Persius/hicric huggingface dataset:
Helix-turn-helix transcription factors
In proteins, the helix-turn-helix (HTH) is a major structural motif capable of binding DNA. Each monomer incorporates two  helices, joined by a short strand of amino acids, that bind to the major groove of DNA. The HTH motif occurs in many proteins that regulate gene expression.

# Discovery
The discovery of the helix-turn-helix motif was based on similarities between several genes encoding transcription regulatory proteins from bacteriophage lambda and Escherichia coli: Cro, CAP, and  repressor, which were found to share a common 2025 amino acid sequence that facilitates DNA recognition.

# Function
The helix-turn-helix motif is a DNA-binding motif. The recognition and binding to DNA by helix-turn-helix proteins is done by the two  helices, one occupying the N-terminal end of the motif, the other at the C-terminus. In most cases, such as in the Cro repressor, the second helix contributes most to DNA recognition, and hence it is often called the "recognition helix". It binds to the major groove of DNA through a series of hydrogen bonds and various Van der Waals interactions with exposed bases. The other  helix stabilizes the interaction between protein and DNA, but does not play a particularly strong role in its recognition. The recognition helix and its preceding helix always have the same relative orientation.

# Classification of helix-turn-helix motifs
Several attempts have been made to classify the helix-turn-helix motifs based on their structure and the spatial arrangement of their helices. Some of the main types are described below.

## Di-helical
The di-helical helix-turn-helix motif is the simplest helix-turn-helix motif. A fragment of Engrailed homeodomain encompassing only the two helices and the turn was found to be an ultrafast independently folding protein domain.

## Tri-helical
An example of this motif is found in the transcriptional activator Myb.

## Tetra-helical
The tetra-helical helix-turn-helix motif has an additional C-terminal helix compared to the tri-helical motifs. These include the LuxR-type DNA-binding HTH domain found in bacterial transcription factors and the helix-turn-helix motif found in the TetR repressors. Multihelical versions with additional helices also occur.

## Winged helix-turn-helix
The winged helix-turn-helix (wHTH) motif is formed by a 3-helical bundle and a 3- or 4-strand beta-sheet (wing). The topology of helices and strands in the wHTH motifs may vary. In the transcription factor ETS wHTH folds into a helix-turn-helix motif on a four-stranded anti-parallel beta-sheet scaffold arranged in the order 1-1-2-2-3-3-4 where the third helix is the DNA recognition helix.

## Other modified helix-turn-helix motifs
Other derivatives of the helix-turn-helix motif include the DNA-binding domain found in MarR, a regulator of multiple antibiotic resistance, which forms a winged helix-turn-helix with an additional C-terminal alpha helix.
How to add WikiDoc Contributions to CV

# Copying Web Address
- Authors can copy the web address of the page that has been created/edited and use it as a reference.
- Clicking on the link of the web address will lead the reader to the page where edits have been made.
- The image given below can serve as an example:

# Adding to Your CV
- Use the following format:
- Doe, J. Contribution to: Bronchiolitis medical therapy. In WikiDoc. 26 January 2016.  Contribution isolated at 
- You can obtain the web address of your contribution isolated in the WikiDoc history by clicking "View history" on the web page you edited and selecting one or more adjacent entries to view.
- The image given below can serve as an example:

# Adding to Electronic Residency Application Service (ERAS)
- If you plan to apply to a medical residency or fellowship program, the MyERAS website has the following publication type that can include WikiDoc edits: "Non Peer Reviewed Online Publication".
- The image given below can serve as a guide:

# Keeping Track of Your Activity
- Authors can keep track of their activity and, if needed, can also quote their contribution.
- Portals which enable the authors to do so are enlisted below:

## 1. Total Edit Count
- To check the count of total edits made by any author, click here.
- The image below can serve as a guide:

## 2. Active Users List
- This list shows the activity of users within the last 30 days.
- To view the list, click here.
How to create a critical pathways page

# Overview
This section  provides a step-by-step guide on how to create a critical pathways page.  It starts by choosing a topic of interest from the resident survival guide page and simply following the instructions below.  It is very easy, you can do it.

# How to create critical pathways

## Select a Topic
A topic of interest is selected from the resident survival guide page and a name is assigned next to it.  Below is a picture of what a critical pathways page looks like.  Click here to select a topic.

## Next Steps
- Use the algorithm in the resident survival guide of the selected topic as reference.  Click on the resident survival guide icon at the top right corner of the page to view the algorithm.
- Use the first branch point on the algorithm as a guide for constructing the first question.
- Provide answers to the question.  There could be two or more answers to this question.
- Link provided answers to corresponding pages on WikiDoc.  Click here to learn how to create links.
- Give Definitions and Action Items for the first question.
- Please add references to the definitions when necessary.  Click here to learn how to add references.
- Use the second branch point after each answer as a reference for the second question.
- Repeat steps 2, 3, and 4.
- After completing the critical pathways page, please add the critical pathways icon to the Main Page of the topic you worked on.
For example, if you are working on hyperkalemia critical pathways, you need to put a link to it on the hyperkalemia page through the critical pathways icon:
You type: ]
You get:

# Definitions
The definition of the answers must be provided and referenced when possible.  For example:
Metabolic acidosis is a state in which the blood pH is less than 7.35 due to increased production of H+ by the body or the inability of the body to form bicarbonate (HCO3-) in the kidney.
Anion gap =  -  - 
Normal reference range for anion gap is between 8 and 16 meq/L.

# Action Items
- This involves determining the next step to take in the patient management.  For example:  Should I check for respiratory compensation in the case of metabolic acidosis or not?  Should I administer bicarbonate or not?
Hypercholesterolemia secondary targets

# The Metabolic Syndrome
The metabolic syndrome is identified as a secondary target of therapy in the NCEP ATP III guidelines, beyond LDL cholesterol. The metabolic syndrome is a constellation of multiple risk factors which are lipid and non-lipid in origin. The basic metabolic abnormality associated with the metabolic syndrome is insulin resistance. Two main factors are responsible for the development of insulin resistance which include abdominal obesity and physical inactivity. The definition of the metabolic syndrome includes:

# Management
The management of the metabolic syndrome is multifold. It is considered as a secondary target for therapy after the LDL goal has been achieved. It mainly includes 3 main components:

## Reducing Weight
Obesity is a major underlying risk factors for CHD.  After the LDL goal has been achieved, targeted interventions towards weight reduction should be designed for each individual. This will help in reducing the LDL and reduce other risk factors associated with the metabolic syndrome.

## Increasing Physical activity
Sedentary lifestyle and physical inactivity are major risk factors for CHD.  Regular physical activity raises HDL, reduces VLDL and may also lower LDL levels.  It also helps in improving cardiovascular fitness and insulin resistance and should be a part of the regimen of each patients on LDL lowering therapy.

## Reducing other Components of Metabolic Syndrome
In addition to the 2 main underlying risk factors (obesity and physical inactivity), it is important to modify the individual components of the metabolic syndrome. This would include better control of hypertension, use of aspirin for primary prevention to reduce the prothrombotic state), better control of diabetes and impaired glucose tolerance and treatment of elevated triglycerides and low HDL.
Interleukin 15 receptor, alpha subunit
Interleukin 15 receptor, alpha subunit is a subunit of the interleukin 15 receptor that in humans is encoded by the IL15RA gene.

# Structure
The IL-15 receptor is composed of three subunits: IL-15R alpha, CD122, and CD132.  Two of these subunits, CD122 and CD132, are shared with the receptor for IL-2, but IL-2 receptor has an additional subunit (CD25).  The shared subunits contain the cytoplasmic motifs required for signal transduction, and this forms the basis of many overlapping biological activities of IL15 and IL2, although in vivo the two cytokines have separate biological effects.  This may be due to effects of the respective alpha chains, which are unique to each receptor, the kinetics and affinity of cytokine-cytokine receptor binding, or due to the availability and concentration of each cytokine.

# Function
IL-15Ralpha specifically binds IL15 with very high affinity, and is capable of binding IL-15 independently of other subunits.  It is suggested that this property allows IL-15 to be produced by one cell, endocytosed by another cell, and then presented to a third party cell.
This receptor is reported to enhance cell proliferation and expression of apoptosis inhibitor BCL2L1/BCL2-XL and BCL2. Multiple alternatively spliced transcript variants of this gene have been reported. The full length sequences of only two variants encoding distinct isoforms are available.

# Isoforms
Several isoforms of the IL-15Ralpha protein have been detected. These isoforms can either result from alternative splicing of the mRNA encoding for the receptor or by shedding of the extra cellular domain of the receptor protein.
Imipenem cilastatin directions for use

# Directions for Use
For IV Use Only.
To Open Diluent Container:
Peel overwrap from the corner and remove container. Some opacity of the plastic due to moisture absorption during the sterilization process may be observed. This is normal and does not affect the solution quality or safety. The opacity will diminish gradually.
To Assemble Vial and Flexible Diluent Container:
(Use Aseptic Technique)
1.Remove the protective covers from the top of the vial and the vial port on the diluent container as follows:
a.To remove the breakaway vial cap, swing the pull ring over the top of the vial and pull down far enough to start the opening. (SEE FIGURE 1.) Pull the ring approximately half way around the cap and then pull straight up to remove the cap. (SEE FIGURE 2.) NOTE: DO NOT ACCESS VIAL WITH SYRINGE.
b.To remove the vial port cover, grasp the tab on the pull ring, pull up to break the three tie strings, then pull back to remove the cover. (SEE FIGURE 3.)
2.Screw the vial into the vial port until it will go no further. THE VIAL MUST BE SCREWED IN TIGHTLY TO ASSURE A SEAL. This occurs approximately 12 turn (180) after the first audible click. (SEE FIGURE 4.) The clicking sound does not assure a seal; the vial must be turned as far as it will go. NOTE: Once vial is seated, do not attempt to remove. (SEE FIGURE 4.)
3.Recheck the vial to assure that it is tight by trying to turn it further in the direction of assembly.
4.Label appropriately.
To Prepare Admixture:
1.Squeeze the bottom of the diluent container gently to inflate the portion of the container surrounding the end of the drug vial.
2.With the other hand, push the drug vial down into the container telescoping the walls of the container. Grasp the inner cap of the vial through the walls of the container. (SEE FIGURE 5.)
3.Pull the inner cap from the drug vial. (SEE FIGURE 6.) Verify that the rubber stopper has been pulled out, allowing the drug and diluent to mix.
4.Mix container contents thoroughly and use within the specified time.
Preparation for Administration:
(Use Aseptic Technique)
1.Confirm the activation and admixture of vial contents.
2.Check for leaks by squeezing container firmly. If leaks are found, discard unit as sterility may be impaired.
3.Close flow control clamp of administration set.
4.Remove cover from outlet port at bottom of container.
5.Insert piercing pin of administration set into port with a twisting motion until the pin is firmly seated. NOTE: See full directions on administration set carton.
6.Lift the free end of the hanger loop on the bottom of the vial, breaking the two tie strings. Bend the loop outward to lock it in the upright position, then suspend container from hanger.
7.Squeeze and release drip chamber to establish proper fluid level in chamber.
8.Open flow control clamp and clear air from set. Close clamp.
9.Attach set to venipuncture device. If device is not indwelling, prime and make venipuncture.
10.Regulate rate of administration with flow control clamp.
WARNING: Do not use flexible container in series connections.
Imperforate anus (patient information)
For the WikiDoc page for this topic, click here

# Overview
Imperforate anus is a birth defect that affects about one of every 5,000 newborns, and is somewhat more common among boys than girls. It is a congenital defect in which the opening to the anus is missing or blocked. The disorder may occur alone or together with other abnormalities of the rectum. The cause is unknown. The baby can be diagnosed by doctor's physical exam or images such as x-ray, CT and MRI. Surgery to reconstructe the anus is the effective treatment. With treatment, many children with imperforate anus go well.

# How do I know if my baby has imperforate anus and what are the symptoms of imperforate anus?
- Anal opening very near the vaginal opening in girls
- Missing or misplaced opening to the anus
- No passage of first stool within 24 - 48 hours after birth
- Stool passes out of the vagina, base of penis, scrotum, or urethra
- Swollen belly area

# Who is at risk for imperforate anus?
The cause of imperforate anus is not clear. Many forms of imperforate anus are associated with other birth defects. It is a relatively common condition that occurs in about 1 out of 5,000 infants.

# How to know your baby has imperforate anus?
- Physical exam: A doctor can diagnose this condition during a physical exam. A fistula, an abnormal connection or opening between the intestine and bladder, suggest the existence imperforate anus. And, if stool is excreted through the urine or from the vagina, imperforate anus would be suspected.
- Images: Images such as x-ray, ultrasound. CT, or MRI may be recommended to diagnose children with any form of anorectal malformation.

# When to seek urgent medical care?
This disorder is usually discovered when the newborn infant is first examined. Call your baby's health care provider if the child that was treated for imperforate anus has abdominal pain or fails to develop any bowel control by the age of 3.

# Treatment options
Surgery to reconstructe the anus is needed. At the same time, the infant should be checked for other defects, especially those affecting the genitals, urinary tract, and spine.

# Where to find medical care for imperforate anus?
Directions to Hospitals Treating imperforate anus

# Prevention of imperforate anus
As the cause is not clear, the prevention of imperforate anus is unknown.

# What to expect (Outlook/Prognosis)?
With treatment, the outcome of imperforate anus is usually good. The prognosis depends on primary fecal continence.

# Copyleft Sources
Interleukin 10 receptor, alpha subunit
Interleukin 10 receptor, alpha subunit is a subunit for the interleukin-10 receptor. IL10RA, is its human gene.
IL10RA has also recently been designated CDW210A (cluster of differentiation W210A).

# Function
The protein encoded by this gene is a receptor for interleukin 10. This protein is structurally related to interferon receptors. It has been shown to mediate the immunosuppressive signal of interleukin 10, and thus inhibits the synthesis of proinflammatory cytokines. This receptor is reported to promote survival of progenitor myeloid cells through the insulin receptor substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor leads to tyrosine phosphorylation of JAK1 and TYK2 kinases.

# Interactions
Interleukin 10 receptor, alpha subunit has been shown to interact with:
- Interleukin 10  and
- Janus kinase 1.
Interleukin 27 receptor, alpha subunit
Interleukin 27 receptor, alpha is a subunit of the interleukin-27 receptor. IL27RA is its human gene.

# Function
In mice, CD4+ helper T-cells differentiate into type 1 (Th1) cells, which are critical for cell-mediated immunity, predominantly under the influence of IL12. Also, IL4 influences their differentiation into type 2 (Th2) cells, which are critical for most antibody responses. Mice deficient in these cytokines, their receptors, or associated transcription factors have impaired, but are not absent of, Th1 or Th2 immune responses. This gene encodes a protein which is similar to the mouse T-cell cytokine receptor Tccr at the amino acid level, and is predicted to be a glycosylated transmembrane protein.

# Interactions
Interleukin 27 receptor, alpha subunit has been shown to interact with STAT1.
International Narcotics Control Caucus
The United States Senate Caucus on International Narcotics Control (also known as the Senate Narcotics Caucus) was created to monitor and encourage the U.S. government and private programs seeking to expand international cooperation against drug abuse and narcotics trafficking, and promote international compliance with narcotics control treaties, including eradication.
As a formal organization of the Senate, the Caucus has the status of a standing committee. It has subpoena power and is authorized to take testimony of witnesses and to produce books, records, papers, and documents that it deems necessary. In the past it has dealt with international cooperation, eradication, trafficking, interdiction, border control, drug strategies, assessments of Federal programs, and money laundering issues.
The Caucus has held numerous hearings over the years and has issued a number of reports on U.S. narcotics control policy. The primary responsibilities of the I.N.C.C. have involved monitoring of compliance with international narcotics control treaties and agreements, and oversight of U.S. counter narcotics policy and activities.

# Establishment
The United States Senate Caucus on International Narcotics Control was originally called the United States Commission on International Narcotics Control, when it was established on August 16, 1985 by the Foreign Relations Authorization Act for fiscal 1986 and 1987.
Pursuant to the Legislative Branch Appropriations Act of 1986 (Template:USPL), the name of the Commission was changed to the United States Senate Caucus on International Narcotics Control, effective November 13, 1985. (The House had requested the name change because it would more accurately reflect the membership of the group, given that no House Members were to be appointed to it.)

# Membership
The group's authorizing legislation (Template:USPL) provided that the Commission draw its membership from the Senate and from experts in the private sector.  Specifically, the group was to be composed of 12 members, seven Members of the U.S. Senate appointed by the President of the Senate, and five members from the private sector appointed by the President of the United States.  Four of the seven Senators, including one designated as Chairman, were to be selected from the majority party after consultation with the Majority Leader, and three, including the Member designated as Co-Chairman, were to be selected from the minority party, after consultation with the Minority Leader.  The five Commission members selected from the private sector were to be appointed by the President after consultation with the Members of the appropriate congressional committees.
The appointment of private citizens was discontinued after 1987 in accordance with the group's redesignation as the U.S. Senate Caucus on International Narcotics Control.

# Current Members of Narcotics Caucus
- Joe Biden (D-DE) Chairman
- Charles Grassley (R-IA) Co-Chairman
- Jeff Sessions (R-AL)
- Dianne Feinstein (D-CA)
- Norm Coleman (R-MN)
John Curtin School of Medical Research
The John Curtin School of Medical Research (JCMSR) is a major biomedial research centre in Australia, based at the Australian National University, Canberra. The school was founded in 1948, as a result of the vision of Australian Nobel Laureate Sir Howard Florey and Prime Minister John Curtin.
The Nobel Prize-winning Peter Doherty conducted his award-winning research here, discovering the way T cells interact with the Major Histocompatibility Complex (MHC) in antigen recognition.
Movie star Jackie Chan has made donations to the School, with the Director in 2006 announcing the Jackie Chan Science Centre will be named after him.
Juvenile idiopathic arthritis overview

# Overview
Juvenile idiopathic arthritis (JIA), formerly known as juvenile rheumatoid arthritis (JRA), is the most common form of persistent arthritis in children.
JIA is sometimes referred to as juvenile chronic arthritis (JCA), a term that is not precise as JIA does not encompass all forms of chronic childhood arthritis.
Arthritis is the inflammation of the synovium (the lining tissues) of a joint.
JIA is a subset of arthritis seen in childhood, which may be transient and self-limited or chronic.  It differs significantly from arthritis commonly seen in adults (osteoarthritis, rheumatoid arthritis), and other types of arthritis that can present in childhood which are chronic conditions (e.g. psoriatic arthritis and ankylosing spondylitis).
Lamivudine zidovudine clinical studies

# Clinical Studies
There have been no clinical trials conducted with COMBIVIR. See Clinical Pharmacology (12.3) for information about bioequivalence. One COMBIVIR Tablet given twice daily is an alternative regimen to EPIVIR Tablets 150 mg twice daily plus RETROVIR 600 mg per day in divided doses.

## Adults
Lamivudine Plus Zidovudine: The NUCB3007 (CAESAR) study was conducted using EPIVIR 150-mg Tablets (150 mg twice daily) and RETROVIR 100-mg Capsules (2 x 100 mg 3 times daily). CAESAR was a multi-center, double-blind, placebo-controlled study comparing continued current therapy (zidovudine alone  or zidovudine with didanosine or zalcitabine ) to the addition of EPIVIR or EPIVIR plus an investigational non-nucleoside reverse transcriptase inhibitor, randomized 1:2:1. A total of 1,816 HIV-1-infected adults with 25 to 250 (median 122) CD4 cells/mm3 at baseline were enrolled: median age was 36 years, 87% were male, 84% were nucleoside-experienced, and 16% were therapy-naive. The median duration on study was 12 months. Results are summarized in Table 5.

## Prevention of Maternal-Fetal HIV-1 Transmission
The utility of zidovudine alone for the prevention of maternal-fetal HIV-1 transmission was demonstrated in a randomized, double-blind, placebo-controlled trial conducted in HIV-1-infected pregnant women with CD4+ cell counts of 200 to 1,818 cells/mm3 (median in the treated group: 560 cells/mm3) who had little or no previous exposure to zidovudine. Oral zidovudine was initiated between 14 and 34 weeks of gestation (median 11 weeks of therapy) followed by IV administration of zidovudine during labor and delivery. Following birth, neonates received oral zidovudine syrup for 6 weeks. The study showed a statistically significant difference in the incidence of HIV-1 infection in the neonates (based on viral culture from peripheral blood) between the group receiving zidovudine and the group receiving placebo. Of 363 neonates evaluated in the study, the estimated risk of HIV-1 infection was 7.8% in the group receiving zidovudine and 24.9% in the placebo group, a relative reduction in transmission risk of 68.7%. Zidovudine was well tolerated by mothers and infants. There was no difference in pregnancy-related adverse events between the treatment groups.