Persius/hicric huggingface dataset:
Biglycan
Biglycan is a small leucine-rich repeat proteoglycan (SLRP) which is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. In humans, biglycan is encoded by the BGN gene which is located on the X chromosome.
The name "biglycan" was proposed in an article by Fisher, Termine and Young in an article in the Journal of Biological Chemistry in 1989 because the proteoglycan contained two GAG chains; formerly it was known as proteoglycan-I (PG-I).

# Structure
Biglycan consists of a protein core containing leucine-rich repeat regions and two glycosaminoglycan (GAG) chains consisting of either chondroitin sulfate (CS) or dermatan sulfate (DS), with DS being more abundant in most connective tissues. The CS/DS chains are attached at amino acids 5 and 10 in human biglycan. The composition of the GAG chains has been reported as varying according to tissue of origin. Non-glycanated forms of biglycan (no GAG chains) increase with age in human articular cartilage.
The composition of GAG chains of biglycan and decorin originating from the same tissue has been reported to be similar.
The structure of biglycan core protein is highly conserved across species; over 90% homology has been reported for rat, mouse, bovine and human biglycan core proteins.

# Function
Biglycan is believed to play a role in the mineralization of bone. Knock-out mice that have had the gene for biglycan suppressed (Bgn -/-) have an osteoporosis-like phenotype with reduced growth rate  and lower bone mass than mice that can express biglycan.
Biglycan core protein binds to the growth factors BMP-4 and influences its bioactivity. It has also been reported that the presence of biglycan is necessary for BMP-4 to exert its effects on osteoblasts. There is also evidence that biglycan binds to TGF-beta 1.

# Interactions
Biglycan interacts with collagen, both via the core protein and GAG chains. It has been reported that biglycan interacts more strongly with collagen type II than collagen type I. Biglycan has been reported to compete with decorin for the same binding site on collagen.
Biglycan has been shown to interact with SGCA.
Biglycan is a particularly important proteoglycan for binding to lipoprotein in human blood vessels, thus being a significant cause of atherosclerosis.
Blastula
The blastula is an early stage of embryonic development in animals. It is also called blastosphere. It is produced by cleavage of a fertilized ovum and consists of a spherical layer of around 128 cells surrounding a central fluid-filled     cavity called the blastocoel. The blastula follows the morula and precedes the gastrula in the developmental sequence.

# Research
A whitefish blastula is often used to help study the processes of mitosis in animal cells. The blastula is prevented from multiplying during the nuclear-injection stage.

# Formation of blastocyst
In mammals, blastulation leads to the formation of the blastocyst, which must not be confused with the blastula; even though they are similar in structure, their cells have different fates.  The blastocyst consists of two primary cell lines:
- the inner cell mass, also known as the "embryoblast"
- the trophoblast
The former is the source of embryonic stem cells and gives rise to all later structures of the adult organism.  The latter combines with the maternal endometrium to form the placenta in eutherian mammals.
Bone wax
Bone wax is made of beeswax containing a softening agent such as paraffin. Bone wax is used to mechanically stop bone bleeding during surgical procedures. The bone wax is smeared across the bleeding edge of the bone, blocking the holes and causing immediate bone hemostasis through a tamponade effect.  Bone wax is supplied in sterile sticks, and most often requires softening before it can be applied. Once applied, it essentially never goes away. Although inexpensive, easy to use and immediate, bone wax has a number of adverse reactions associated with it.
Bone wax inhibits formation of new bone osteogenesis and acts as a physical barrier preventing bone union.
In the presence of bone wax, osteoblasts will be absent in a bone defect. In defects where bone wax was applied and removed after 10 minutes, there was complete inhibition of bone regeneration. For this reason bone wax is almost never used in areas where bone fusion is critical.
Bone wax increases infection rates and impairs the ability of bone to clear bacteria. In the presence of bone wax, the number of bacteria needed to produce osteomyelitis is reduced by a factor of 10,007.  In a recent study of infection rates following spinal surgery, surgical site infections occurred in 6 of 42 cases in which bone wax was used, and in only 1 of 72 cases in which it was not used.
Infection and non-union are a particularly important problem in cardiac surgery. According to the American Heart Association, the incidence of deep sternal wound infections is 1% to 5% of patients undergoing coronary artery bypass surgery, with a mortality rate of about 25%.
Bone wax remains as a foreign body for many years, and can cause a giant cell reaction and local inflammation. In skull base surgery, bone wax has been reported to cause granuloma formation and CSF fluid leaks.
The FDA has recently approved a new water soluble bone hemostasis material designed to look and feel like bone wax. This material comprises a sterile mixture of water-soluble alkylene oxide copolymers, derived from ethylene oxide and propylene oxide. These copolymers have a long history in the medical and pharmaceutical fields, and they are considered inert. These compounds are not metabolized, but eliminated from the body unchanged. 
It is anticipated that with the introduction of these new hemostatic materials, the incidence of surgical bone infections, non-union and inflammatory complications will decrease with time.
The alternative to bone wax is called Ostene. It does not have any of the complications known to occur with the use of traditional bone wax.
Boosting
Boosting is a machine learning meta-algorithm for performing supervised learning.  Boosting is based on the question posed by Kearns: can a set of weak learners create a single strong learner?  A weak learner is defined to be a classifier which is only slightly correlated with the true classification.  In contrast, a strong learner is a classifier that is arbitrarily well-correlated with the true classification.
The affirmative answer to Kearns question has significant ramifications in machine learning and statistics.

# Boosting Algorithms
While boosting is not algorithmically constrained, most boosting algorithms follow a template.  Typically boosting occurs in iterations, by incrementally adding weak learners to a final strong learner. At every iteration, a weak learner learns the training data with respect to a distribution. The weak learner is then added to the final strong learner.  This is typically done by weighting the weak learner in some manner, which is typically related to the weak learner's accuracy.  After the weak learner is added to the final strong learner, the data is reweighted: examples that are misclassified gain weight and examples that are classified correctly lose weight (some boosting algorithms will actually decrease the weight of repeatedly misclassified examples, e.g. boost by majority and BrownBoost).  Thus, future weak learners will focus more on the examples that previous weak learners misclassified.
There are many boosting algorithms.  The original algorithms proposed by Rob Schapire (a recursive majority gate formulation ) and Yoav Freund (boost by majority ) were not adaptive and could not take full advantage of the weak learners.
Some algorithms refer to themselves as "boosting algorithms," and these algorithms can be quite effective.  However, in the probably approximately correct learning (PAC) model, only provable boosting algorithms should adopt the title "boosting."  Algorithms that are similar to boosting in spirit, but not provably PAC-boosters, are sometimes called "leveraging algorithms."  These can be quite effective machine learning algorithms .

# Examples of Boosting Algorithms
The main variation between many boosting algorithms is their method of weighting training data points and hypotheses.  AdaBoost is very popular and perhaps the most significant historically as it was the first algorithm that could adapt to the weak learners.  However, there are many more recent algorithms such as LPBoost, TotalBoost, BrownBoost,MadaBoost, LogitBoost, and others.  Many boosting algorithms fit into the AnyBoost framework, which shows that boosting performs gradient descent in function space using a convex cost function.
Borazine
Borazine is an inorganic compound composed of the elements boron, nitrogen and hydrogen. In this cyclic compound three hydroborane (BH) units and three amino units (NH) alternate.
The compound was synthesised in 1926 by the chemists Alfred Stock and Pohland by a reaction of diborane with ammonia.  The structure is isoelectronic and isostructural with benzene and for this reason borazine is called inorganic benzene by a proposal of Nils Wiberg and the compound also goes by the name of borazol from the German name for benzene which is benzol.

# Synthesis
Borazine is synthesized from diborane and ammonia in a 1:2 ratio at 250 - 300 C with a conversion of 50%.
An alternative more efficient route begins with lithium borohydride and ammonium chloride with improved chemical yield:
In a two-step process to borazine, boron trichloride is first converted to trichloroborazine:
The B-Cl bonds are subsequently converted to B-H bonds:

# Properties
Borazine is a colourless liquid with an aromatic smell. In water it decomposes to boric acid, ammonia, and hydrogen. Borazine, with a standard enthalpy change of formation Hf of -531 kJ/mol, is thermally very stable.

## Structure
Borazine is isostructural with benzene and bond lengths are identical just as in benzene. The distance between boron and nitrogen in the ring is 0.1436 nm, the carbon carbon bond in benzene has a length of 0.1397 nm. The boron nitrogen bond is between that of the boron nitrogen single bond with 0.151 nm and the boron nitrogen double bond which is 0.131 nm. This suggests partial delocalisation of nitrogen lone pair electrons.

## Mesomers
The electronegativity of boron (2.04 on the Pauling scale) compared to that of nitrogen (3.04) and also the electron deficiency on the boron atom and the lone pair on nitrogen favor alternative mesomer structures for borazine.
Boron is the Lewis acid and nitrogen is the Lewis base.

# Reactions
Borazine is more reactive than benzene. It reacts with hydrogen chloride in an addition reaction. If borazine were truly aromatic like benzene this reaction would not occur without a Lewis acid catalyst.
The addition reaction with bromine takes place without catalyst. Borazines interact with nucleophilic attack at boron and electrophilic attack at nitrogen. Heating borazine at 70 C  expulses hydrogen with formation of a borazinyl polymer or polyborazylene in which the monomer units are coupled in a para fashion by new boron - nitrogen bonds.

# Applications
Borazine and borazine derivatives are potential precursors to boron nitride ceramics. Boron nitride can be prepared by heating polyborazylene to 1000 C. Borazines are also starting materials for other potential ceramics such as boron carbonitrides:
Bothrops
Bothrops is a genus of venomous pitvipers found in Central America, South America. Currently, 32 species are recognized. The generic name is derived from the Greek words bothros and ops that mean "pit" and "eye" or "face"; an allusion to the heat-sensitive loreal pit organs. Members of this genus are responsible for more human deaths in the Americas than any other group of venomous snakes.

# Description
These snakes range from small, never growing to more than 50-70 cm, to large at over 200 cm in length. Most are characterized by having a sharp canthus rostralis and an unelevated snout.
The arrangement of the scales on top of the head is extremely variable; the number of intrasupraoculars may be anything from 3 to 14. Usually there are 7-9 supralabials and 9-11 sublabials. There are 21-29 midbody dorsal scales, 139-240 ventral scales and 30-86 subcaudals, which are generally divided.

# Geographic range
Found in northeastern Mexico (Tamaulipas) southward through Central and South America to Argentina. Also occurs on the islands of Saint Lucia and Martinique in the Lesser Antilles, as well as on Ilha da Queimada Grande off the coast of Brazil.

# Behavior
Most species are nocturnal, although a few that are found at higher altitudes are active during the day. Otherwise they may be seen on cloudy days or during periods of rain. Most are terrestrial, even though all are capable of climbing. One in particular, B. insularis, has a reputation for often being found in trees.

# Venom
Members of this genus are responsible for more fatalities in the Americas than any other group of venomous snakes. In this regard, the most important species are B. asper, B. atrox and B. jararaca. Without treatment, the fatality rate is estimated to be about 7%, but with treatment this is reduced to 0.5-3%.
Typical symptoms of bothropic envenomation include immediate burning pain, dizziness, nausea, vomiting, sweating, headache, massive swelling of the bitten extremity, hemorrhagic blebs, local necrosis, bleeding from the nose and gums, ecchymosis, erythemia, hypotension, tachycardia, coagulopathy with hypofibrinogenemia and thrombocytopenia, hematemesis, melena, epistaxis, hematuria, intracerebral hemorrhage and renal failure secondary to hypotension and bilateral cortical necrosis. There is usually some discoloration around the bite site and rashes may develop on the torso or the extremities.
In general, death results from hypotension secondary to hypovolemia, renal failure and intracranial hemorrhage. Common complications include necrosis and renal failure secondary to hypovolemic shock and the toxic effects of the venom.

# Species
*) Not including the nominate subspecies (typical form).
T) Type species.

# Taxonomy
Other (new) species may be encountered in literature, such as:
- B. alcatraz - Marques, Martins & Sazima, 2002. Range: Brazil (Sao Paulo). Common name: jararaca-de-Alcatrazes.
- B. muriciensis - Ferrarezzi & Freire, 2001. Range: northeastern Brazil (Alagoas). Common name: Murici lancehead.
Brodmann

# Overview
Korbinian Brodmann (November 17, 1868 - August 22, 1918) was a German neurologist who became famous for his definition of the cerebral cortex into 52 distinct regions from their cytoarchitectonic (histological) characteristics. These areas are now usually referred to as Brodmann areas. Some of these areas were later associated to nervous functions, such as areas 41 and 42 in the temporal lobe (related to hearing), areas 1, 2 and 3 in the postcentral gyrus of the parietal lobe (the somatosensory region), and the areas 17 and 18 in the occipital lobe (the primary visual areas).

# Historical Perspective
Brodmann studied medicine in Munich, Wurzburg, Berlin and Freiburg, where he received his medical diploma in 1895. Subsequently he studied at the Medical School in the University of Lausanne in Switzerland, and then worked in the University Clinic in Munich. He got a doctor of medicine degree from the University of Leipzig in 1898, with a thesis on chronical ependymal sclerosis. He worked also in the Psychiatric Clinic in the University of Jena, with Ludwig Binswanger, and in the Municipal Mental Asylum in Frankfurt, from 1900 to 1901. There, he met Alois Alzheimer, who was influential in his decision to pursue neuroscientific basic research.
Following this, Brodmann started to work in 1901 with Cecile and Oskar Vogt at the private institute "Neurobiologischen Zentralstation" in Berlin, and in 1902 in the Neurobiological Laboratory of the University of Berlin. In 1915 he joined the Kaiser-Wilhelm-Institut fur Hirnforschung (Institute for Brain Research).
In 1909 he published his original research on cortical cytoarchitectonics in "Vergleichende Lokalisationslehre der Grohirnrinde in ihren Prinzipien dargestellt auf Grund des Zellenbaues" (Comparative Localization Studies in the Brain Cortex, its Fundamentals Represented on the Basis of its Cellular Architecture).
In the following years he worked at the University of Tubingen, where he was habilitated and made a full professor in 1913, and from 1910 to 1916 as physician and chairman of the Anatomical Laboratory at the University Psychiatric Clinic. In 1916 he moved to Halle in order to work in the Nietleben Municipal Hospital. Finally, in 1918, he accepted an invitation from the University of Munich to direct the group of histology at Psychiatric Research Center.
He died in Munich rather suddenly of a generalized septic infection following a pneumonia, barely under 50 years of age on August 22, 1918.
Brucella

# Overview
Human brucellosis is caused by four Brucellae species: B. abortus, B. canis, B. melitensis, and B. suis.

# Causes
- Brucella is a genus of gram-negative bacteria.They are small (0.5 to 0.7 by 0.6 to 1.5 m), non-motile and encapsulated coccobacilli.

## Brucella species
Brucella species have been found primarily in mammals.  Brucellla species, with their host and degree of virulence is described below:

## Tests to differentiate brucella species
Following tests may be used to differentiate between the different species of brucella.
C11orf16
Gene C11orf16, chromosome 11 open reading frame 16, is a protein in humans that is encoded by the C11orf16 gene. It has 7 exons, and the size of 467 amino acids.

# Gene

## Location
The gene C11orf16 is located on chromosome 11(p15.4), starting at 8,920,076bp and ending at 8,933,006bp.

## Gene Neighborhood
Gene ASCL3 and AKIP1 are the neighbor genes of C11orf16 on Chromosome 11.

## Expression

### Human
The gene does not have high expression throughout the body tissues. The percentile rank within the sample are higher in pancreas, ovary, and appendix.

### Mouse Brain
Even though the gene does not have a significant high expression in the mouse brain, it is most expressed in midbrain, isocortex, olfactory areas, and medulla.

## Transcription Factors
Some transcription factors that have the higher martix similarity are Kruppel-like zinc finger protein 219, Zinc finger protein 263, ZKSCAN12 (zinc finger protein with KRAB and SCAN domains 12), chorion-specific transcription factor GCMa, and Ras-responsive element binding protein 1.

# mRNA

## Isoform
The predicted C11orf16 transcript variant X1 is 2386bp long and has NCBI accession number of XM_017018013.1.

# Homology

## Paralogs
No paralogs were found for the C11orf16 gene through NCBI BLAST.

## Orthologs

## Conservation
The gene C11orf16 is conserved in many animal species including mammals, avians, and reptiles.

# Protein

## Molecular Weight
The predicted molecular weight of the protein encoded by C11orf16 is 51 kiloDaltons.

## Domains and Motifs
Several protein domains and motifs were found including CHD5-like protein, Tyrosine kinase phosphorylation site, Protein kinase C phosphorylation site, N-myristoylation site, Casein kinase II phosphorylation site, and cGMP-dependent protein kinase phosphorylation site. The picture indicates the location of the motifs.

## Secondary Structure
The protein is predicted to be made up with 21.2% of alpha helix, 15.2% of extended strand, and 63% of random coil.

## Post-translational Modifications
No transmembrane helices, potential GPI-modification site, and TM-protein were found. There were 7 predicted sumoylation sites, multiple phosporylation cites with most of them being unsp, and 9 glycosylation cites.

## Subcellular Localization Predictor
The protein is predicted to be localized to the nucleus with the probability of 47.8%; mitochondria with the probability of 26.1%.

## Protein Interaction
Proteins C1orf105(Chromosome 1 open reading frame105 ), PWWP2A, and SMYD1(SET and MYND domain containing 1) were found to be interacting with C11orf16.

# Clinical Significance

## Disease Association
Protein coded by C11orf16 gene is also predicted to have 19.61% sequence identity to tumor suppressor p53-binding protein suggesting that this gene might be involved with tumor suppressing process.
C11orf30
Protein EMSY is a protein that in humans is encoded by the C11orf30 gene.

# Clinical significance
C11orf30 has been shown to associate with atopy and susceptibility to poly-sensitisation.

# Interactions
C11orf30 has been shown to interact with ZMYND11, BRCA2 and CBX1.
C16orf42
C16orf42, or chromosome 16 open reading frame 42, is a hypothetical human protein found on chromosome 16. Its protein is 312 amino acids long. and its cDNA has 1214 base pairs

# Function
The function of C16orf42 is unknown. It is predicted to be a transmembrane protein, however the cellular or subcellular membrane in which is resides is as well unknown.

# Homology
C16orf42 can also be found in many other organisms, including mammals, and certain fungi and plants. It is not found in bacteria. C16orf42 is highly conserved in many of its orthologs, especially its mammalian orthologs, as high as 95% identity in rhesus monkeys. It also has fairly high conservation in its more distant homologs, 53% identity in corn for example. It has one potential human paralog, the protein EGFL6.
Ortholog Analysis:

# Expression
C16orf42 is not expressed ubiquitously in humans. It is most highly expressed in the ovary, but not expressed at all in the blood and very little in the brain. One microarray experiment suggested that malaria causes its expression in the blood, but further experimentation is needed to support this claim. Its expression in tissues tends to remain constant when the tissue is diseased. However, a brief analysis of its orthologs show inconsistencies in tissue expression. This could be due to a lack of research of this protein in other species.

# Structure
The structure of C16orf42 is unknown. It is predicted to have multiple regions of alpha-helices, and a few short stretches of beta-strands. It contains a potential metal binding domain between amino acids 60-90. It has a predicted molecular weight of 33.6 kdal and an isoelectric point of 6.496000, making it slightly acidic. Compared to other human proteins, C16orf42 is high in the amino acids arginine and alanine, and low in the amino acid threonine.  A brief analysis of its strict orthologs show that they too are generally high in arginine and low in threonine as well as compared to the typical protein in their respective species.