Persius/hicric huggingface dataset:
ORAI1
Calcium release-activated calcium channel protein 1 is a calcium selective ion channel that in humans is encoded by the ORAI1 gene. Orai channels play  an important role in the activation of T-lymphocytes. The loss of function mutation of Orai1 causes severe combined immunodeficiency (SCID) in humans  The mammalian orai family has two additional homologs, Orai2 and Orai3. Orai proteins share no homology with any other ion channel family of any other known proteins. They have 4 transmembrane domains and form hexamers.

# Structure and function
Orai channels are activated upon the depletion of internal calcium stores, which is called the "store-operated" or the "capacitative" mechanism. They are molecular constituents of the "calcium release activated calcium currents" (ICRAC). Upon activation of phospholipase C by various cell surface receptors, inositol trisphosphate is formed that releases calcium from the endoplasmic reticulum. The decreased calcium concentration in the endoplasmic reticulum is sensed by the STIM1 protein. STIM1 clusters upon the depletion of the calcium stores and forms "puncta", and relocates near the plasma membrane, where it activates Orai1 via protein-protein interaction.
In 2012, a 3.35-angstrom (A) crystal structure of the Drosophila Orai channel, which shares 73% sequence identity with human Orai1 within its transmembrane region, was published. The structure, thought to show the closed state of the channel, revealed that a single channel is composed of six Orai subunits, with the transmembrane domains arranged in concentric rings around a central aqueous pore formed exclusively by the first transmembrane helix of each subunit. Transmembrane helices 2 and 3 surround TM1 and are hypothesized to shield it from the surrounding lipid bilayer and provide structural support. The fourth transmembrane helix forms the outermost layer.
ORCON
ORCON (Operational Research CONsultancy) was developed by a UK consultancy company in 1974 as a standard for monitoring ambulance service performance.
The standard was later adopted internationally by a number of different countries including the Australian ambulance service.
ORCON standards are monitored through key performance indicators.
- Activation - All calls should have an ambulance 'activated' within 3 minutes of the phone being answered. This is usually made up of the control room tasking the crew within one minute, and the crew having a further 2 minutes to be 'on the road'. This is supposed to be achieved with 95% of calls.
- Category A calls, which are calls designated by AMPDS as being immediately life threatening. 75% of calls should receive an initial response within eight minutes (of the operator answering the call) and 95% of calls should receive an initial response within 19 minutes. The performance indicator generated by the ambulance service is expressed as a percentage of how many calls meet this.
- Category B are calls which are designated by AMPDS as being serious, but not immediately life threatening. 95% of calls should receive an initial response within 19 minutes. The performance indicator generated by the ambulance service is expressed as a percentage of how many calls meet this.
The distinction between urban/rural services ceased on 1 April 2006. Previously 95% of incidents had to be responded to within 14 minutes in urban services or 19 minutes in rural services. All services are now subject to the same response time requirements of 19 minutes.
OVGP1
Oviduct-specific glycoprotein also known as oviductal glycoprotein (OGP) or estrogen-dependent oviduct protein (EGP) or mucin-9 (MUC9) is a protein that in humans is encoded by the OVGP1 gene.

# Function
Oviduct-specific glycoprotein is a large, carbohydrate-rich, epithelial glycoprotein with numerous O-glycosylation sites located within threonine, serine, and proline-rich tandem repeats. The gene is similar to members of the mucin and the glycosyl hydrolase 18 gene families. Regulation of expression may be estrogen-dependent. Gene expression and protein secretion occur during late follicular development through early cleavage-stage embryonic development. The protein is secreted from non-ciliated oviductal epithelial cells and associates with ovulated oocytes, blastomeres, and spermatozoon acrosomal regions.
Beyond the oviduct, OVGP1 is detected in the mouse ovary, testis and epididymis suggesting its roles beyond fertilization. It is not detected in the mouse uterus, cervix, vagina, breast, seminal vesicles and prostate gland 
OVGP1 is expressed by the surface epithelium of the endometrium at the time of embryo implantation in the mouse. It is required for maintain the receptivity phenotype and trophoblast adhesion, OVGP1 mRNA levels are reduced in endometrium of women with recurrent implantation failure
OXA1L
Mitochondrial inner membrane protein OXA1L is a protein that in humans is encoded by the OXA1L gene located on 14q11.2.  The C-terminus of this protein interacts with mitochondrial ribosomes and helps insert both mitochondrial and nuclear produced proteins into the inner membrane of the mitochondria.

# Reference
-  Molina-Gomes D, Bonnefoy N, Nguyen VC, Viegas-Pequignot E, Rotig A, Dujardin G (1995). "The OXA1L gene that controls cytochrome oxidase assembly maps to the 14q11.2 region of the human genome". Genomics. 30 (2): 3968. PMID 8586451..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"\"""\"""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{display:none;font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
-  Haque ME, Elmore KB, Tripathy A, Koc H, Koc EC, Spremulli LL (2010). "Properties of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L and its interactions with mammalian mitochondrial ribosomes". The Journal of Biological Chemistry. 285 (36): 2835362. doi:10.1074/jbc.M110.148262. PMC 2934699. PMID 20601428.
-  Haque ME, Spremulli LL, Fecko CJ (2010). "Identification of protein-protein and protein-ribosome interacting regions of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L". The Journal of Biological Chemistry. 285 (45): 349918. doi:10.1074/jbc.M110.163808. PMC 2966113. PMID 20739282.
Obagi
Zein E. Obagi, M.D.
Diplomat, American Board of Dermatology Fellow, American Academy of Dermatology Licensed to practice in California and Michigan
Career & Education
1981  Present	 Private Practice
1980  1981 Staff Dermatologist, Naval Hospital Long Beach, CA
1977  1980 Resident in Dermatology, the Naval Hospital of San Diego San Diego, CA
1976  1977	 Naval Medical Officer, United States Navy Honolulu, HI
1975  1976	 Gynecology, Henry Ford Hospital, Detroit, MI
1973  1975	 Pathology Residency, William Beaumont Hospital Royal Oak, MI
1972  1973	 Rotating Intern, Deaconess Hospital Detroit, MI
1965  1972	 Damascus Medical School Damascus, Syria
Private Practices
2006  Present	 Obagi Skin Health Institute 270 N. Canon Drive, Suite 100 Beverly Hills, CA 90210
1994  2006	 Obagi Dermatology Medical Clinic 9033 Wilshire Boulevard, Suite 100 Beverly Hills, CA 90211
1994  Present	 Obagi Dermatology Medical Clinic, San Gabriel Annex 140 West Valley Blvd. #217 San Gabriel, CA 91776
Dr. Zein Obagi  Medical Director
Dr. Obagi is the Medical Director of ZO Skin Health, Inc. He is responsible for the development of new skincare treatments, protocols and product to achieve healthy skin. Additionally, he is a board certified practicing dermatologist and head of the Obagi Skin Health Institute in Beverly Hills, CA. , and an author and educator that has presented more than 200 skin health lectures throughout the world. For more than 35 years Dr. Obagi has defined and continues to advance skincare to include the concept of creating and maintaining healthy skin as opposed to just treating disease and damaged skin.
Dr. Obagi originally conceived and brought to market what would become the world's most recognized brands of physician dispensed skincare products  the original Obagi Nu-Derm and Obagi Blue Peel kit. Now Dr. Obagi, as the ZO Skin Health medical director, has redefined the concept of skin health to include comprehensive solutions that bridge the gap between therapeutics and maintaining truly healthy skin.
Oncom
Oncom is one of the staple foods of Indonesia. In Indonesia, there are two kinds of oncom: red oncom and black oncom. Oncom is closely related to tempeh; both are foods fermented using molds, traditionally made in Indonesia. Oncom is particularly associated with West Java.
Oncom is made from the sediment left behind as a by-product form other foods -- soy bean sediment when making tofu, peanut sediment left when extracting peanut oil, cassava sediment when extracting the starch (pati singkong), coconut sediment left after extracting coconut milk.
Red oncom is made by using the mold Neurospora sitophila; it is the only human food produced by Neurospora species.
Black oncom is made by using the mold Rhizopus oligosporus.

# Toxicity
In the production of oncom, sanitation and hygiene are important to avoid contaminating the culture with bacteria or other fungi like Apergillus flavus (which produces Aflatoxin). The molds used, Neurospora sitophila and Rhizopus oligosporus, are identified to be able to reduce the aflatoxin produced by Apergillus flavus.
While it is known that soya beans are the best substrate for growing R. oligosporus to create tempeh, oncom has not been as thoroughly studied; the best types of sediment for producing oncom are not yet known.
-  "Production of High-Quality Oncom, a Traditional Indonesian Fermented Food, by the Inoculation with Selected Mold Strains in the Form of Pure Culture and Solid Inoculum", D. D. Sastraatmadja et al., J. Grad. Sch. Agr. Hokkaido Univ., Vol. 70, Pt. 2: 111-127 (2002), at 
id:Oncom
su:Oncom
P110
The phosphatidylinositol-4,5-bisphosphate 3-kinase, catalytic subunit alpha (the HUGO-approved official symbol = PIK3CA; HGNC ID, HGNC:8975), also called p110 protein, is a class I PI 3-kinase catalytic subunit. The human p110 protein is encoded by the PIK3CA gene.
Its role was uncovered by molecular pathological epidemiology (MPE).

# Function
Phosphatidylinositol-4,5-bisphosphate 3-kinase (also called phosphatidylinositol 3-kinase (PI3K)) is composed of an 85 kDa regulatory subunit and a 110 kDa catalytic subunit. The protein encoded by this gene represents the catalytic subunit, which uses ATP to phosphorylate phosphatidylinositols (PtdIns), PtdIns4P and PtdIns(4,5)P2.
The involvement of p110 in human cancer has been hypothesized since 1995. Support for this hypothesis came from genetic and functional studies, including the discovery of common activating PIK3CA missense mutations in common human tumors. It has been found to be oncogenic and is implicated in cervical cancers. PIK3CA mutations are present in over one-third of breast cancers, with enrichment in the luminal and in human epidermal growth factor receptor 2-positive subtypes (HER2 +). The three hotspot mutation positions (GLU542, GLU545, and HIS1047) have been widely reported till date. While substantial preclinical data show an association with robust activation of the pathway and resistance to common therapies, clinical data do not indicate that such mutations are associated with high levels of pathway activation or with a poor prognosis. It is unknown whether the mutation predicts increased sensitivity to agents targeting the P3K pathway.
PIK3CA participates in a complex interaction within the tumor microenvironment in this phenomenon.

# Clinical characteristics
Due to the association between p110 and cancer, it may be an appropriate drug target. Pharmaceutical companies are designing and characterizing potential p110 isoform specific inhibitors.
The presence of  PIK3CA mutation may predict response to aspirin therapy for colorectal cancer.
Somatic activating mutations in PIK3CA are found in Klippel-Trenaunay syndrome and venous malformation.
PIK3CA-associated segmental overgrowth includes brain disorders such as macrocephaly-capillary malformation (MCAP) and hemimegalencephaly. It is also associated with congenital, lipomatous overgrowth of vascular malformations, epidermal nevi and skeletal/spinal anomalies (CLOVES syndrome) and fibroadipose hyperplasia (FH). The conditions are caused by heterozygous (usually somatic mosaic) mutations.

# Inhibition
All PI 3-kinases are inhibited by the drugs wortmannin and LY294002 but wortmannin shows better efficiency than LY294002 on the hotspot mutation positions.

# Pharmacology
In September 2017 Copanlisib, inhibiting predominantly p110 and p110, got FDA approval for the treatment of adult patients with relapsed follicular lymphoma (FL) who have received at least two prior systemic therapies.
P2RX4
P2X purinoceptor 4 is a protein that in humans is encoded by the P2RX4 gene.
The product of this gene belongs to the family of purinoceptors for ATP. Multiple alternatively spliced transcript variants have been identified for this gene although their full-length natures have not been determined.
The receptor is found in the central and peripheral nervous systems, in the epithelia of ducted glands and airways, in the smooth muscle of the bladder, gastrointestinal tract, uterus, and arteries, in uterine endometrium, and in fat cells. P2X4 receptors have been implicated in the regulation of cardiac function, ATP-mediated cell death, synaptic strengthening, and activating of the inflammasome in response to injury.

# Receptor structure and kinetics
The P2X4 subunits can form homomeric or heteromeric receptors. The P2X4 receptor has a typical P2X receptor structure. The zebrafish P2X4 receptor was the first purinergic receptor to be crystallized and have its three-dimensional structure solved, forming the model for the P2X receptor family.  
The P2X4 receptor is a ligand-gated cation channel that opens in response to ATP binding. The P2X4 receptor has high calcium permeability, leading to the depolarization of the cell membrane and the activation of various Ca2+-sensitive intracellular processes. Continued binding leads to increased permeability to N-methyl-D-glucamine (NMDG+) in about 50% of the cells expressing the P2X4 receptor.  The desensitization of P2X4 receptors is intermediate when compared to P2X1 and P2X2 receptors.

# Pharmacology

## Agonists
P2X4 receptors respond to ATP, but not meATP.  These receptors are also potentiated by ivermectin, cibacron blue, and zinc.

## Antagonists
The main pharmacological distinction between the members of the purinoceptor family is the relative sensitivity to the antagonists suramin and pyridoxalphosphate-6-azophenyl-2',4'-disulphonic acid (PPADS). The product of this gene has the lowest sensitivity for these antagonists

# Receptor trafficking
P2X4 receptors are stored in lysosomes and brought to the cell surface in response to extracellular signals.  These signals include IFN-, CCL21, CCL2. Fibronectin is also involved in upregulation of P2X4 receptors through interactions with integrins that lead to the activation of SRC-family kinase member, Lyn. Lyn then activates PI3K-AKT and MEK-ERK signaling pathways to stimulate receptor trafficking. Internalization of P2X4 receptors is clathrin- and dynamin-dependent endocytosis.

# Neuropathic pain
The P2X4 receptor has been linked to neuropathic pain mediated by microglia in vitro and in vivo.  P2X4 receptors are upregulated following injury.  This upregulation allows for increased activation of p38 mitogen-activated protein kinases, thereby increasing the release of brain-derived neurotrophic factor (BDNF) from microglia.  BDNF released from microglia induces neuronal hyperexcitability through interaction with the TrkB receptor. More importantly, recent work shows that P2X4 receptor activation is not only necessary for neuropathic pain, but it is also sufficient to cause neuropathic pain.
P2Y12
In the field of purinergic signaling, the P2Y12 protein is found mainly but not exclusively on the surface of blood platelets, and is an important regulator in blood clotting.
P2Y12 belongs to the Gi class of a group of G protein-coupled (GPCR) purinergic receptors and is a chemoreceptor for adenosine diphosphate (ADP). This P2Y receptor family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. The P2Y12 receptor is involved in platelet aggregation and is thus a biological target for the treatment of thromboembolisms and other clotting disorders. Two transcript variants encoding the same isoform have been identified for this gene.

# Clinical significance
The drugs clopidogrel (Plavix), prasugrel (Efient, Effient), ticagrelor (Brilinta), and cangrelor (Kengreal) bind to this receptor and are marketed as antiplatelet agents.
P2Y12 inhibitors do not change the risk of death when given as a pretreatment prior to routine percutaneous coronary intervention (PCI) in people who have had a non-ST-elevation myocardial infarction (NSTEMI). Though, a P2Y12 inhibitor in addition to aspirin should be administered for up to 12 months to most patients with non-ST-elevation acute coronary syndrome. They do however increase the risk of bleeding and decrease the risk of further cardiovascular problems. Thus their routine use in this context is of questionable value.
In patients undergoing primary PCI for an ST-segment elevation myocardial infarction (STEMI), a P2Y12 inhibitor should be administered as soon as possible. The use of clopidogrel in particular has been shown to improve morbidity and mortality endpoints including cardiovascular death, recurrent MI, and stroke at 30 days after PCI.
P2RY8
P2Y purinoceptor 8 is a protein that in humans is encoded by the P2RY8 gene.

# Function
The protein encoded by this gene belongs to the family of G-protein coupled receptors, that are preferentially activated by adenosine and uridine nucleotides. This gene is moderately expressed in undifferentiated HL60 cells, and is located on both chromosomes X and Y.

# Clinical relevance
Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.
PA2G4
Proliferation-associated protein 2G4 (PA2G4) also known as ErbB3-binding protein 1 (EBP1) is a protein that in humans is encoded by the PA2G4 gene.

# Function
This gene encodes an RNA-binding protein that is involved in growth regulation. This protein is present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. This protein can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. This protein is also a transcriptional corepressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. This protein has been implicated in growth inhibition and the induction of differentiation of human cancer cells. Paradoxically, the expression of EBP1 is decreased in prostate cancer , but increased in Acute Myelogneous Leukemia. Six pseudogenes, located on chromosomes 3, 6, 9, 18, 20 and X, have been identified.

# Interactions
PA2G4 has been shown to interact with ERBB3, retinoblastoma protein, and androgen receptor.
PACS1
Phosphofurin acidic cluster sorting protein 1, also known as PACS-1, is a protein that in humans is encoded by the PACS1 gene.

# Function
The PACS-1 protein has a putative role in the localization of trans-Golgi network (TGN) membrane proteins. Mouse and rat homologs have been identified and studies of the homologous rat protein indicate a role in directing TGN localization of furin by binding to the protease's phosphorylated cytosolic domain. In addition, the human protein plays a role in HIV-1 Nef-mediated downregulation of cell surface MHC-I molecules to the TGN, thereby enabling HIV-1 to escape immune surveillance.

# Interactions
PACS1 has been shown to interact with Furin.

# Clinical significance
A de novo mutation c.607C>T in the PACS1 gene has been shown to result in a syndromic phenotype (colloquially called PACS1 Syndrome) that is characterized by global developmental delay, intellectual disability, and specific facial features.

## Prevalence and diagnosis
The first two cases were identified in early 2011 by doctors in the Netherlands. As of late 2014, there were 20 cases identified worldwide.
Diagnosis is typically done using full genome or exome sequencing.  There are likely several more cases that will eventually be reported as knowledge of the mutation spreads and testing becomes more accessible.

## Observed and reported traits
Individuals with the mutation have been reported to have similar facial features, such as:
- Widely spaced eyes and low-set ears
- Down-slanting eye corners and mild uni-brow
- Highly arched eyebrows and long eyelashes
- Rounded button nose with a flat bridge
- Wide mouth with down-turned corners
- Thin upper lip and widely spaced teeth
Other common traits reported by care givers of affected individuals are:
- Low muscle tone
- Seizures
- Repetitive self-stimulatory behavior
- Sensory processing disorder
- Delayed development of gross motor skills and fine motor skills
- Delayed cognitive development
- Chewing and swallowing difficulties
- Digestion or bowel problems
- Slow growth resulting in below average height and weight

## Prognosis and treatment
In combination, these traits affect walking, talking, feeding, and learning skills. No impact on life expectancy has been found. As with many developmental disabilities, there is no "cure".
In order to improve quality of life and enhance life skills of affected individuals, care givers have found a number of tools and strategies. It is important to note that all of these may not be applicable to a particular individual, and reported effectiveness has varied. It is recommended to consult with a physician prior to initiating any form of treatment.
- physiotherapy (PT)
- occupational therapy (OT)
- speech therapy (including augmentative and alternative communication) (SPT)
- behavioural therapy (applied behavior analysis/intensive behavioural intervention etc.)
- discrete trial teaching
- early intervention programs
- massage therapy and pediatric massage
- feeding therapy
- music therapy
- hippotherapy
- hydrotherapy
PADI2
Protein-arginine deiminase type-2 is an enzyme that in humans is encoded by the PADI2 gene.
This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages.
This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes.