Persius/hicric huggingface dataset:
Hoof
A hoof is the tip of a toe of an ungulate mammal, strengthened by a thick horny (keratin) covering.  The hoof consists of a hard or rubbery sole, and a hard wall formed by a thick nail rolled around the tip of the toe.  The weight of the animal is normally borne by both the sole and the edge of the hoof wall.  Hooves grow continuously, and are constantly worn down by use.  "Hoof" is Template:PronEng or Template:IPA; the plural is either hooves (Template:PronEng or Template:IPA), or hoofs (Template:IPA).
Most even-toed ungulates (such as sheep, goats, deer, cattle, bison, and pigs) have two main hooves on each foot, together called a cloven hoof.  Most cloven-hoofed animals also have two smaller hoofs called dew-claws a little further up the leg  these are not normally used for walking, but in some species with larger dew-claws (such as deer and pigs) they may touch the ground when running or jumping, or if the ground is soft.  Other cloven-hoofed animals (such as giraffes and pronghorns) have no dew claws.  In some so-called "cloven-hoofed" animals such as camels, there are no hooves proper  the toe is softer, and the hoof itself is reduced to little more than a nail.
Some odd-toed ungulates (equids) have one hoof on each foot; others (including rhinoceroses, tapirs and many extinct species) have (or had) three hoofed or heavily nailed toes, or one hoof and two dew-claws.  The tapir is a special case, with three toes on each hind foot and four toes on each front foot.
The number of toes is considered in determining the kosher status of the animal's flesh.
Stye
Synonyms and keywords: Hordeolum

# Overview
A stye (also known as a hordeolum) is a painful infection of the sebaceous glands at the base of the eyelashes on, inside, or under the eyelid.. The infection may be internal or external. In many cases, a hordeolum may resolve without treatment; however, the inflammation may spread to other ocular glands or recur. 

# Causes
A stye is usually caused by Staphylococcus aureus. They can be triggered by stress, poor nutrition or lack of sleep. A stye may be secondary to blepharitis.

# Differential Diagnosis
A stye must be differentiated from:
- Xanthelasma
- Papilloma
- Cyst
- Pyogenic Granuloma
- Amyloid Deposition

# Risk Factors
Common risk factors in the development of hordeola are:
- Dry eyes
- Chronic blepharitis

# Epidemiology & Demographics
Styes are particularly common in infants, though they may occur at any age.

# Diagnosis

## History and Symptoms
The first signs are tenderness and redness in the affected area. Symptoms of a stye include:
- Swelling
- Watering of the eye
- Sensitivity to light
- Discomfort during blinking

## Physical examination

### Eyes
- A localized and tender area with a pointing eruption may be seen in the affected area.
- A yellowish bump may be noted.

### Lymph Nodes
- Adjacent lymph nodes may be palpable.

### Gallery
- Hordeolum. With permission from Dermatology Atlas.
- Hordeolum. With permission from Dermatology Atlas.

# Treatment

## Medical Therapy
Most cases of hordeolum resolve without treatment. Supportive therapy for hordeolum consists of warm compresses.  Antimicrobial ophthalmic ointments may be administered.
- Hordeolum
- 1. External hordeolum, for a  single lesion
- Preferred regimen: Supportive therapy is sufficient. Application of warm compresses 4-6 times/day.
- Note: Antibiotic therapy is questionable value for a single lesion and often not indicated.
- 2. External hordeolum, for multiple/recurrent lesions
- Preferred regimen (1): Bacitracin ophthalmic q8-24h
- Preferred regimen (2): Erythromycin topical q4-6h
- 3. Internal hordeolum
- Preferred regimen: Warm compresses 4-6 times/day in conjugation with systemic antistaphylococcal antibiotics
- Note: If the lesion do not respond to this regimen, incision and drainage are indicated.
IGL@
Immunoglobulin lambda locus, also known as IGL@, is a region on human chromosome 22 that contains genes for the lambda light chains of antibodies (or immunoglobulins).

# Function
Immunoglobulins recognize foreign antigens and initiate immune responses such as phagocytosis and the complement system. Each immunoglobulin molecule consists of two identical heavy chains and two identical light chains. There are two classes of light chains, kappa and lambda. This region represents the germline organization of the lambda light chain locus. The locus includes V (variable), J (joining), and C (constant) segments. During B cell development, a recombination event at the DNA level joins a single V segment with a J segment; the C segment is later joined by splicing at the RNA level. Recombination of many different V segments with several J segments provides a wide range of antigen recognition. Additional diversity is attained by junctional diversity, resulting from the random additional of nucleotides by terminal deoxynucleotidyltransferase, and by somatic hypermutation, which occurs during B cell maturation in the spleen and lymph nodes. Several V segments and three C segments are known to be incapable of encoding a protein and are considered pseudogenes. The locus also includes several non-immunoglobulin genes, many of which are pseudogenes or are predicted by automated computational analysis or homology to other species.

# Genes
The immunoglobulin lambda locus contains the following genes:
- IGLC@  constant group
IGLC1  immunoglobulin lambda constant 1 (Mcg marker)
IGLC2  immunoglobulin lambda constant 2 (Kern-Oz- marker)
IGLC3  immunoglobulin lambda constant 3 (Kern-Oz+ marker)
IGLC7  immunoglobulin lambda constant 7
- IGLC1  immunoglobulin lambda constant 1 (Mcg marker)
- IGLC2  immunoglobulin lambda constant 2 (Kern-Oz- marker)
- IGLC3  immunoglobulin lambda constant 3 (Kern-Oz+ marker)
- IGLC7  immunoglobulin lambda constant 7
- IGLJ@  joining group
IGLJn  immunoglobulin lambda joining n
IGLJ1, IGLJ2, IGLJ3, IGLJ6, IGLJ7
- IGLJn  immunoglobulin lambda joining n
- IGLJ1, IGLJ2, IGLJ3, IGLJ6, IGLJ7
- IGLV@  variable group
IGLVm-n  immunoglobulin lambda variable n-m
IGLV1-36, IGLV1-40, IGLV1-44, IGLV1-47, IGLV1-51, IGLV1-62
IGLV2-5, IGLV2-8, IGLV2-11, IGLV2-14, IGLV2-18, IGLV2-23
IGLV3-1, IGLV3-10, IGLV3-12, IGLV3-16, IGLV3-19, IGLV3-21, IGLV3-25, IGLV3-27
IGLV4-3, IGLV4-60, IGLV4-69
IGLV5-37, IGLV5-39, IGLV5-45, IGLV5-52
IGLV6-57
IGLV7-43
IGLV9-49
IGLV10-54
- IGLVm-n  immunoglobulin lambda variable n-m
- IGLV1-36, IGLV1-40, IGLV1-44, IGLV1-47, IGLV1-51, IGLV1-62
- IGLV2-5, IGLV2-8, IGLV2-11, IGLV2-14, IGLV2-18, IGLV2-23
- IGLV3-1, IGLV3-10, IGLV3-12, IGLV3-16, IGLV3-19, IGLV3-21, IGLV3-25, IGLV3-27
- IGLV4-3, IGLV4-60, IGLV4-69
- IGLV5-37, IGLV5-39, IGLV5-45, IGLV5-52
- IGLV6-57
- IGLV7-43
- IGLV9-49
- IGLV10-54
Ig lambda chain C regions is a protein that in humans is encoded by the IGLC2 gene.
IKK2
IKK- also known as  inhibitor of nuclear factor kappa-B kinase subunit beta is a protein that in humans is encoded by the IKBKB (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase beta) gene.

# Function
IKK- is an enzyme that serves as a protein subunit of IB kinase,  which is a component of the cytokine-activated intracellular signaling pathway involved in triggering immune responses. IKK's activity causes activation of a transcription factor known as Nuclear Transcription factor kappa-B or NF-B.  Activated IKK- phosphorylates a protein called the inhibitor of NF-B, IB (IB), which binds NF-B to inhibit its function. Phosphorylated IB is degraded via the ubiquitination pathway, freeing NF-B, and allowing its entry into the nucleus of the cell where it activates various genes involved in inflammation and other immune responses.

# Clinical significance
IKK- plays a significant role in brain cells following a stroke.  If NF-B activation by IKK- is blocked, damaged cells within the brain stay alive, and according to a study performed by the University of Heidelberg and the University of Ulm, the cells even appear to make some recovery.
Inhibition of IKK and IKK-related kinases has been investigated as a therapeutic option for the treatment of inflammatory diseases and cancer. The small-molecule inhibitor of IKK2 SAR113945, developed by Sanofi-Aventis, was evaluated in patients with knee osteoarthritis.

# Model organisms
Model organisms have been used in the study of IKK- function. The size of an infarct, or tissue killed or damaged by ischemia, is reduced in mice in which IKK- has been blocked. Additionally, experimental mice with an overactive form of IKK- experience loss of many more neurons than normal mice after a stroke-simulating event.  Researchers found a molecule that could block the signaling of IKK- for up to four and a half hours. In another study, researchers found that inhibiting IKK- prevented kidney and wasting diseases in an animal model used to study wasting diseases of human AIDS sufferers.
A conditional knockout mouse line, called Ikbkbtm1a(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  at the Wellcome Trust Sanger Institute.
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty six tests were carried out and two phenotypes were reported. A reduced number of homozygous mutant embryos were identified during gestation, and none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice, and no significant abnormalities were observed in these animals.

# Interactions
IKK- (IKBKB) has been shown to interact with
- CDC37,
- CHUK
- CTNNB1,
- FANCA,
- IKBKG
- IRAK1,
- NFKBIA,
- MAP3K14,
- NFKB1,
- NFKBIB,
- NCOA3,
- PPM1B,
- TNFRSF1A, and
- TRAF2.
ILF2
Interleukin enhancer-binding factor 2 is a protein that in humans is encoded by the ILF2 gene.

# Function
Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of the interleukin 2 gene. NFAT binds to a sequence in the interleukin 2 gene enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the smaller of which is the product of this gene. The encoded protein binds strongly to the 90 kDa protein and stimulates its ability to enhance gene expression.

# Interactions
ILF2 has been shown to interact with CDC5L and DNA-PKcs.
ILF2 and ILF3 have been identified as autoantigens in mice with induced lupus, in canine systemic rheumatic  autoimmune disease, and as a rare finding in humans with autoimmune disease.
ILF3
Interleukin enhancer-binding factor 3 is a protein that in humans is encoded by the ILF3 gene.

# Function
Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of this gene. The encoded protein, which is primarily localized to ribosomes, probably regulates transcription at the level of mRNA elongation. At least three transcript variants encoding three different isoforms have been found for this gene.

# Interactions
ILF3 has been shown to interact with:
- DNA-PKcs,
- FUS,
- PRMT1
- Protein kinase R,  and
- XPO5.
- C5orf36
Small NF90/ILF3-associated RNAs (snaR) (~120 nucleotides long) and are known to interact with ILF3 double-stranded RNA-binding motifs. snaR-A is abundant in human testis and has been shown to associate with ribosomes in HeLa cells. snaR-A is present in human and gorilla but not in chimpanzee. Other snaR RNAs are found in African Great Apes (including chimpanzee and bonobo).
ILF2 and ILF3 have been identified as autoantigens in mice with induced lupus, in canine systemic rheumatic  autoimmune disease, and as a rare finding in humans with autoimmune disease.
ING4
Inhibitor of growth protein 4 is a protein that in humans is encoded by the ING4 gene.

# Function
The protein encoded by this gene is similar to ING1, a tumor suppressor protein that can interact with TP53, inhibit cell growth, and induce apoptosis. This protein contains a PHD-finger, which is a common motif in proteins involved in chromatin remodeling. This protein can bind TP53 and EP300/p300, a component of the histone acetyl transferase complex, suggesting its involvement in the TP53-dependent regulatory pathway. Alternatively spliced transcript variants have been observed, but the biological validity of them has not been determined.

# Interactions
ING4 has been shown to interact with EP300, RELA and P53.
IPO5
Importin-5 is a protein that in humans is encoded by the IPO5 gene. The protein encoded by this gene is a member of the importin beta family.

# Function
Nuclear transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex.
IPO5 facilitates cytoplasmic polyadenylation element-binding protein (CPEB)3 translocation by binding to RRM1 motif of CPEB3 in neurons. NMDAR signaling increases RanBP1 expression and reduces the level of cytoplasmic GTP-bound Ran. These changes enhance CPEB3IPO5 interaction, which consequently accelerates the nuclear import of CPEB3 and promotes its nuclear function.
IRF3
Interferon regulatory factor 3, also known as IRF3, is an interferon regulatory factor.

# Function
IRF3 is a member of the interferon regulatory transcription factor (IRF) family. IRF3 was originally discovered as a homolog of IRF1 and IRF2. IRF3 has been further characterized and shown to contain several functional domains including a nuclear export signal, a DNA-binding domain, a C-terminal IRF association domain and several regulatory phosphorylation sites. IRF3 is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes.
IRF3 plays an important role in the innate immune system's response to viral infection. Aggregated MAVS have been found to activate IRF3 dimerization. A recent study shows phosphorylation of innate immune adaptor proteins MAVS, STING and TRIF at a conserved pLxIS motif recruits and specifies IRF3 phosphorylation and activation by the Serine/threonine-protein kinase TBK1, thereby restricts the production of type-I interferons. Another study has shown that IRF3-/- knockouts protect from myocardial infarction. The same study identified IRF3 and the type I IFN response as a potential therapeutic target for post-myocardial infarction cardioprotection.

# Interactions
IRF3 has been shown to interact with IRF7.
IRF4
Interferon regulatory factor 4 also known as MUM1 is a protein that in humans is encoded by the IRF4 gene, located at 6p25-p23.
The MUM1 symbol is polysemous; although it is an older synonym for IRF4 (HGNC:6119), it is also the current HGNC official symbol for melanoma associated antigen (mutated) 1 (HGNC:29641; located at 19p13.3).

# Clinical significance
In melanocytic cells the IRF4 gene may be regulated by MITF. IRF4 is a transcription factor that has been implicated in acute leukemia. This gene is strongly associated with pigmentation: sensitivity of skin to sun exposure, freckles, blue eyes, and brown hair color. A variant has been implicated in greying of hair.

# Interactions
IRF4 has been shown to interact with:
- BCL6,
- NFATC2,
- SPI1, and
- STAT6.
IRF5
Interferon regulatory factor 5 is a protein that in humans is encoded by the IRF5 gene.

# Function
IRF5 is a member of the interferon regulatory factor (IRF) family, a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Alternative splice variants encoding different isoforms exist.

# Clinical significance
IRF5 acts as a molecular switch that controls whether macrophages will promote or inhibit inflammation. Blocking the production of IRF5 in macrophages may help treat a wide range of autoimmune diseases, and that boosting IRF5 levels might help treat people whose immune systems are weak, compromised, or damaged. IRF5 seems to work "either by interacting with DNA directly, or by interacting with other proteins that themselves control which genes are switched on."
IRF6
Interferon regulatory factor 6 also known as IRF6 is a protein that in humans is encoded by the IRF6 gene.

# Function
This gene encodes a member of the interferon regulatory transcription factor (IRF) family. Family members share a highly conserved N-terminal helix-turn-helix DNA-binding domain and a less conserved C-terminal protein-binding domain.
The function of IRF6 is related to the formation of connective tissue, for example that of the palate.  This gene encodes a member of the interferon regulatory transcription factor (IRF) family.

# Pathology
A mutation of the IRF6 gene can lead to the autosomal dominant van der Woude syndrome (VWS)  or the related popliteal pterygium syndrome (PPS).  Van der Woude syndrome can include cleft lip and palate features along with dental anomalies and lip fistulas. In addition, common alleles in IRF6 have also been associated with non-syndromic cases of cleft lip and/or palate through genome-wide association studies and in many candidate gene studies. These disorders are caused by mutations in the IRF6 gene and some of the phenotypic heterogeneity is due to different types of IRF6 mutations.
One explanation  for this phenotypic variation between syndromes is based on a differential impact on the structure of the dimerized mutant proteins. VWS mutations appear to result in haploinsufficiency while PPS mutations may be dominant negative in nature. The spectrum of mutations in VWS and PPS has been recently summarized. IRF6 has been shown to play a critical role in keratinocyte development. A role for IRF6 in the common forms of cleft lip and palate has also been demonstrated and may explain ~20% of cases of cleft lip only. Variants in IRF6 have yielded consistent evidence of association with syndromic cleft and/or palate across multiple studies. A study by Birnbaum and colleagues in 2009 confirmed the impact of this gene on the etiology of cleft lip and/or palate, and the GENEVA Cleft Consortium study, which studied families from multiple populations, reconfirmed the findings that IRF6 mutations are strongly associated with cleft and/or palate.  A role of IRF6 in causing cleft lip and/or palate is further supported by analysis of IRF6 mutant mice which exhibit a hyper-proliferative epidermis that fails to undergo terminal differentiation, leading to multiple epithelial adhesions that can occlude the oral cavity and result in cleft palate. Research on animal models indicate IRF6 determines keratinocyte proliferation and also has a key role in the formation of oral periderm. Recently, through utilization of mouse genetics, gene expression analyses, chromatin immunoprecipitation studies and luciferase reporter assays, it has been shown that IRF6 is a direct target of p63, which underlies several malformation syndromes that include cleft features, and p63 activates IRF6 transcription through the IRF6 enhancer element.  Variation in the enhancer element increases susceptibility to cleft lip only. Both cleft lip with or without a cleft palate and cleft palate only features have been seen in families with an IRF6 mutation. In addition, different types of clefts can segregate within the same family.
IRF7
Interferon regulatory factor 7, also known as IRF7, is a member of the interferon regulatory factor family of transcription factors.

# Function
IRF7 encodes interferon regulatory factor 7, a member of the interferon regulatory transcription factor (IRF) family. IRF7 has been shown to play a role in the transcriptional activation of virus-inducible cellular genes, including the type I interferon genes. In particular, IRF7 regulates many interferon-alpha genes. Constitutive expression of IRF7 is largely restricted to lymphoid tissue, largely plasmacytoid dendritic cells, whereas IRF7 is inducible in many tissues. Multiple IRF7 transcript variants have been identified, although the functional consequences of these have not yet been established.
The IRF7 pathway was shown to be silenced in some metastatic breast cancer cell lines, which may help the cells avoid the host immune response. Restoring IRF7 to these cell lines reduced metastases and increased host survival time in animal models.
The IRF7 gene and product were shown to be defective in a patient with severe susceptibility to H1N1 influenza, while susceptibility to other viral diseases such as CMV, RSV, and parainfluenza was unaffected.

# Interactions
IRF7 has been shown to interact with IRF3. Also, IRF7 has been shown to interact with Aryl Hydrocarbon Receptor Interacting Protein (AIP), which is a negative regulator for the antiviral pathway.