Persius/hicric huggingface dataset:
Imipenem
Imipenem is an intravenous beta-lactam antibiotic developed in 1985. 
Imipenem belongs to the subgroup of carbapenems. It is derived from a compound called thienamycin, which is produced by the bacteria Streptomyces cattleya. Imipenem has a broad spectrum of activity against aerobic and anaerobic Gram positive as well as Gram negative bacteria. It is particularly important for its activity against Pseudomonas aeruginosa and the Enterococcus species. It is not active against methicillin-resistant Staphylococcus aureus, however.  Imipenem and other drugs in the carbapenem class are commonly referred to as "magic bullets."  Their use is typically restricted in order to avoid widespread bacterial resistance.

# Method of action
Imipenem acts as an antimicrobial through inhibiting cell wall synthesis of various gram-positive and gram-negative bacteria. It remains very stable in the presence of beta-lactamase (both penicillinase and cephalosporinase) produced by some bacteria, and is a strong inhibitor of beta-lactamases from some gram-negative bacteria that are resistant to most beta-lactam antibiotics.

# Co-administration with cilastatin
Imipenem is rapidly degraded by the renal enzyme dehydropeptidase when administered alone, and is always co-administered with cilastatin to prevent this inactivation.

# Adverse effects
Common adverse drug reactions are nausea and vomiting. People who are allergic to penicillin and other beta-lactam antibiotics should not take imipenem. Imipenem can also cause seizures.
In vitro

# Overview
In vitro (Latin: (with) in the glass) refers to the technique of performing a given experiment in a test tube, or, generally, in a controlled environment outside a living organism. In vitro fertilization is a well-known example of this. Many experiments in cellular biology are conducted outside of organisms or cells; because the test conditions may not correspond to the conditions inside of the organism, this may result in inaccurate results. Consequently, such experimental results are often annotated with in vitro, in contradistinction with in vivo .

# In vitro research
This type of research aims at describing the effects of an experimental variable on a subset of an organism's constituent parts. It tends to focus on organs, tissues, cells, cellular components, proteins, and/or biomolecules. Overall, it is better suited for deducing the mechanisms of action (See in vivo for its description and respective merits). With fewer variables and perceptually amplified reactions to subtle causes, results are, generally, more discernible.
The massive adoption of low-cost in vitro molecular biology techniques has caused a shift away from in vivo research which is more idiosyncratic and expensive in comparison to its molecular counterpart. Currently, in vitro research is both vital and highly productive.
Indiplon
Indiplon (INN and USAN) is a nonbenzodiazepine, hypnotic sedative being developed in 2 formulations - an immediate release product for sleep onset and a modified-release version for sleep maintenance.

# Mode of action
Indiplon is said to work by enhancing the action of the inhibitory neurotransmitter GABA, like most other nonbenzodiazepine sedatives. Its primary function is to bind to BZ1 and Alpha1 subunits of the GABA-A receptors in the brain.

# Availability
Indiplon was originally scheduled for release to doctors and pharmacies sometime in 2007, most likely in the springtime of that year, which is when Sanofi-Aventis' popular sleep aid, zolpidem, lost its patent rights in the United States and thus became available to patients as a much less expensive generic. Neurocrine Biosciences had planned to comarket indiplon in the US with Pfizer. However, following the issuing of a nonapprovable letter for the modified-release formulation and an approvable letter for the immediate-release version by the FDA (May 2006), Pfizer decided to end its relationship with Neurocrine.
The planned brand name has not yet been revealed to the public. Various setbacks have given cause for industry pundits to say that Indiplon will not become available until sometime in 2008 at the earliest. The delay has caused Neurocrine's stock value to drop significantly. The new drug application (NDA) was approved by the FDA in 1998, and since then, Neurocrine has been conducting clinical trials, with purportedly satisfactory results.
The impending availability of Indiplon is, as of mid-2007, unknown. Repeated problems getting the drug approved by the FDA has sent Neurocrine back to the drawing board numerous times since it first started development of the drug in the 1990s.
According to the FDA, capsules containing 5 mg and 10 mg are approvable pending additional submission of information to the FDA, but tablets containing 15 mg received a letter of disapproval indicating significant data are needed to refile with the FDA for further consideration.
It should also be noted that the domains indiplon.com and indiplon.net are both owned by domain squatters. Normally, when a company is developing a new product, they'll register, if possible, several domain names to promote the product. Neurocrine/Pfizer has curiously not done this, contrary to Pfizer's regular practice of doing so.
Inotrope

# Overview
An inotrope (IPA: Template:IPA) is an agent which increases or decreases the force or energy of muscular contractions. Negatively inotropic agents weaken the force of muscular contractions. Positively inotropic agents increase the strength of muscular contraction.
Most commonly, the inotropic state is used in reference to various drugs that affect the strength of contraction of heart muscle (myocardial contractility). However, it can also refer to pathological conditions. For example, ventricular hypertrophy can increase inotropic state, while myocardial infarction can decrease it.

# Cardiac inotropes
Both positive and negative inotropes are used in the management of various cardiovascular conditions.
The choice of agent largely depends on specific pharmacological effects of individual agents with respect to the condition.
One of the most important factors affecting inotropic state is the level of calcium in the cytoplasm. Positive inotropes usually increase the level, while negative inotropes decrease it. However, not all drugs involve calcium release, and among those which do, the mechanism for manipulating the calcium level can vary from drug to drug.

# Positive inotropic agents
Positive inotropic agents increase myocardial contractility, and are used to support cardiac function in conditions such as decompensated congestive heart failure, cardiogenic shock, septic shock, myocardial infarction, cardiomyopathy, etc.
Examples of positive inotropic agents include:
- Calcium
- Calcium sensitisers
Levosimendan
- Levosimendan
- Cardiac glycosides
Digoxin
- Digoxin
- Catecholamines
Dopamine
Dobutamine
Dopexamine
Epinephrine (adrenaline)
Isoprenaline (isoproterenol)
Norepinephrine (noradrenaline)
- Dopamine
- Dobutamine
- Dopexamine
- Epinephrine (adrenaline)
- Isoprenaline (isoproterenol)
- Norepinephrine (noradrenaline)
- Phosphodiesterase inhibitors
Enoximone
Milrinone
Theophylline
- Enoximone
- Milrinone
- Theophylline

# Negative inotropic agents
Negative inotropic agents decrease myocardial contractility, and are used to decrease cardiac workload in conditions such as angina. While negative inotropism may precipitate or exacerbate heart failure, certain beta blockers (e.g. carvedilol) have been shown to reduce morbidity and mortality in congestive heart failure.
- Beta blockers
- Diltiazem
- Verapamil
Integrin

# Overview
Integrins are transmembrane receptors that mediate the attachment between a cell and its surroundings, such as other cells or the extracellular matrix (ECM). In signal transduction, integrins pass information about the chemical composition and mechanical status of the ECM into the cell. Therefore, in addition to transmitting mechanical forces across otherwise vulnerable membranes, they are involved in cell signaling and the regulation of cell cycle, shape, and motility.
Typically, receptors inform a cell of the molecules in its environment and the cell responds. Not only do integrins perform this outside-in signaling, but they also operate an inside-out mode. Thus, they transduce information from the ECM to the cell as well as reveal the status of the cell to the outside, allowing rapid and flexible responses to changes in the environment, for example to allow blood coagulation by platelets.
There are many types of integrin, and many cells have multiple types on their surface. Integrins are of vital importance to all animals and have been found in all animals investigated, from sponges to mammals. Integrins have been extensively studied in humans.
Integrins work alongside other proteins such as cadherins, immunoglobulin superfamily cell adhesion molecules, selectins and syndecans to mediate cellcell and cellmatrix interaction and communication. Integrins bind cell surface and ECM components such as fibronectin, vitronectin, collagen, and laminin.

# Structure
Integrins are obligate heterodimers containing two distinct chains, called the  (alpha) and  (beta) subunits. In mammals, eighteen  and eight  subunits have been characterized, whereas the Drosophila genome encodes only five  and two  subunits, and Caenorhabditis nematodes possess genes for two  subunits and one . The  and  subunits each penetrate the plasma membrane and possess small cytoplasmic domains.
Iodoform

# Overview
The compound iodoform is CHI3. A pale yellow, crystalline, volatile substance, it has a penetrating odor (in older chemistry texts, the smell is sometimes referred to as the smell of hospitals) and, analogous to chloroform, sweetish taste. It is slightly soluble in glycerol, petroleum ether or alcohol (78 g/l at 25 C), averagely soluble in chloroform, acetic acid and ether (136 g/l at 25 C) and easily soluble in benzene and acetone (120 g/l at 25 C).

# Physical properties
Its entalphy of sublimation is 69.9 kJ.mol-1 at range of temperatures 35 - 92 C.
Iodoform molecule parameters are: d(C-I) = 2.12  0.04 A, d(I-I) = 3.535  0.01 A and I-C-I = 113. Dipole moment is 1 D. Its space group is P63 and lattice constants are a = 6.83 A, c = 7.52 A.
It has critical point at 584.85 C, 5.63 MPa. Refractive index is 1.786 (D, 20 C).

# Synthesis
It was first prepared by Georges Serrulas in 1822 and its molecular formula was identified by Jean-Baptiste Dumas in 1834.
Iodoform can be synthesized in the haloform reaction by the reaction of iodine and sodium hydroxide with any one of these four kinds of organic compounds:
- a methyl ketone: CH3COR, where R is an organic side chain.
- acetaldehyde: CH3CHO
- ethanol: CH3CH2OH
- secondary alcohols: CH3CHROH, where R is an alkyl or aryl group.
These reactions are so reliable that it is called the iodoform test, signalled by the precipitation of pale yellow crystals.

# Reactions
Some reagents (e.g. hydroiodic acid) can convert iodoform to diiodomethane.
Also conversion to carbon dioxide is possible. Iodoform reacts with silver nitrate producing carbon monoxide, which is oxidized by mixture of sulfuric acid and iodine pentaoxide.

# Uses
It was used in medicine as a healing and antiseptic dressing for wounds and sores around the beginning of the 20th century, though this use is now superseded by better antiseptics.
Iodophor
An Iodophor is a preparation containing iodine complexed with a solubilizing agent, such as a surfactant or povidone (forming povidone-iodine).  The result is a water-soluble material that releases free iodine when in solution.  Iodophors are prepared by mixing iodine with the solubilizing agent; heat can be used to speed up the reaction.

# Medical Use
Free iodine kills the eukaryotic or prokaryotic cells by iodination of lipids and oxidation of compounds in the cytoplasm and cell membrane. Unlike with some antibiotics, microbes do not develop resistant strains against iodine. However, iodine is an irritant to mucous membranes and corrodes medical instruments. Iodine also kills live cells of mammals. Therefore, a slow release in smaller concentrations is desirable for patient use.
In iodophor formulations free iodine is released slowly from the carrier molecules, and thus are more gentle to the skin and have increased shelf-life. Effectiveness of any iodophore depends on active free iodine percentage. Percentages greater than 3.5% have no additional advantage.
Despite of all these advantages, iodophores must be used under technical supervision.  Many cases of toxicity and adverse reaction have been reported.

# Home Use
Diluted iodophor is often used by homebrewers and home wine makers to sanitize equipment and bottles.  Its major advantage over other sanitizers is that when used in proper proportions it sublimates directly from solution to gas, and hence leaves no residues. It is also non-toxic to humans and therefore especially suited to food processing applications. It is cheap and effective, but it can leave unattractive orange-brown stains on plastic parts and equipment that it is left in contact with.
It is often supplied in different concentrations and is further diluted with water before use. The label will advise the appropriate dilution rate, commonly 1:1000 or 1:100. Equipment to be sanitized should be thoroughly clean and left in contact with the solution for at least 2 minutes.
JC virus

# Overview
The JC virus (JCV)  is a type of human polyomavirus (formerly known as papovavirus) and is genetically similar to BK virus and SV40.  It was discovered in 1971 and named after the two initials of a patient with progressive multifocal leukoencephalopathy (PML). The virus is widespread, with 86% of the general population presenting antibodies, but it usually remains latent, causing disease only when the immune system has been severely weakened. The virus causes PML and other diseases only in cases of immunodeficiency, as in AIDS, or immunosuppression, as in organ transplant patients.

# Epidemiology
The virus is very common in the general population, infecting 70 to 90 percent of humans; most people acquire JCV in childhood or adolescence . It is found in high concentrations in urban sewage worldwide, leading some researchers to suspect contaminated water as a typical route of infection .
Minor genetic variations are found consistently in different geographic areas; thus, genetic analysis of JC virus samples has been useful in tracing the history of human migration .

# Infection and pathogenesis
The initial site of infection may be the tonsils , or possibly the gastrointestinal tract . The virus then remains latent in the gastrointestinal tract  and can also infect epithelial cells in the kidneys, where it continues to reproduce, shedding virus particles in the urine.
JCV can cross the blood-brain barrier into the central nervous system, where it infects oligodendrocytes and astrocytes, possibly through the 5-HT2A serotonin receptor . It is found within the brain even in people with no symptoms .
When immunodeficiency or immunosuppression allows JCV to reactivate, it attacks the previously infected tissues. In the kidneys, this results in hemorrhagic cystitis and ureteral stenosis; in the brain, it causes the usually fatal progressive multifocal leukoencephalopathy or PML by destroying oligodendrocytes. Several studies since 2000 have suggested that the virus is also linked to colorectal cancer, as JCV has been found in malignant colon tumors, but these findings are still controversial .
Java Man
Java Man is the name given to fossils discovered in 1891 at Trinil on the banks of the Bengawan Solo River in East Java, Indonesia, one of the first known specimens of Homo erectus. Its discoverer, Eugene Dubois, gave it the scientific name Pithecanthropus erectus, a name derived from Greek and Latin roots meaning upright ape-man.

# History and significance
Dubois' find was not a complete specimen, but consisted of a skullcap, a femur, and a few teeth. There is some dissent as to whether all these bones represent the same species. A second, more complete specimen was later discovered in the village of Sangiran, Central Java, 18km to the north of Solo. This find, a skullcap of similar size to that found by Dubois, was discovered by Berlin-born paleontologist GHR von Koenigswald in 1936. Many more finds have subsequently been made at the Sangiran site  , although official reports remain critical of the site's "poor" presentation and interpretation .
Until older human remains were discovered in the Great Rift Valley in Kenya, Dubois' and Koenigswald's discoveries were the oldest hominid remains ever found. Some scientists of the day suggested Dubois' Java Man as a potential intermediate form between modern humans and the common ancestor we share with the other great apes. The current consensus of anthropologists is that the direct ancestors of modern humans were African populations of Homo erectus (possibly Homo ergaster), rather than the Asian populations exemplified by Java Man and Peking Man.
As with many notable hominid fossil finds, some creationists have attempted to downplay the evolutionary significance of Java Man by arguing the specimen should be considered either fully human or fully ape. An example of the former argument is the claim that Java Man is "a true member of the Human family"; an example of the latter is the erroneous claim that Dubois himself later decided that Java Man was really a large Gibbon.
KCNQ1OT1
KCNQ1 overlapping transcript 1, also known as KCNQ1OT1, is a long non-coding RNA gene found in the KCNQ1 locus. This locus consists of 8-10 protein-coding genes, specifically expressed from the maternal allele (including the KCNQ1 gene), and the paternally expressed non-coding RNA gene KCNQ1OT1.  KCNQ1OT1 and KCNQ1 are imprinted genes and are part of an imprinting control region (ICR). Mitsuya identified that KCNQ1OT1 is an antisense transcript of KCNQ1. KCNQ1OT1 is a paternally expressed allele and KCNQ1 is a maternally expressed allele. KCNQ1OT1 is a nuclear, 91 kb transcript, found in close proximity to the nucleolus in certain cell types.
It interacts with chromatin, the histone methyltransferase G9a (responsible for the mono- and dimethylation of histone 3 lysine 9, H3K9), and the Polycomb Repressive Complex 2, PRC2, (responsible for the trimethylation of H3K27). It plays an important role in the transcriptional silencing of the KCNQ1 locus by regulating histone methylation. An 890 bp region at the 5' end of KCNQ1OT1 acts as a silencing domain. This region regulates CpG methylation levels of somatically acquired differentially methylated regions (DMRs), mediates the interaction of KCNQ1OT1 with chromatin and with DNA (cytosine-5)-methyltransferase 1 (DNMT1), but does not affect the interactions of histone methyltransferases with KCNQ1OT1.
The misregulation of the imprinted gene KCNQ1OT1 can lead to a variety of abnormalities. The loss of the maternal methylation of the KCNQ1OT1 allele is most commonly associated with Beckwith-Wiedemann syndrome. The deletion of KCNQ1OT1 in males can result in a removal of the repressor in six cis genes. Offspring from the males that had KCNQ1OT1 knocked out  weighed 20-25% less than the control.  If the deletion occurred in females, their offspring had no growth restrictions. Furthermore, uniparental paternal disomy (UPD) of KCNQ1OT1 is strongly associated with Wilms tumor.  In fact, three out of four patients with Beckwith-Wiedemann Syndrome and Wilms tumor  had UPD. When KCNQ1OT1 transcript is truncated, normally repressed alleles on the paternal chromosome are instead expressed. As the evidence shows, the misregulation of KCNQ1OT1 can lead to disastrous physical and genetic effects.
KIAA0319
KIAA0319 is a protein which in humans is encoded by the KIAA0319 gene.

# Clinical significance
Variants of the KIAA0319 gene have been associated with developmental dyslexia.
Reading disability, or dyslexia, is a major social, educational, and mental health problem. In spite of average intelligence and adequate educational opportunities, 5 to 10% of school children have substantial reading deficits. Twin and family studies have shown a substantial genetic component to this disorder, with heritable variation estimated at 50 to 70%.
An NIDCD-supported investigator recently has identified a mutation in a gene on chromosome 6, called the KIAA0319 gene, that appears to play a key role in Specific Language Impairment.

# Function
The KIAA0319 protein is expressed on the cell membrane and may be involved in neuronal migration.  Furthermore, KIAA0319 follows a clathrin-mediated endocytic pathway
KIAA0895
KIAA0895 is a human gene that encodes a protein known as KIAA0895 protein or hypothetical protein LOC23366. Other known aliases are OTTHUMP00000206979 and OTTHUMP00000206980.

# Gene
The KIAA0895 gene is located at p14.2 on chromosome 7.
It can be transcribed into 15 transcript variants, which in turn can produce 13 different isoforms of the protein.
The genomic DNA is 65,976 s long, while the longest mRNA that it produces is 4463 bases long.

## Gene Neighborhood
KIAA0895 is surrounded by the following genes on chromosome 7:
- ELMO1
- AOAH
- HERPUD2
- TBX20

# Protein
The longest protein isoform that is produced by the KIAA0895 gene is termed LOC23366 isoform 1 and is 520 amino acids long.

## Regions
LOC23366 contains a protein domain of unknown function called DUF1704.
It also contains a region of low complexity from position 120 to position 150 in the protein, and an arginine-rich area from position 12 to position 51.

## Post-translational Modification
The KIAA0895 protein is predicted to undergo phosphorylation at several serines, threonines, and tyrosines throughout its structure, particularly in the first half of the protein The predicted phosphorylation sites are shown on the accompanying graph. There are also predicted to be three N-linked glycosylation sites.

# Expression
KIAA0895 is shown to be expressed at low levels in various tissues throughout the body. It is expressed most highly in the adrenal gland, the bone marrow, and the testis. It is also found in cancerous tissues, most highly in cervical tumors and bladder carcinoma.

# Conservation
KIAA0895 has one paralog in humans known as KIAA0895L. Orthologs have been found in all mammals, and eukaryotes through T. thermophila. The full list of organisms in which orthologs have been found is given below.
- Pan troglodytes
- Pongo abelii
- Macaca mulatta
- Callithrix jacchus
- Sus scrofa
- Canis familiaris
- Ailuropoda melanoleuca
- Equus caballus
- Oryctolagus cuniculus
- Mus musculus
- Rattus norvegicus
- Monodelphis domestica
- Ornithorhynchus anatinus
- Taeniopygia guttata
- Meleagris gallopavo
- Gallus gallus
- Xenopus (Silurana) tropicalis
- Danio rerio
- Ciona intestinalis
- Strongylocentrotus purpuratus
- Branchiostoma floridae
- Tetrahymena thermophila