Persius/hicric huggingface dataset:
IPLEX
IPLEX (mecasermin rinfabate  injection) is a drug developed by INSMED corporation for the treatment of growth failure in children with severe primary IGF-I deficiency (Primary IGFD) or with growth hormone (GH) gene deletion who have developed neutralizing antibodies to GH.
Due to a patent settlement, IPLEX is being taken off the market for shortstature related indications. However, IPLEX is being studied as a treatment for other several serious medical conditions.

# Potential treatment of Myotonic Muscular Dystrophy
IPLEX is being investigated in a Phase II clinical study at the University of Rochester School of Medicine, with funding provided by the Muscular Dystrophy Association and the National Institutes of Health. This Phase II program is studying the safety and tolerability of once-daily, subcutaneous injection of IPLEX in patients with MMD. Initial data from this trial will be available in the second quarter of 2007.

# Potential treatment of HIV-Associated Adipose Redistribution Syndrome
IPLEX is also being explored as a possible therapy for HIV- Associated Adipose Redistribution Syndrome (HARS). Data is being collected from a Phase II open-label clinical study directed by Morris Schambelan, M.D., a professor of medicine at University of California San Francisco. Dr Shambelan serves as Chief of Endocrinology and Director of the General Clinical Research Center at San Francisco General Hospital. This study is designed to evaluate the safety and efficacy of IPLEX treatment with the primary goal of determining the effects of IPLEX on visceral fat distribution and glucose and lipid metabolism. Initial data from this trial is to be available in 2007, with Phase III trials initiating in 2009.

# Potential treatment of Retinopathy of Prematurity
Clinical work is at an earlier stage in the development of IPLEX to treat Retinopathy of Prematurity (ROP). This disease, affecting an estimated 14,000 to 16,000 premature infants each year, causes the lack of development of the small blood vessels in the back of the eye leading to blindness in the majority of cases. A Phase I clinical study investigating IPLEX as a treatment for ROP has been initiated at the University of Gothenburg in Sweden, in collaboration with scientists at the Harvard Medical School in the U.S. results of this study are expected by the end of 2007.

# Potential treatment of ALS
Amyotrophic Lateral Sclerosis (ALS), also known as Lou Gehrig's Disease is a progressive neurodegenerative disease that affects nerve cells in the brain and the spinal cord. Motor neurons reach from the brain to the spinal cord and from the spinal cord to the muscles throughout the body. The progressive degeneration of the motor neurons in ALS eventually leads to their death. When the motor neurons die, the ability of the brain to initiate and control muscle movement is lost. With voluntary muscle action progressively affected, patients in the later stages of the disease may become totally paralyzed.
In January 2007, INSMED announced that the Italian Ministry of Health requested INSMED corporation to make IPLEX available to treat Italian patients sufferings from ALS.

# Sources
- INSMED
KPNB1
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Importin subunit beta-1 is a protein that in humans is encoded by the KPNB1 gene.

# Function
Nucleocytoplasmic transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a classical nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits. Each of these subunits are part of the karyopherin family of proteins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. The protein encoded by this gene is a member of the importin beta family.

# Interactions
KPNB1 has been shown to interact with:
- KPNA3,
- Karyopherin alpha 1,
- Karyopherin alpha 2,
- Mothers against decapentaplegic homolog 3,
- NUP153
- NUP50,
- NUP98,
- Nucleoporin 62,
- P53,
- Parathyroid hormone-related protein,
- RANBP1,
- RANBP2,
- Ran (biology),  and
- SMN1.
ISFET

# Overview
An ISFET is an ion-sensitive field effect transistor used to measure ion concentrations in solution; when the ion concentration (such as pH) changes, the current through the transistor will change accordingly. Here, the solution is used as the gate electrode. A voltage between substrate and oxide surfaces arises due to an ions sheath.
The surface hydrolyzation of OH groups of the gate materials varies in aqueous solutions due to pH value. Typical gate materials are Si3N4, Al2O3 and Ta2O5.
An ISFET's source and drain are constructed as for a MOSFET. The gate electrode is separated from the channel by a barrier which is sensitive to hydrogen ions and a gap to allow the substance under test to come in contact with the sensitive barrier. An ISFET's threshold voltage depends on the pH of the substance in contact with its ion-sensitive barrier.
ISG15
Interferon-stimulated gene 15 (ISG15) is a 17 kDA secreted protein that in humans is encoded by the ISG15 gene. The main cellular function of the protein is ISGylation, its covalent addition to cytoplasmic and nuclear proteins, similar to ubiquitination. In addition, ISG15 has anti-viral activity.
ISG15 shares several common properties with other ubiquitin-like proteins (UBLs), but its activity is tightly regulated by specific signaling pathways that have a role in innate immunity. ISG15 was identified as an interferon stimulated gene (ISG) since its expression is induced in response to type I interferons or lipopolysaccharide treatment. Upon interferon treatment, ISG15 can be detected in both free and conjugated forms, and is secreted from monocytes and lymphocytes where it can function as a cytokine. In the cell, ISG15 co-localizes with intermediate filaments and ISGylation may modulate the JAK-STAT pathway or certain aspects of neurological disease. It is also known as UCRP (ubiquitin cross-reactive protein) since it contains 2 tandem ubiquitin homology domains and is cross-reactive with ubiquitin antibodies. In contrast to other UBLs, ISG15 has not been identified in lower eukaryotes (yeast, nematode, insects, plants) indicating its role in specialized functions.

# ISGylation
The mechanism of ISGylation and deISGylation is similar to that of ubiquitin, although the complete system components have not yet been identified. The activating E1 enzyme (UBE1L) charges ISG15 by forming a high-energy thiolester intermediate and transfers it to the UbcH8 E2 protein. UbcH8 has been identified as the major E2 for ISGylation, although it also functions in ubiquitination. The E2 protein subsequently transfers the ISG15 to specific E3 ligases (Herc5) and relevant intracellular substrates. Only one deconjugating protease with specificity to ISG15 has been identified to date: UBP43 (a member of the USP family) cleaves ISG15-peptide fusions and also removes ISG15 (deISGylation) from native conjugates.

# Pathology
In pancreatic ductal adenocarcinoma, tumor-associated macrophages secrete ISG15 enhancing the phenotype of cancer stem cells in the tumor.
iSOFT
iSOFT is an international supplier of software applications for the healthcare sector. Its products are used by more than 8,000 organisations in 27 countries for managing patient information and healthcare services.
The company, which has its headquarters in England, is heavily involved in the UK National Health Service's National Programme for IT (NPfIT), which aims to connect over 30,000 doctors in general practice to almost 300 hospitals and to give patients access to their own healthcare information.
Although iSOFTs revenue increased by 8.4% to just over 200m in 2005-6, the company reported a pre-tax loss of 343.8m for the 12 months ended 30 April 2006, due mainly to a one-off goodwill impairment charge of 351.4m  a non-cash adjustment related to iSOFTs acquisition of other companies in recent years.
In August 2006, it was confirmed that the UK government watchdog, the Financial Services Authority (FSA), was investigating possible accounting irregularities at iSOFT, in relation to the years ended 30 April 2004 and 2005.
On 23rd January 2007, the sale of iSOFT started to move forward, with three companies being shortlisted as bidders for the company. The Times newspaper listed U.S. healthcare IT providers Cerner and McKesson, as well as U.S. private equity company General Atlantic as the three companies looking at a package of around 200m to purchase iSoft.
On 16th May 2007, iSOFT announced its recommendation to accept a merger with Australian company IBA Health in an all-stock deal. 
On 6th June 2007, Computer_Sciences_Corporation said it was not excluding the possibility of a CSC bid for iSOFT.
On 6th July 2007, iSOFT shareholders voted in favour of the IBA Health offer.
On 20th July 2007, CompuGROUP made an eleventh hour offer. iSOFT directors considered this proposal and concluded that the offer represented better value to iSOFT shareholders than the IBA offer. More details here.
On 21st August 2007, IBA made a revised offer and the iSOFT board recommended acceptance by shareholders. CompuGROUP said in response that it would not be increasing its own offer.
ITFG3
Protein ITFG3 also known as family with sequence similarity 234 member A (FAM234A) is a protein that in humans is encoded by the ITFG3 gene.  Here, the gene is explored as encoded by mRNA found in Homo sapiens.  The FAM234A gene is conserved in mice, rats, chickens, zebrafish, dogs, cows, frogs, chimpanzees, and rhesus monkeys. Orthologs of the gene can be found in at least 220 organisms including the tropical clawed frog, pandas, and Chinese hamsters. The gene is located at 16p13.3 and has a total of 19 exons.  The mRNA has a total of 3224 bp and the protein has 552 aa.  The molecular mass of the protein produced by this gene is 59660 Da.  It is expressed in at least 27 tissue types in humans, with the greatest presence in the duodenum, fat, small intestine, and heart.
A Newfoundland deletion or a0-thalassemia deletion has been found within the second intervening sequence of the FAM234A gene. The gene is associated with multiple red blood cell phenotypes in African Americans  though the exact function or effect of the gene was not entirely clear.  Review of GeneCards current database on the FAM234A gene provided no additional elucidation on the function of the gene.

# Gene
FAM234A is located on Chromosome 16 (234,546 - 269, 943). It is 35,398 bases long, contains 11 exons, and is oriented on the plus strand in the 5' to 3' direction. Other aliases include ITFG3, C16orf9, and gs19.
There are no known paralogs of FAM234A.
The FAM234A gene is conserved in at least 220 organisms, with no evidence for conservation of the gene in single celled organisms. Listed below is a selection of orthologs with the estimated date of divergence from human lineage in million years ago (MYA), the accession number, and the % identity to human FAM234A. This list does not contain all of the known orthologs.

# mRNA
There are at least 11 FAM234A isoforms. Aside from the longest transcript, the other isoforms differ by truncation, primarily at the 3' end. This results in a wide variation in sequence length between isoforms.

# Protein
The FAM234A gene encodes a serine and leucine rich protein titled the "FAM234A Protein" or ITFG3. The encoded protein is 552 amino acids in length with a predicted molecular weight of 59,660Da and a basal isoelectric point of 5.84. The FAM234A protein has a notable hydrophobic region from position 49-70 in the amino acid sequence that correlates with one of the two trans-membrane regions found on FAM234A. FAM234A has membrane topology type 3a, indicating multiple trans-membrane regions with it's N-terminus facing the cytosol. The protein is predicted to be located in the endoplasmic reticulum, with portions of it found within the endoplasmic reticulum lumen. Within the cell, FAM234A has also been localized to the ribosomes and nucleus.
ITGA9
Integrin alpha-9 is a protein that in humans is encoded by the ITGA9 gene.

# Function
This gene encodes an alpha integrin. Integrins are heterodimeric integral membrane glycoproteins composed of an alpha chain and a beta chain that mediate cell-cell and cell-matrix adhesion. The protein encoded by this gene, when bound to the beta 1 chain, forms an integrin that is a receptor for tenascin-C, VCAM1 and osteopontin. Expression of this gene has been found to be upregulated in small cell lung cancers.

# Interactions
The 9 subunit forms a heterodimeric complex with a 1 subunit to form the 91 integrin. This integrin participates in cell adhesion with various ligands in the extracellular matrix (ECM), including extra domain A (EDA) fibronectin, tenascin-C, ADAMs, EMELIN1, osteopontin, and VEGF. 91 binding is independent of the RGD peptide sequence.
ITGAV
Integrin alpha-V is a protein that in humans is encoded by the ITGAV gene.

# Function
ITGAV encodes integrin alpha chain V. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha V undergoes post-translational cleavage to yield disulfide-linked heavy and light chains, that combine with multiple integrin beta chains to form different integrins. Among the known associating beta chains (beta chains 1,3,5,6, and 8; 'ITGB1', 'ITGB3', 'ITGB5', 'ITGB6', and 'ITGB8'), each can interact with extracellular matrix ligands; the alpha V beta 3 integrin, perhaps the most studied of these, is referred to as the Vitronectin receptor (VNR). In addition to adhesion, many integrins are known to facilitate signal transduction.

# Alpha V class integrins
In mammals the integrins that include alpha-V are :

# Clinical significance
Overexpression of the ITGAV gene is associated with progression and spread of colorectal cancer, and prostate cancer.

# As a drug target
The mAbs intetumumab, and abituzumab target this protein which is found on some tumour cells.
ITGB4
Integrin, beta 4 (ITGB4) also known as CD104 (Cluster of Differentiation 104), is a human gene.

# Function
Integrins are heterodimers composed of alpha and beta subunits, that are noncovalently associated transmembrane glycoprotein receptors. Different combinations of alpha and beta polypeptides form complexes that vary in their ligand-binding specificities. Integrins mediate cell-matrix or cell-cell adhesion, and transduced signals that regulate gene expression and cell growth. This gene encodes the integrin beta 4 subunit, a receptor for the laminins. This subunit tends to associate with alpha 6 subunit and is likely to play a pivotal role in the biology of invasive carcinoma. Mutations in this gene are associated with epidermolysis bullosa with pyloric atresia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

# Interactions
ITGB4 has been shown to interact with Collagen, type XVII, alpha 1, EIF6 and Erbin.
ITGB8
Integrin beta-8 is a protein that in humans is encoded by the ITGB8 gene.

# Function
This gene is a member of the integrin beta chain family and encodes a single-pass type I membrane protein with a VWFA domain and four cysteine-rich repeats. This protein noncovalently binds to an alpha subunit to form a heterodimeric integrin complex. In general, integrin complexes mediate cell-cell and cell-extracellular matrix interactions and this complex plays a role in human airway epithelial proliferation. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.  Additionally, it has been shown to interact with RhoGDI1 to alter the activation of Rho GTPases to promote Glioblastoma cell invasiveness.  Uncoupling the v8-RhoGDI1 interaction has been seen to block GBM cell invasion by hyperactivating Rho GTPases.

# Clinical significance
High expression levels of ITGB8 are associated with high angiogenic and poorly invasive glioblastoma tumors.  Conversely low expression of ITGB8 correlates with highly invasive but low angiogenic tumors.
ITM2A
Integral membrane protein 2A is a protein that in humans is encoded by the ITM2A gene.

# Function
The protein encoded by this gene is  involved in osteo- and chondrogenic cellular differentiation (the cells which are responsible for the development of bone and cartilage respectively).
ITM2A  is also involved in activation of T-cells in the immune system and in myocyte differentiation.
ITPKA
Inositol-trisphosphate 3-kinase A is an enzyme that in humans is encoded by the ITPKA gene.

# Structure
ITPKA is one of three inositol-trisphosphate 3-kinase (ITP3K) genes in humans. ITP3K proteins regulate inositol phosphate metabolism by phosphorylation of the second messenger inositol 1,4,5-trisphosphate to produce Ins(1,3,4,5)P4, which is sometimes abbreviated as IP4. Structurally, ITPKA belongs to the inositol polyphosphate kinase (IPK) family. The activity of the inositol 1,4,5-trisphosphate 3-kinase is responsible for regulating the levels of a large number of inositol polyphosphates that are important in cellular signaling, most notably, inositol trisphosphate, which is the enzyme's only substrate. Both calcium/calmodulin and protein phosphorylation mechanisms control its activity. It is also a substrate for the cyclic AMP-dependent protein kinase, calcium/calmodulin- dependent protein kinase II, and protein kinase C in vitro. ITPKA and ITPKB are 68% identical in the C-terminus region The amino- terminal region of ITPKA binds filamentous actin. This property localizes the ITPKA to dendritic spines in principal neurons. ITPKA is expressed physiologically in neurons, but it is sometimes expressed in cancer cells and may contribute to processes of metastasis.

# Physiological function
ITPKA participates in learning and memory processes in neurons.

# Roles in human disease
Although ITPKA is expressed physiologically in neurons and testis, it sometimes becomes expressed in cancer cells, and the expression usually makes the cancer more aggressive.

# Relationship to F-tractin
F-tractin is amino acids 9-52 of rat ITPKA. It was later determined that amino acids 9-40 were sufficient for binding filamentous actin. When fused to a reporter, such as green fluorescent protein, It is useful for the vsualization of actin dynamics in living cells.
ITPKC
ITPKC is one of 3 human genes that encode for an Inositol-trisphosphate 3-kinase.  This gene that has been associated with Kawasaki disease. Kawasaki disease is an acute febrile illness that involves the inflammation of blood vessels throughout the body. The majority of cases that have been diagnosed involve children under the age of 5. In untreated cases involving children, 15 to 25 percent of these cases developed coronary artery aneurysms. The overproduction of T cells may be correlated with the immune hyperactivity in Kawasaki disease.
This gene is located at chromosome 19q13.1, it codes for one of three isoenzymes. The other two enzymes being ITPKA and ITPKB. ITPKC is involved in the Ca(2+)/NFAT pathway, negatively regulating T cell activation.
A mutation in this gene occurs through a single-nucleotide polymorphism. When a mutation occurs the gene does not produce a functioning enzyme, meaning it will no longer be effective in negatively regulating T cells. When there is this reduced expression of the enzyme, ITPKC, there is a higher amount of IP3 which leads to the calcium channels being opened, and a higher amount of calcium being released. Leading to overly active T cells, and having this mutation in ITPKC is correlated to the increased risk of developing symptoms.
IUBMB
The International Union of Biochemistry and Molecular Biology (IUBMB) is an international non-governmental organisation concerned with biochemistry and molecular biology. Formed in 1955 as the International Union of Biochemistry, the union has presently 77 member countries (as of 2008).
IUBMB organizes a triennial Congress of Biochemistry and Molecular Biology, and sponsors more frequent conferences, symposia, educational activities and lectures.
It publishes standards on biochemical nomenclature, including enzyme nomenclature, in some cases jointly with the International Union of Pure and Applied Chemistry (IUPAC).
It is associated with the journals Biochemistry and Molecular Biology Education (formerly Biochemical Education), BioEssays, BioFactors, Biotechnology and Applied Biochemistry, IUBMB Life, Molecular Aspects of Medicine and Trends (journals)|Trends in Biochemical Sciences.
The current president is Angelo Azzi. Past presidents include George Kenyon, Brian F.C. Clark, Mary Osborn, Harland G. Wood, William J. Whelan, K. Yagi and Hans Kornberg.
IUPAP
The International Union of Pure and Applied Physics (IUPAP) is an international non-governmental organization devoted to the advancement of physics. It was established in 1922 and the first General Assembly was held in 1923 in Paris.
The aims of the Union are: to stimulate and promote international cooperation in physics; to sponsor suitable international meetings and to assist organizing committees; to foster the preparation and the publication of abstracts of papers and tables of physical constants; to promote international agreements on the use of symbols, units, nomenclature and standards; to foster free circulation of scientists; to encourage research and education.
The Union is governed by its General Assembly, which meets every three years. The Council is its top executive body, supervising the activities of the nineteen specialized International Commissions and the three Affiliated Commissions. The Union is composed of Members representing identified physics communities. At present 49 Members adhere to IUPAP.
IUPAP is a member of the International Council for Science (ICSU).
The SUNAMCO Commission of the IUPAP published the book entitled Symbols, Units, Nomenclature and Fundamental Constants in Physics, 1987 Revision, by E.R. Cohen and P. Giacomo which is also known as the red book, I.U.P.A.P.-25, or SUNAMCO 87-1.  This book was reprinted from Physica, Vol. 146A, Nos. 1-2, p. 1 (November, 1987) .  The SP Technical Research Institute of Sweden website  makes the 1987 edition of the Symbols, Units, Nomenclature and Fundamental Constants in Physics available on the internet.