpoint in the duplicated fragment and the insertion site in 7q31. It is the first association of IMMP2L gene to Tourette syndrome. 
Recent investigation by Bertelsen et al. further indicated that IMMP2L was one of the genes as a susceptibility factor in disease pathogenesis. Tourette syndrome is often accompanied by comorbidities such as attention-deficit hyperactivity-disorder and obsessive compulsive disorder. Tourette syndrome has a complex etiology and the underlying environmental and genetic factors responsible for this disease are still largely unknown.
IMPDH1
Inosine-5'-monophosphate dehydrogenase 1, also known as IMP dehydrogenase 1, is an enzyme that in humans is encoded by the IMPDH1 gene.

# Function
IMP dehydrogenase 1 acts as a homotetramer to regulate cell growth. IMPDH1 is an enzyme that catalyzes the synthesis of xanthine monophosphate (XMP) from inosine-5'-monophosphate (IMP). This is the rate-limiting step in the de novo synthesis of guanine nucleotides.

# Clinical significance
Defects in the IMPDH1 gene are a cause of retinitis pigmentosa type 10 (RP10).
IMPDH2
Inosine-5'-monophosphate dehydrogenase 2, also known as IMP dehydrogenase 2, is an enzyme that in humans is encoded by the IMPDH2 gene.

# Function
IMP dehydrogenase 2 is the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. It is thus involved in maintaining cellular guanine deoxy- and ribonucleotide pools needed for DNA and RNA synthesis. IMPDH2 catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is then converted into guanosine-5'-monophosphate. IMPDH2 has been identified as an intracellular target of the natural product sanglifehrin A

# Clinical significance
This gene is up-regulated in some neoplasms, suggesting it may play a role in malignant transformation.
INCENP
Inner centromere protein is a protein that in humans is encoded by the INCENP gene.
In mammalian cells, two broad groups of centromere-interacting proteins have been described: constitutively binding centromere proteins and 'passenger' (or transiently interacting) proteins. The constitutive proteins include CENPA (centromere protein A), CENPB, CENPC1, and CENPD.
The term 'passenger proteins' encompasses a broad collection of proteins that localize to the centromere during specific stages of the cell cycle. These include CENPE; MCAK; KID; cytoplasmic dynein (e.g., DYNC1H1); CliPs (e.g. CLIP1); and CENPF/mitosin (CENPF). The inner centromere proteins (INCENPs), the initial members of the passenger protein group, display a broad localization along chromosomes in the early stages of mitosis but gradually become concentrated at centromeres as the cell cycle progresses into mid-metaphase. During telophase, the proteins are located within the midbody in the intercellular bridge, where they are discarded after cytokinesis.
INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N-terminal domain of INCENP is the domain involved in formation of this three-helical bundle.

# Interactions
INCENP has been shown to interact with H2AFZ, Survivin and CDCA8. The ARK binding region has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.
INPP5D
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 is an enzyme that in humans is encoded by the INPP5D gene.

# Function
This gene is a member of the inositol polyphosphate-5-phosphatase (INPP5) family and encodes a protein with an N-terminal SH2 domain, an inositol phosphatase domain, and two C-terminal protein interaction domains. Expression of this protein is restricted to hematopoietic cells where its movement from the cytosol to the plasma membrane is mediated by tyrosine phosphorylation. At the plasma membrane, the protein hydrolyzes the 5' phosphate from phosphatidylinositol (3,4,5)-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, thereby affecting multiple signaling pathways. Overall, the protein functions as a negative regulator of myeloid cell proliferation and survival. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

# Interactions
INPP5D has been shown to interact with DOK2, LYN, CD22, Grb2, CRKL, CD31, DOK1 and SHC1.

# Medicines
Rosiptor (AQX-1125) is an INPP5D activator that is under development as an anti-inflammatory drug.
INTS12
Integrator complex subunit 12 (Int12) also known as PHD finger protein 22 (PHF22) is a protein that in humans is encoded by the INTS12 gene.
INTS12 is a subunit of the Integrator complex, which associates with the C-terminal domain of RNA polymerase II large subunit (POLR2A) and mediates 3-prime end processing of small nuclear RNAs U1 (RNU1) and U2 (RNU2)

# Model organisms
Model organisms have been used in the study of INTS12 function. A conditional knockout mouse line, called Ints12tm1a(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 seven tests were carried out on mutant mice and two significant abnormalities were observed.  No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.
IQSEC1
IQ motif and SEC7 domain-containing protein 1  also known as ARF-GEP100 (ADP-Ribosylation Factor - Guanine nucleotide-Exchange Protein -  100-kDa) is a protein that in humans is encoded by the IQSEC1 gene.

# Function
The ARF-GEP100 protein is involved in signal transduction. It is a guanine nucleotide exchange factor that promotes binding of GTP to ADP ribosylation factor protein ARF6 and to a lesser extent ARF1 and ARF5. This activates the ADP-ribosylation activity of the target protein and cause it to modify its substrates. ARF-GEP100, through activation of ARF6, is therefore involved in the control of processes such as endocytosis of plasma membrane proteins, E-cadherin recycling and actin cytoskeleton remodeling. ARF-GEP100 appears particularly important in regulating cell adhesion, with reductions in the level of this protein causing enhanced spreading and attachment of cells.
It is highly expressed in the prefrontal cortex, and throughout the rest of the brain, and is believed to have a role in learning and memory, having been detected as phosphorylated in a phospho screen of the PSD.
IQSEC3
IQSEC3 is a human gene, known as IQ motif and Sec7 domain 3.
It contains an IQ domain, followed by a SEC7 and then a PH. It functions as an ARF-GEF for the ARF family of GTPases, which is to say that it causes GDP to release, and GTP to bind, thereby activating the ARF protein.
It is highly expressed in the brain, particularly in the amygdala, and is known to have a role in learning.
In a largescale phospho screening of the PSD, it was found to be phosphorylated following activation of the NMDAR complex.
IQSEC3 was originally known as 'KIAA1110', under which name it was found to act as a GEF for Arf1 but not Arf6. It is related to the other Arf-GEF protein IQSEC1.
ITGA11
Integrin alpha-11 is a protein that, in humans, is encoded by the ITGA11 gene.
This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This protein contains an I domain, is expressed in muscle tissue, dimerizes with beta 1 integrin in vitro, and appears to bind collagen in this form. Therefore, the protein may be involved in attaching muscle tissue to the extracellular matrix. Alternative transcriptional splice variants have been found for this gene, but their biological validity is not determined.
According to one study, ITGA11 expression is increased in the anterior stroma of corneal buttons excised from the eyes affected by keratoconus.