Persius/hicric huggingface dataset:
Butterbur
The plants commonly referred to as Butterbur are found in the daisy family Asteraceae in the genus Petasites. They are mostly quite robust plants with thick, creeping underground rhizomes and large Rhubarb-like leaves during the growing season. Another common name for many species of this genus is Sweet Coltsfoot.
The short spikes of flowers are produced just before these leaves in Spring, emerging with only a few elongated basal bracts and are usually green, flesh coloured or dull white depending on species.
Butterburs are found in the temperate zone of the Northern Hemisphere.  They prefer moist environments such as riverbanks, marshes and ditches.
Petasites is very closely related to the genus Tussilago (Coltsfoot), and also related to the huge genus Senecio.

# Medicinal uses
Butterbur was used by native Americans as a remedy for headache and inflammation.  Some Butterbur contains petasin and isopetasin, with the highest concentrations occurring in the root. The best-documented beneficial effect of Butterbur extracts are as a treatment of migraine headaches.  Several mainstream double-blind studies have shown that extracts of Butterbur petasin and/or isopetasin are effective both in preventing and in relieving migraine, with the best results coming in more severe cases . Additionally, a peer-reviewed journal published a Swiss study showing Butterbur extract to be an effective treament for hay fever without the sedative effect of the antihistamine cetirizine .
Butterbur naturally contains components called pyrrolizidine alkaloids. They are toxic to the liver and may cause cancers. The concentrations are often highest in the rhizomes and stalks and lowest in the leaves and may vary depending on where the plants are grown.  Butterbur extract should be taken only when prepared by a reputable laboratory.  Long-term health effects and interaction with other drugs have not been studied.

# Selected species
- Petasites albus White Butterbur
- Petasites amplus
- Petasites doerfleri
- Petasites formosanus
- Petasites fragrans Winter Heliotrope
- Petasites frigidus (syn. P. speciosa) Arctic Butterbur or Arctic Sweet Coltsfoot
- Petasites hybridus Common Butterbur
- Petasites japonicus Giant Butterbur, or Fuki
- Petasites kablikianus
- Petasites paradoxus
- Petasites radiatus
- Petasites sagittatus
- Petasites sibiricus
- Petasites spurius
- Petasites tatewakianus
- Petasites tricholobus

# Hybrids
- Petasites x vitifolius

# In popular culture
In the manga Shaman King, the young Ainu shaman Horohoro dreams of planting a vast field of Butterbur from the east to the west coast of Hokkaido.
C-peptide

# Overview
C-peptide is a peptide which is made when proinsulin is split into insulin and C-peptide. They split when proinsulin is released from the pancreas into the blood in response to a rise in serum glucose - one C-peptide for each insulin molecule.
- In proinsulin, C-peptide is an amino-acid chain connecting A and B chains of insulin
- The level of C-peptide in the body is indicative of how much insulin is being produced in the body 
- Reference range: 0.33-1.20 nmol/l

# Etymology and History
C-peptide is the abbreviation for "connecting peptide", although its name was probably also inspired by the fact that insulin is also composed of an "A" chain and a "B" chain.
C-peptide was discovered in 1967. The first documented use of the C-peptide test was in 1972.
It should not to be confused with c-reactive protein or Protein C.

# Function
C-peptide functions in repair of the muscular layer of the arteries.
C-peptide also exerts beneficial therapeutic effects on many complications associated with diabetes mellitus  , , such as for instance diabetic neuropathy and other diabetes-induced ailments. In the kidneys, C-peptide prevents diabetic nephropathy , , and in the heart  blood flow is improved in diabetic patients.
In spite of these physiological functions, C-peptide is actually removed from pharmaceutical preparations of insulin sold by drug companies when they manufacture the synthetic human insulin that is in widescale clinical usage today.

# Uses
- Newly diagnosed diabetes patients often get their C-peptide levels measured, to find if they are type 1 diabetes or type 2 diabetes.  The reason that the C-peptide levels are measured instead of the insulin levels themselves is because insulin concentration in the portal vein ranges from two to ten times higher than in the peripheral circulation.  The liver extracts about half the insulin reaching it (the plasma), but this varies with the nutritional state.  The pancreas of patients with type 1 diabetes is unable to produce insulin and they will therefore usually have a decreased level of C-peptide, while C-peptide levels in type 2 patients is normal or higher than normal. Measuring C-peptide in patients injecting insulin can help to determine how much of their own natural insulin these patients are still producing.
- C peptide is also used for determining the possibility of gastrinomas associated with Multiple endocrine neoplasia (MEN).  Since a significant amount of gastrinomas also include MEN which include pancreatic, parathyroid, and pituitary adenomas, higher levels of c-protein in addition to a gastrinoma may suggest other organs than just the stomach may include neoplasms.
- Can be used for identifying malingering: hypoglycemia with low C-peptide level may indicate abuse of insulin.
C-peptide levels are also checked to determine how insulin resistant women with Polycystic Ovarian Syndrome may be.

# Differential Diagnosis

## Decreased
- Low insulin production
- With elevated serum insulin: drug-induced hypoglycemia

## Increased
- Insulinoma

### Normal Values in Patients with Injections of Insulin
- Patient is still producing insulin
C10orf118
C10orf118 is a protein that in humans is encoded by the C10orf118 gene  The C10orf118 (CCDC186) gene is also known as the CTCL-tumor associated antigen with accession number NM_018017.

# Gene

## Location
C10orf118 has the chromosome location of 10q25.3 and is 53,750 bases in size oriented on the minus strand. PSORTII Protein k-NN Prediction indicated that C10orf118 is 65.2% of the time nuclear, 17.4% cytosolic, 8.7% mitochondrial, 4.3% vesicles of secretory system, and 4.3% endoplasmic reticulum.

## Expression
Analysis of gene expression in humans and other species indicates C10orf118 is ubiquitously expressed in all tissue types at varying developmental stages. An EST profile from NCBI displayed the greatest expression in bone marrow, kidneys, and the prostate cell lines. Breakdown by health state indicates high expression of C10orf118 in bladder carcinoma and prostate cancer.

# Protein

## General Properties
The protein of CCDC186 (NP_060487) is 898 amino acids in length. The predicted molecular weight is 103.7kdal and the isoelectric point is predicted to be 5.92.

## Composition
A serine rich region is observed in amino acids 710-747. A compositional analysis revealed that C10orf118 is Proline (1.1%) poor and Glutamic acid (14.1%) and Lysine (12.0%) rich.

## Interactions
C10orf118 protein was found to interact with proteins PLEKAH5, Ezra, GAMMAHV.ORF23, and SMAD3.

## Homology
Orthologous sequences of C10orf118 were not found to be in bacteria, archea, protist, or plants. C10orf118 has no human paralogs. The date of divergence for the orthologous sequences highly correlates with the sequences similarity in that the percent identity decreases as you go back in time. Closely related orthologs include mammals and birds and moderately related orthologs include other vertebrates such as fish, reptiles, and amphibians. Distantly related orthologous sequences are primarily observed in invertebrates.

## Motifs

## Post Translational Modification
C10orf118 is predicted to undergo multiple posttranslational modifications including predicted O-beta-GlcNAc attachment, phosphorylation, a nuclear export signal, glycation of lysines, GlcNAc O-glycosylation, N-glycosylation, and NetCorona sites.

## Clinical significance
Prior research indicates that the open reading frame of C10orf118 is linked to cutaneous T-cell lymphoma by a tumor antigen L14-2. The protein C10orf118 is also found at higher than normal levels in the breast cancer cell line BC 8701.
C14orf159
UPF0317 protein C14orf159, mitochondrial is a protein that in humans is encoded by the C14orf159 gene (chromosome 14 open reading frame 159).

# Orthologs
The human gene, c14orf159 mRNA, is highly conserved in mammals and birds. Orthologs gathered from BLAST and BLAT searches reveal that the human c14orf159 mRNA sequence is conserved with a sequence identity of 98% in chimpanzees, 88% in mice, and 81% in platypus and chicken. The following table contains a list orthologs that were gathered from BLAST searches.  Sequence alignments were performed using blastn to derive sequence identity, score, and E-values between the human c14orf159 variant 1 mRNA and its orthologs.
The protein that the human gene c14orf159 encodes has been found to be highly conserved among mammals, birds, amphibians, fish, tunicates, cnidarians, and echinoderms.  However, no protein orthologs have been found in nematodes, arthropods, fungi, protists, plants, bacteria, or archea.  Fungi and bacteria contain the DUF1445 conserved domain which is found in human c14orf159 and its orthologs.  BLAST and BLAT searches have been utilized to find orthologs to the c14orf159 protein.  The following table lists protein orthologs for the human protein with sequence identity, sequence similarity, scores, and E-values derived from blastp sequence comparisons.

# Post-translational modification
The protein product of the C14orf159 gene is predicted and was found to be translocated to mitochondrion.
Post-translational modifications are predicted for the protein c14orf159.  All predicted sites in human c14orf159 were compared to orthologs using multiple sequence alignments to determine likelihood of modification.

# Regulation
Estrogen receptor alpha, in the presence of estradiol, binds to the C14orf159 gene and likely regulates its expression.
CAMP test
Synonyms and keywords: CAMP reaction; Christie Atkins MunchPetersen reaction; Christie-Atkins-MunchPetersen reaction

# Overview
The CAMP test is a test to identify Group B -streptococci based on their formation of a substance (CAMP factor) that enlarges the area of hemolysis formed by -hemolysin from Staphylococcus aureus. It is frequently used to identify Listeria species. The name has no relationship to cyclic adenosine monophosphate (cAMP).

# Historical Perspective
It is an acronym for R. Christie, N. E. Atkins, and E. Munch-Peterson, for the three researchers who discovered the phenomenon.
It is often incorrectly reported as the product of four people (counting Munch-Petersen as two people).

# CAMP factor
Although usually used to identify group "B", there is some evidence that the CAMP factor gene is present in several groups of streptococci, including group "A".
A similar factor has been identified in Bartonella henselae.

# Uses
It can be used to identify Streptococcus agalactiae. Though not strongly beta-hemolytic on its own, it presents with a wedge-shape in the presence of Staphylococcus aureus.
Caspase 2
Caspase 2  also known as CASP2 is an enzyme that, in humans, is encoded by the CASP2 gene. CASP2 orthologs  have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

# Function
Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The proteolytic cleavage of this protein is induced by a variety of apoptotic stimuli.
Caspase 2 proteolytically cleaves other proteins. It belongs to a family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase 2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase 2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase 4, caspase 5, and caspase 9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase 9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12.
It has been shown to associate with several proteins involved in apoptosis using its CARD domain, including RIP-associated Ich-1/Ced-3-homologue protein with a death domain (RAIDD), apoptosis repressor with caspase recruitment domain (ARC), and death effector filament-forming Ced-4-like apoptosis protein (DEFCAP). Together with RAIDD and p53-induced protein with a death domain ()(LRDD), caspase 2 has been shown to form the so-called PIDDosome, which may serve as an activation platform for the protease, although it may also be activated in the absence of PIDD. Overall, caspase 2 appears to be a very versatile caspase with multiple functions beyond cell death induction.

# Interactions
Caspase 2 has been shown to interact with:
- BH3 interacting domain death agonist,
- CRADD,  and
- Caspase 8.
Caspase 6
Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene.
CASP6 orthologs  have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Caspase-6 has known functions in apoptosis, early immune response and neurodegeneration in Huntington's and Alzheimer's disease.

# Function
This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms.
Caspase-6 plays a role in the early immune response via de-repression. It reduces the expression of the immunosuppressant cytokine interleukin-10 and cleaves the macrophage suppressing IRAK-M.
With respect to neurodegeneration, caspase-6 cleaves HTT in Huntington's and APP in Alzheimer's disease. Resulting in both cases in protein aggregation of the fragments.

# Interactions
Caspase 6 has been shown to interact with Caspase 8.
Caspase 7
Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7 gene.
CASP7 orthologs  have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

# Function
Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis.  Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms.

# Interactions
Caspase 7 has been shown to interact with:
- Caspase 8,
- Survivin  and
- XIAP.
Cyclin B2
G2/mitotic-specific cyclin-B2 is a protein that in humans is encoded by the CCNB2 gene.

# Function
Cyclin B2 is a member of the cyclin family, specifically the B-type cyclins. The B-type cyclins, B1 and B2, associate with p34cdc2 and are essential components of the cell cycle regulatory machinery. B1 and B2 differ in their subcellular localization. Cyclin B1 co-localizes with microtubules, whereas cyclin B2 is primarily associated with the Golgi region. Cyclin B2 also binds to transforming growth factor beta RII and thus cyclin B2/cdc2 may play a key role in transforming growth factor beta-mediated cell cycle control.

# Interactions
Cyclin B2 has been shown to interact with TGF beta receptor 2.
Cyclin D2
G1/S-specific cyclin-D2 is a protein that in humans is encoded by the CCND2 gene.

# Function
The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of cyclin-dependent kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activity is required for cell cycle G1/S transition. This protein has been shown to interact with and be involved in the phosphorylation of tumor suppressor protein Rb. Knockout studies of the homologous gene in mouse suggest the essential roles of this gene in ovarian granulosa and germ cell proliferation. High level expression of this gene was observed in ovarian and testicular tumors.

# Clinical significance
Mutations in  CCND2 are associated to                 megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome            .
CNTO 1275
CNTO 1275 is the experimental name for a human immunosuppressive drug developed by the biotechnology company Centocor.  It is a laboratory-manufactured, monoclonal antibody directed against interleukins IL-12 and IL-23 and presently undergoing clinical trials to determine its safety and effectiveness against the diseases Multiple Sclerosis, Psoriasis, and Psoriatic Arthritis.
Once released for public use, administration and dosage of the drug will most likely by doctor's prescription and direction only.

# Development
As of January 2007, there were 5 NIH-listed research studies involving CNTO 1275 on a multinational basis, including 3 Phase II and 2 Phase III trials.  Three studies are focused on patients with psoriasis, one on psoriatic arthritis, and one on Multiple Sclerosis.
CNTO 1275 is not yet approved by the U.S. Food and Drug Administration.

# Delivery
Note: Because the drug is not yet released for public use, the official drug's prescribing information and disclosure (required by federal law) is not available.
Patients enrolled in clinical trials of CNTO 1275 are scheduled to receive the drug by subcutaneous injections at doses of either 45 or 90 mg.  The dosage and frequency varies by study and application (type of disease targeted).  Generally the initial dosing interval is once per week followed by a step-down to once per month or even once every three months.

# Mode of action
Similar to the immunosuppressive function of Etanercept(Enbrel), CNTO 1275 is designed to interfere with the triggering of the body's inflamatory response through the suppression of certain cytokines.  Specifically, CNTO 1275 blocks interleukin IL-12 and IL-23 which help activiate certain T-cells.
COUP-TFII
COUP-TFII (COUP transcription factor 2), also known as NR2F2 (nuclear receptor subfamily 2, group F, member 2) is a protein that in humans is encoded by the NR2F2 gene. The COUP acronym stands for chicken ovalbumin upstream promoter.

# Function
COUP-TFII plays a critical role in controlling the development of a number of tissues and organs including heart, blood vessels, muscles and limbs.
The glucocorticoid receptor (GR) stimulates COUP-TFII-induced transactivation while COUP-TFII represses the GR transcriptional activity. COUP-TFII interacts with GATA2 to inhibit adipocyte differentiation.

# Interactions
COUP-TFII has been shown to interact with:
- HDAC1
- Lck
- V-erbA-related gene.
- Nucleolin
CYP2C9*13
Cytochrome P450 2C9 (CYP2C9), a member of the
CYP2C enzyme subfamily, ranks amongst the most
important drug metabolizing enzymes in humans.
Human CYP2C9 has been shown to exhibit genetic polymorphism. In addition to the wild-type protein CYP2C9*1, at least 30 single nucleotide polymorphisms (SNPs) have been reported within the coding region of the CYP2C9 gene producing the variant allozymes. CYP2C9*13 is one of them. It involves a T-to-C transversion at nucleotide position 269 causing a mutation at codon 90, which results in a Leu->Pro substitution. Frequency analysis in 147 unrelated Chinese males indicated approximately 2% of the Chinese population carry the allele. CYP2C9*13 was found in Japanese and Korean, too.
CYP2C9*13 allele was correlated with reduced plasma clearance of drugs that are substrates for CYP2C9.
CYP2C9*13 was found by Si Dayong, Zhou Hui*, Zhang Yifan and Zhong Dafang- in 2004.
Calcaneus

# Overview
The calcaneus is the largest bone of the human foot. The skeleton of the human foot is made up of three groups of bones: the tarsus, the metatarsus and the phalanges. The tarsal bones consist of the calcaneus, talus, cuboid, navicular, and the first, second, and third cuneiforms. The calcaneus forms part of the tarsi and constitutes the heel of the human foot or the point of an animal's hock . It is also known as the heel bone.

# Human
It articulates with two other tarsal bones, the talus above and the cuboid toward the midfoot.  In addition to receiving the weight of the body with each step, the calcaneus is the anchor for the plantar fascia, which supports the arch of the foot.

## Calcaneal tuberosity
The posterior-most portion of the calcaneus is the calcaneal tuberosity, a large, non-articulating process that is the insertion point for the calcaneal tendon (or Achilles tendon).  In addition, this process is the origin for some of the muscles and tendons of the foot.

# Horse
The calcaneus has two articulations, being part of the Proximal intertarsal joint and the Talocalcaneal joint. As in humans it is the insertion of the gastrocnemius and superficial digital flexor tendons. The point of the calcaneus is covered by the calcanean bursa.
Caldesmon
Caldesmon is a protein that in humans is encoded by the CALD1 gene.
Caldesmon is a calmodulin binding protein. Like calponin, caldesmon  tonically inhibits the ATPase activity of myosin in smooth muscle.
This gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca++-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca++-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.

# Immunochemistry
In diagnostic immunochemistry, caldesmon is a marker for smooth muscle differentiation.