Persius/hicric huggingface dataset:
CCDC144A
Coiled-coil domain-containing protein 144A is a protein that in humans is encoded by the CCDC144A gene. An alias of this gene is called KIAA0565. There are four members of the CCDC family: CCDC 144A, 144B, 144C and putative CCDC 144 N-terminal like proteins.

# Gene
This gene has a nucleotide sequence that is 5140 bp long, and it encodes 641 amino acids.  It is found on the short arm, plus (forward) strand of chromosome 17 at p11.2.  The mRNA for the CCDC144A gene has 3 alternative splicing isoforms named A2RUR9-1, A2RUR9-2, AND A2RUR9-3, but there is no experimental confirmation available yet.

# Protein
This protein for this gene is also known as coiled coil domain containing 144A (CCDC144A) protein. It consists of 641 amino acids.   This protein weighs 75.8 kDa and has an isoelecric point of 6.357. This protein localizes near the nucleus, and is a soluble protein with a hydrophobicity of -1.021842. This protein is also non-secretory and has 10 potential serine and 3 potential threonine phosphorylation sites. There are no tyrosine sulfation sites, but there are a few potential sumoylation sites on this protein. Also, this protein is predicted to be non-myristoylated and does not contain a signal peptide.

## Structure
This protein has a domain of unknown function (DUF) 3496, which has been conserved in eukaryotes.  The DUF3496 domain is found from amino acids 547-622.
CCDC144A, an alias of this gene, indicates that there should be a coiled coil domain within the protein. Coiled coils are structural motifs in proteins in which 2 more alpha helices are coiled together, and they usually contain a heptad repeat, hxxhcxc, or hydrophobic (h) and charge (c) amino acid residues. The 5' and 3' untranslated regions of the nucleotide sequence of this gene are rich in stem-loop structures. In place of a coiled coil, a leucine zipper was found. Residues from 478-499, "LHNTRDALGRESLILERVQRDL", are the residues that form the leucine zipper pattern. The structure of this protein consists of mostly alpha helices, with some random coils.

# Evolution
Orthologs of KIAA0565 protein have been identified mostly in mammals, but some birds, reptiles, amphibians, and fish as well.

## Potential Orthologs

# Clinical significance
This gene has been linked to Smith-Magenis Syndrome (SMS), which is also known as chromosome 17p11.2 deletion syndrome, chromosome 17p deletion syndrome, deletion 17p syndrome, partial monosomy 17p, and deletion abnormality.

## Interacting proteins
There may potentially be two proteins that interact with KIAA0565, and they are ubiquitin specific peptidase 32 (USP32) and ubiquitin specific peptidase 25 (USP25).

## Expression
This protein has been shown to have relatively low expression in all tissues.
Cyclin H
Cyclin-H is a protein that in humans is encoded by the CCNH 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 CDK 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 CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, thus functions as a CDK-activating kinase (CAK). This cyclin and its kinase partner are components of TFIIH, as well as RNA polymerase II protein complexes. They participate in two different transcriptional regulation processes, suggesting an important link between basal transcription control and the cell cycle machinery.

# Interactions
Cyclin H has been shown to interact with P53, Cyclin-dependent kinase 7 and MNAT1.
Cyclin K
Cyclin-K is a protein that in humans is encoded by the CCNK gene.

# Function
The protein encoded by this gene is a member of the transcription cyclin family. These cyclins may regulate transcription through their association with and activation of cyclin-dependent kinases (CDKs) through conformational changes. Activation of CDKs through their cyclin partner, creates kinase complexes that will activate target proteins through phosphorylation. Targeted proteins can then ultimately regulate decisions of a cells progression within the cell cycle to occur. This gene product may be seen to play a dual role in both regulating CDK and RNA polymerase II (RNAP2) activities. Cyclin K only uses RNA recruitment to activate transcription.

# Interactions
Cyclin K has been shown to interact with multiple CDKs including CDK9 and latest CDK12 and CDK13. Roles include helping to phosphorylate C-terminal domains of subunits of RNAP2. Cyclin K is most noted for its associated induction of processive elongation. Also, identified with G1 and S phase cyclin activity, however functions are not deeply understood.
Cyclin K also interacts with HIV nef protein. In the presence of overexpressed Nef protein, Cyclin k and CDK9 binding is induced, inhibiting the positive elongation factor of other CDK9 binding complexes, resulting in an inhibition of specific HIV-1 gene expression.  CDK 13 may also be characterized to interact with HIV mRNA splicing, alongside Nef, and the underexpression of Gag and Env related proteins. 
Cyclin K is indispensable for Leukemia growth. SETD1A, is also known to bind Cyclin K through its FLOS domain. The interaction is shown to be important to DNA damage response genes and for Leukemia proliferation.
CDK5RAP2
CDK5 regulatory subunit-associated protein 2 is a protein that in humans is encoded by the CDK5RAP2 gene. Multiple transcript variants exist for this gene, but the full-length nature of only two has been determined. CDK5RAP2 is homologous to the Drosophila protein centrosomin (cnn).

# Function
Neuronal CDC2-like kinase, which is involved in the regulation of neuronal differentiation, is composed of a catalytic subunit, CDK5, and an activating subunit, p25NCK5A. The protein encoded by this gene binds to p25NCK5A and therefore may be involved in neuronal differentiation. The encoded protein may also be a substrate of neuronal CDC2-like kinase.

# Clinical significance
A magnetic resonance imaging study has demonstrated a link between common variation in the CDK5RAP2 gene and brain structure. More specifically, associations were found between several single nucleotide polymorphisms (SNPs) and brain cortical surface area and total brain volume.  These associations were found exclusively in male subjects and all SNPs were located upstream in non-exonic regions. The functional significance of these loci is not yet known. However, given their location close to regulatory elements, it is possible that they are involved in gene regulation, which suggests that common variance in brain structure could be associated with differences in gene regulation rather than protein structure, consistent with findings in other complex human traits.
CDK5RAP2 is needed as a scaffolding protein in the Corona of the centrosome of the Dictyostelium.

# Interactions
CDK5RAP2 has been shown to interact with CDK5R1.
CHRFAM7A
CHRNA7-FAM7A fusion protein is a protein that in humans is encoded by the CHRFAM7A gene.
The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The family member CHRNA7, which is located on chromosome 15 in a region associated with several neuropsychiatric disorders, is partially duplicated and forms a hybrid with a novel gene from the family with sequence similarity 7 (FAM7A). Alternative splicing has been observed, and two variants exist, for this hybrid gene. The N-terminally truncated products predicted by the largest open reading frames for each variant would lack the majority of the neurotransmitter-gated ion-channel ligand binding domain but retain the transmembrane region that forms the ion channel. Although current evidence supports transcription of this hybrid gene, translation of the nicotinic acetylcholine receptor-like protein-encoding open reading frames has not been confirmed.
CHRFAM7A has not been found in nonhuman primates, and its occurrence in individuals of African descent is significantly lower than in Caucasian populations.
Cadherin

# Overview
Cadherins are a class of type-1 transmembrane proteins.  They play important roles in cell adhesion, ensuring that cells within tissues are bound together.  They are dependent on calcium (Ca2+) ions to function, hence their name.
The cadherin superfamily includes cadherins, protocadherins, desmogleins, and desmocollins, and more. In structure, they share cadherin repeats, which are the extracellular Ca2+-binding domains. There are multiple classes of cadherin molecule, each designated with a one-letter prefix (generally noting the type of tissue with which it is associated). Cadherins within one class will bind only to themselves. For example, an N-cadherin will bind only to another N-cadherin molecule. Because of this specificity, groups of cells that express the same type of cadherin molecule tend to cluster together during development, whereas cells expressing different types of cadherin molecules tend to separate.

# Types
Different members of the cadherin family are found in different locations.
E-cadherins are found in epithelial tissue; N-cadherins are found in neurons; and P-cadherins are found in the placenta.  T-cadherins have no cytoplasmic domains and must be tethered to the plasma membrane.

# E-cadherin
E-cadherin (epithelial) is probably the best understood cadherin. It consists of 5 cadherin repeats (EC1 ~ EC5) in the extracellular domain, one transmembrane domain, and an intracellular domain that binds p120-catenin and beta-catenin. The intracellular domain contains a highly-phosphorylated region vital to beta-catenin binding and therefore to E-cadherin function. Beta-catenin can also bind to alpha-catenin. Alpha-catenin participates in regulation of actin-containing cytoskeletal filaments. In epithelial cells, E-cadherin-containing cell-to-cell junctions are often adjacent to actin-containing filaments of the cytoskeleton.
E-cadherin is first expressed in the 2-cell stage of mammalian development, and becomes phosphorylated by the 8-cell stage, where it causes compaction. In adult tissues, E-cadherin is expressed in epithelial tissues, where it is constantly regenerated with a 5-hour half-life on the cell surface.
Loss of E-cadherin function or expression has been implicated in cancer progression and metastasis. E-cadherin downregulation decreases the strength of cellular adhesion within a tissue, resulting in an increase in cellular motility. This in turn may allow cancer cells to cross the basement membrane and invade surrounding tissues.
Caecitis

# Overview
Caecitis, also called typhlitis or typhlenteritis, is an inflammation of the caecum (part of the small intestine) that may be associated with infection.

# Cause
The condition is usually caused by gram negative enteric commensal bacteria of the gut (gut flora). The most common agent associated with the condition is Pseudomonas aeruginosa.
Caecitis affects immunocompromised patients, such as those undergoing chemotherapy, patients with AIDS, kidney transplant patients, or the elderly.

# Signs and symptoms
Signs and symptoms of caecitis include a distended abdomen, fever, chills, nausea, vomiting, abdominal pain and tenderness, and diarrhea.

# Prognosis
Inflammation can spread to other parts of the gut in patients with caecitis.
The condition can also cause the cecum to become distended and can cut off its blood supply.  This and other factors can result in necrosis and perforation of the bowel, which can cause peritonitis and sepsis.  The mortality rate for caecitis can be as high as 40 to 50%, mostly because it is frequently associated with bowel perforation.  Caecitis is diagnosed with a radiograph CT scan showing thickening of the caecum and "fat stranding".
Cafergot
Cafergot is the proprietary name of a medication consisting of ergotamine tartrate or ergoline and caffeine.  This combination is used for the treatment of vascular headaches, such as migraine headache.

# Use
Correct timing of use is important. Cafergot is an abortive headache treatment, which prevents the development of the headache, rather than a treatment for an established headache. The medication should be administered at the first sign of headache.

# Mechanism of action
The causes of migraine are not fully understood, but dilation of blood vessels in the brain may play a part in causing the headache pain. Ergotamine tartrate and caffeine both are vasoconstrictors, substances which act to constrict blood vessels.

# Adverse effects
Because the vasoconstrictive effects of ergotamine and caffeine are not selective for the brain, adverse effects due to systemic vasoconstiction can occur. Cold feet or hands, angina pectoris or dizziness are some examples.
Ergotamine, if used frequently over a prolonged period of time, can cause dependence in the patient. If dependence occurs then cessation of ergotamine use can precipitate the same headaches which the drug was being used to treat. For this reason frequency of use must be restricted.
Cage bed
A cage bed is a bed with either metal bars or netting designed to restrain a person within the boundaries of the bed.
Psychiatric practitioners in the Czech Republic have stubbornly defended the use of the beds, calling them the best way to restrain patients who could harm themselves or others. "We can either use cage beds, or increase people's medication, strap them down, or put them in solitary confinement," says Jan Slezak, director of Social Care Home in Raby, eastern Bohemia. "We see cage beds as the best solution."
A political campaign to ban the use of cage beds in the Czech Republic was popularized by author J. K. Rowling.
Calmurid
Calmurid is the name of a cream that is manufactured by Galderma. Calmurid Cream contains the active ingredients lactic acid and urea, whereas Calmurid HC contains an additional ingredient, the mild corticosteroid hydrocortisone.
Due to lactic acid's keratolytic properties (to break down hard skin cells) and urea's hydrating properties, Calmurid is used primarily in the treatment of dry, scaly skin. Ichthyosis and general dermatitis in the absence of inflammation are some of its indications.
When the extra steroid component is added (as in Calmurid HC), it is used to treat dry, scaly skin that is accompanied by inflammation of the skin. This may include various forms of eczema. The presence of a corticosteroid, however, means that the cream should be used only sparingly and only for the shortest time period due to possible side effects that may occur due to systemic absorption of the steroid.
Calnexin
Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail.

# Function
Calnexin is a chaperone, characterized by assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. It specifically acts to retain unfolded or unassembled N-linked glycoproteins in the ER. Calnexin binds only those N-glycoproteins that have GlcNAc2Man9Glc1 oligosaccharides. These monoglucosylated oligosaccharides  result from the trimming of two glucose residues by the sequential action of two glucosidases, I and II. Glucosidase II can also remove the third and last glucose residue. If the glycoprotein is not properly folded, an enzyme called UGGT (for UDP-glucose:glycoprotein glucosyltransferase) will add the glucose residue back onto the oligosaccharide thus regenerating the glycoprotein's ability to bind to calnexin. The improperly-folded glycoprotein chain thus loiters in the ER, risking the encounter with MNS1 (alpha-mannosidase), which eventually sentences the underperforming glycoprotein to degradation by removing one of the nine mannose residues. If the protein is correctly translated, the chance of it being correctly folded before it encounters MNS1 is high.
Calnexin also functions as a chaperone for the folding of MHC class I -chain in the membrane of the ER. As newly synthesized MHC class I -chains enter the endoplasmic reticulum, calnexin binds on to them retaining them in a partly folded state. After the 2-microglobulin binds to the MHC class I peptide-loading complex (PLC), calreticulin and ERp57 take over the job of chaperoning the MHC class I protein while the tapasin links the complex to the Transporter associated with antigen processing (TAP) complex. This association prepares the MHC class I for binding an antigen for presentation on the cell surface.

# Cofactors
ATP and calcium ions are  cofactors involved in substrate binding for calnexin.
Catechin
Catechins are polyphenolic antioxidant plant metabolites, specifically flavonoids called flavan-3-ols. Although present in numerous plant species, the largest source in the human diet is from various teas derived from the tea-plant Camellia sinensis.

# Catechin, epicatechin, gallocatechin, epigallocatechin, and the gallates
Catechin and epicatechin are epimers, with (-)-epicatechin and (+)-catechin being the most common optical isomers found in nature. Catechin was first isolated from the plant extract catechu, from which it derives its name. Heating catechin past its point of decomposition releases pyrocatechol, which explains the common origin of the names of these compounds.
Epigallocatechin and gallocatechin contain an additional phenolic hydroxyl group when compared to epicatechin and catechin, respectively, similar to the difference in  pyrogallol compared to pyrocatechol.
Catechin gallates are gallic acid esters of the catechins; such as EGCG (epigallocatechin gallate), which is commonly the most abundant catechin in tea.

# Sources of catechins
Catechins constitute about 25% of the dry weight of fresh tea leaf, although total catechin content varies widely depending on clonal variation, growing location, seasonal/ light variation, and altitude. They are present in nearly all teas made from Camellia sinensis, including white tea, green tea, black tea and Oolong tea.
Catechins are also present in the human diet in chocolate, fruits, vegetables and wine and are found in many other plant species.

# Health benefits of catechins
The health benefits of catechins have been studied extensively in humans and in animal models. Reduction in atherosclerotic plaques was seen in animal models.  Reduction in carcinogenesis was seen in vitro.
Many studies on health benefits have been linked to the catechin content.
According to Norman Hollenberg, professor of medicine at Harvard Medical School, epicatechin can reduce the risk of four of the major health problems: stroke, heart failure, cancer and diabetes. He studied the Kuna people in Panama, who drink up to 40 cups of cocoa a week, and found that the prevalence of the "big four" is less than 10%. He believes that epicatechin should be considered essential to the diet and thus classed as a vitamin.Science Daily March 12, 2007
According to one researcher epigallocatechin-3-gallate is an antioxidant that helps protect the skin from UV radiation-induced damage and tumor formation.
A study on green-tea catechins is reviewed here:
Cefotiam

# Overview
Cefotiam is a parenteral second-generation cephalosporin antibiotic. It has broad-spectrum activity against Gram-positive and Gram-negative bacteria. As a beta-lactam, its bactericidal activity results from the inhibition of cell wall synthesis via affinity for penicillin-binding proteins.
Cefotiam was launched as Pansporin in February 1981 by Takeda Pharmaceutical of Japan and has been available as a generic since February 1993.

# Mechanism of action
Cefotiam inhibits final cross-linking stage of peptidoglycan production, thus inhibiting bacterial cell wall synthesis. It has similar or less activity against Gram-positive staphylococci and streptococci, but is resistant to some beta-lactamases produced by Gram-negative bacteria. It is more active against many of the Enterobacteriaceae including Enterobacter, E. coli, Klebsiella, Salmonella and indole-positive Proteus species.
In clinical use, high concentrations of cefotiam are observed in several tissues (kidney, heart, ear, prostate, and genital tract), as well as in fluids and secretions (bile, ascitic fluid).

# Spectrum of bacterial susceptibility
Cefotiam has a broad spectrum of activity and has been used to treat infections caused by a number of enteric bacteria and bacteria responsible for causing skin infections. The following represents MIC susceptibility data for a few medically significant bacteria.
- Bacteroides fragilis: - 16 - >128 g/ml
- Clostridium difficile: >128 g/ml
- Staphylococcus aureus: 0.25 - 32 g/ml

# Indications
This drug is indicated for prophylaxis for surgical infection, postoperative infections, bacterial septicaemia, bone and joint infections, cholangitis, cholecystitis, peritonitis, prostatitis, pyelonephritis, respiratory tract infections, skin and soft tissue infections, cystitis, urethritis, and infections caused by susceptible organisms. It does not have activity against Pseudomonas aeruginosa.

# Dosage
For adults, the dose is up to 6 grams daily by intravenous or intramuscular route in divided doses according to severity of infection. In patients with renal impairment a dose reduction may be needed.

# Adverse effects
Side effects include nausea and vomiting, diarrhoea, hypersensitivity reactions, nephrotoxicity, convulsions, CNS toxicity, hepatic dysfunction, haematologic disorders, pain at injection site, thrombophloebitis, pseudomembranous colitis, and superinfection with prolonged use.
Celacade
Celacade is a non-pharmacological treatment also known as Immune Modulation Therapy (IMT), developed by the Canadian based biotherapeutics company Vasogen, for treatment of chronic heart failure and peripheral artery disease. 
At the World Congress of Cardiology in September 2006 the Advanced Chronic Heart Failure Clinical Assessment of Immune Modulation Therapy (ACCLAIM) a phase III randomized, double-blind, placebo-controlled clinical trial involving some 2408 patients in 7 countries with left ventricular ejection fraction of 30% or less,  reported that patients with a previous cardiovascular event receiving celacade where 39% less likely to die or be hospitalized due to a heart attack or stroke and tended to have improved quality of life.  
Celacade is believed to inhibit inflammation, platelet aggregation and progression of arterial lesions by a mechanism independent of cholesterol lowering. 
Celcade is a device-based outpatient procedure involving ex vivo exposure of 10ml autologous blood to heat, ultraviolet irradiation, controlled oxidative ozone therapy and subsequent intramuscular administration at monthly intervals. 
The results of ACCLAIM support the hypothesis that immune dysfunction plays a role in the pathogenesis of atherosclerosis  and Immune Modulation therapy has a broad-spectrum positive effect on a number of immune mediators, including regulation and enhancement of cytokines and the vascular dilator nitric oxide. These cell signaling molecules regulate inflammation and facilitate the healing process. 
Vasogen in collaboration with Grupo Ferrer Internacional has regulatory approval to market Celacade as a medical device for the treatment of chronic heart failure in the European Union and Latin America.
In the United States the FDA has recommended that Vasogen conduct a further confirmatory study to support a pre-market approval filing.