Persius/hicric huggingface dataset:
Acanthosis nigricans (patient information)
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# Overview
Acanthosis nigricans is a skin disorder in which there is darker, thick, velvety skin in body folds and creases.

# What are the symptoms of Acanthosis nigricans?
Acanthosis nigricans usually appears slowly and doesn't cause any symptoms other than skin changes.
Eventually, dark, velvety skin with very visible markings and creases appears in the armpits, groin and neck folds, and over the joints of the fingers and toes.
Less commonly, the lips, palms, soles of the feet, or other areas may be affected. These symptoms are more common in people with cancer.

# What causes Acanthosis nigricans?
Obesity can lead to acanthosis nigricans, as can some endocrine disorders. It is often found in people with obesity-related diabetes.
Some drugs, particularly hormones such as human growth hormone or oral contraceptives ("the pill"), can also cause acanthosis nigricans.
People with lymphoma or cancers of the gastrointestinal or genitourinary tracts can also develop severe cases of acanthosis nigricans.

# Who is at highest risk?
Acanthosis nigricans can affect otherwise healthy people, or it can be related to medical problems. Some cases are genetically inherited. The condition is most commonly seen among people of African descent, in part because it is easier to see in darker skin.

# Diagnosis
Your health care provider can usually diagnose acanthosis nigricans by looking at your skin. A skin biopsy may be needed in unusual cases.
If there is no clear cause of acanthosis nigricans, you may need to have tests. Your health care provider may order blood tests, an endoscopy, or x-rays to rule out diabetes or cancer as the cause.

# When to seek urgent medical care?
Call your health care provider if you develop areas of thick, dark, velvety skin.

# Treatment options
Because acanthosis nigricans usually only changes the skin's appearance, no treatment is needed.
It is important, however, to treat any underlying medical problem that may be causing these skin changes. When acanthosis nigricans is related to obesity, losing weight often improves the condition.

# Where to find medical care for Acanthosis nigricans?
Directions to Hospitals Treating Acanthosis nigricans

# What to expect (Outlook/Prognosis)?
Acanthosis nigricans often fades if the cause can be found and treated.

# Sources
Acute coronary syndrome initial management

# Initial Management

# 2021 ACC/AHA/SCAI Guideline for Coronary Artery Revascularization. (Please do not edit).

## Use of Coronary Physiology to Guide Revascularization With PCI

## Intravascular Ultrasound to Assess Lesion Severity

## 2014 AHA/ACC/HRS Guideline for the Management of Patients With Atrial Fibrillation (DO NOT EDIT)

### AF Complicating Acute Coronary Syndrome

## ACC / AHA 2011 Guidelines - Acute Coronary Syndrome - Initial Management (DO NOT EDIT) 

# See Also
- The UA / NSTEMI Living Guidelines: Vote on current recommendations and suggest revisions to the guidelines

# Sources
- 2011 ACCF/AHA Focused Update Incorporated Into the ACC/AHA 2007 Guidelines for the Management of Patients With Unstable Angina/Non-ST-Elevation Myocardial Infarction: A Report of the American College of Cardiology Foundation/American Heart Association Task Force on Practice Guidelines
- The ACC/AHA 2007 Guidelines for the Management of Patients With Unstable Angina/Non-ST-Elevation Myocardial Infarction
Acyl-CoA:lysocardiolipin acyltransferase-1
Acyl-CoA:lysocardiolipin acyltransferase-1 (ALCAT1) is a polyglycerophospholipid acyltransferase of the endoplasmic reticulum which is primarily known for catalyzing the acylation of monolysocardiolipin back into cardiolipin, although it does catalyze the acylation of other polyglycerophospholipids.
ALCAT1 is widely distributed throughout the body, with the highest concentrations being in the heart and liver.

# Function
ALCAT1 facilitates the transfer of acyl groups from linoleoyl-CoA and oleoyl-CoA onto monolysocardiolipin and dilysocardiolipin. The pathway is thought to be important in maintaining heart function, as the ALCAT1 gene is conserved among many species of vertebrates, but not in organisms lacking heart atria.
Recent research has shown that ALCAT1 activity is involved with mitochondrial dysfunction in disease. ALCAT1 is upregulated by oxidative stress and diet-induced obesity, and produces a species of cardiolipin that is highly sensitive to oxidative damage. Deficiency of ALCAT1 prevented the onset of diet-induced obesity, improved mitochondria function, and prevented insulin resistance.

# Interactions
ALCAT1 was reported to be regulated by thyroid hormone, a universal regulator of metabolism. Its activity also appeared to be inhibited by the presence of ADP and ATP, but not its analogs or other nucleotides, such as UTP and GTP.
Adaptor-related protein complex 2, alpha 1
AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene.
This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles. The AP-2 complex is a heterotetramer consisting of two large adaptins (alpha or beta), a medium adaptin (mu), and a small adaptin (sigma). The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in vesicles. Alternative splicing of this gene results in two transcript variants encoding two different isoforms. A third transcript variant has been described, but its full length nature has not been determined.

# Interactions
Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB.
American Board of Psychiatry and Neurology

# Overview
The American Board of Psychiatry and Neurology, Inc. (ABPN) sets the standards for training and certifying psychiatrists and neurologists in the United States, with the self-stated aim of promoting excellence in practice through its certification process. The ABPN is one of 24 member boards of the American Board of Medical Specialties (ABMS).
Psychiatrists and neurologists who have passed the requisite training may take examinations to become board-certified by ABPN. As of 1994, physicians attaining ABPN Board certification are issued ten-year, time-limited certificates.

# History
The American Board of Psychiatry and Neurology, a non-profit organization, was founded in 1934 by a committee of individuals drawn from the American Psychiatric Association, the American Neurological Association, and the American Medical Association. A notable founder was Walter Freeman, known as an enthusiastic advocate and practitioner of the lobotomy, who was also president from 1946 to 1948.

# Organization
The 2007 President of the ABPN Board of Directors is Michael V. Johnston, MD of Baltimore, Maryland. The Board of Directors is independently incorporated and has sixteen voting members; nominees are proposed by the American College of Psychiatrists, American Psychiatric Association, American Medical Association, American Neurological Association and the American Academy of Neurology, and selected by the Board.
ABPN reports that it certifies around 1000 psychiatrists and 500 neurologists per year.

# Examination Process
The ABPN examination includes a Part 1 computer-administered written test and a Part II oral examination involving an actual patient interview as well as clinical vignettes (video clips of former patients), followed by focused questioning from examiners and evaluation by numerical score.

# Related Chapters
- Royal College of Physicians and Surgeons of Canada
- Royal College of Psychiatrists
Amphotericin B liposomal drug interactions

# Drug-Laboratory Interactions
- Serum phosphate false elevation
False elevations of serum phosphate may occur when samples from patients receiving AmBisome are analyzed using the PHOSm assay (e.g. used in Beckman Coulter analyzers including the Synchron LX20). This assay is intended for the quantitative determination of inorganic phosphorus in human serum, plasma or urine samples.

# Drug Interactions
No formal clinical studies of drug interactions have been conducted with AmBisome. However, the following drugs are known to interact with amphotericin B and may interact with AmBisome:
- Antineoplastic Agents
Concurrent use of antineoplastic agents may enhance the potential for renal toxicity, bronchospasm, and hypotension. Antineoplastic agents should be given concomitantly with caution.
- Corticosteroids and Corticotropin (ACTH)
Concurrent use of corticosteroids and ACTH may potentiate hypokalemia which could predispose the patient to cardiac dysfunction. If used concomitantly, serum electrolytes and cardiac function should be closely monitored.
- Digitalis Glycosides
Concurrent use may induce hypokalemia and may potentiate digitalis toxicity. When administered concomitantly, serum potassium levels should be closely monitored.
- Flucytosine
Concurrent use of flucytosine may increase the toxicity of flucytosine by possibly increasing its cellular uptake and/or impairing its renal excretion.
- Azoles (e.g. ketoconazole, miconazole, clotrimazole, fluconazole, etc.)
In vitro and in vivo animal studies of the combination of amphotericin B and imidazoles suggest that imidazoles may induce fungal resistance to amphotericin B. Combination therapy should be administered with caution, especially in immunocompromised patients.
- Leukocyte Transfusions
Acute pulmonary toxicity has been reported in patients simultaneously receiving intravenous amphotericin B and leukocyte transfusions.
- Other Nephrotoxic Medications
Concurrent use of amphotericin B and other nephrotoxic medications may enhance the potential for drug-induced renal toxicity. Intensive monitoring of renal function is recommended in patients requiring any combination of nephrotoxic medications.
- Skeletal Muscle Relaxants
Amphotericin B-induced hypokalemia may enhance the curariform effect of skeletal muscle relaxants (e.g. tubocurarine) due to hypokalemia. When administered concomitantly, serum potassium levels should be closely monitored.
Ampicillin sulbactam clinical pharmacology

# Clinical Pharmacology
Immediately after completion of a 15-minute intravenous infusion, peak serum concentrations of ampicillin and sulbactam are attained. Ampicillin serum levels are similar to those produced by the administration of equivalent amounts of ampicillin alone. Peak ampicillin serum levels ranging from 109 to 150 mcg/mL are attained after administration of 2000 mg of ampicillin plus 1000 mg sulbactam and 40 to 71 mcg/mL after administration of 1000 mg ampicillin plus 500 mg sulbactam. The corresponding mean peak serum levels for sulbactam range from 48 to 88 mcg/mL and 21 to 40 mcg/mL, respectively. After an intramuscular injection of 1000 mg ampicillin plus 500 mg sulbactam, peak ampicillin serum levels ranging from 8 to 37 mcg/mL and peak sulbactam serum levels ranging from 6 to 24 mcg/mL are attained. The mean serum half-life of both drugs is approximately 1 hour in healthy volunteers. Approximately 75 to 85% of both ampicillin and sulbactam are excreted unchanged in the urine during the first 8 hours after administration to individuals with normal renal function. Somewhat higher and more prolonged serum levels of ampicillin and sulbactam can be achieved with the concurrent administration of probenecid.
In patients with impaired renal function the elimination kinetics of ampicillin and sulbactam are similarly affected, hence the ratio of one to the other will remain constant whatever the renal function. The dose in such patients should be administered less frequently in accordance with the usual practice for ampicillin. Ampicillin has been found to be approximately 28% reversibly bound to human serum protein and sulbactam approximately 38% reversibly bound.
Penetration of both ampicillin and sulbactam into cerebrospinal fluid in the presence of inflamed meninges has been demonstrated after IV administration of ampicillin/sulbactam. The pharmacokinetics of ampicillin and sulbactam in pediatric patients receiving ampicillin/sulbactam are similar to those observed in adults. Immediately after a 15-minute infusion of 50 to 75 mg ampicillin/sulbactam per kg body weight, peak serum and plasma concentrations of 82 to 446 mcg ampicillin/mL and 44 to 203 mcg sulbactam/mL were obtained. Mean half-life values were approximately 1 hour.
Ampicillin sulbactam indications and usage

# Indications and Usage
UNASYN is indicated for the treatment of infections due to susceptible strains of the designated microorganisms in the conditions listed below.
- Acinetobacter calcoaceticus*
- Bacteroides fragilis*
- Enterobacter spp.*
- Escherichia coli*
- Klebsiella spp.- (including K. pneumoniae*)
- Proteus mirabilis*
- Staphylococcus aureus
- Bacteroides species, including B. fragilis
- Enterobacter spp.*
- Escherichia coli*
- Klebsiella spp.- (including K. pneumoniae*)
- Bacteroides species, including B. fragilis
- Escherichia coli*
- Efficacy for this organism in this organ system was studied in fewer than 10 infections.
While UNASYN is indicated only for the conditions listed above, infections caused by ampicillin-susceptible organisms are also amenable to treatment with UNASYN due to its ampicillin content. Therefore, mixed infections caused by ampicillin-susceptible organisms and beta-lactamase producing organisms susceptible to UNASYN should not require the addition of another antibiotic. Appropriate culture and susceptibility tests should be performed before treatment in order to isolate and identify the organisms causing infection and to determine their susceptibility to UNASYN. Therapy may be instituted prior to obtaining the results from bacteriological and susceptibility studies when there is reason to believe the infection may involve any of the beta-lactamase producing organisms listed above in the indicated organ systems. Once the results are known, therapy should be adjusted if appropriate. To reduce the development of drug-resistant bacteria and maintain effectiveness of UNASYN and other antibacterial drugs, UNASYN should be used only to treat or prevent infections that are proven or strongly suspected to be caused by susceptible bacteria. When culture and susceptibility information are available, they should be considered in selecting or modifying antibacterial therapy. In the absence of such data, local epidemiology and susceptibility patterns may contribute to the empiric selection of therapy.
Aortic insufficiency surgery complications
For the WikiPatient page for this topic, click here; For the main page of aortic insufficiency, click here
Related Key Words and Synonyms: Aortic valve replacement.

# Aortic Insufficiency Surgery Complications
Risks of any surgery
Some Complications associated with any surgical procedure include:
- Pulmonary embolism where blood clots in the legs travel to the lungs
- Blood loss
- Breathing problems
- Infection, including in the lungs, kidneys, bladder, chest, or heart valves
- Reactions to medicines
- Nausea and vomiting
- Abnormal or painful scar formation
- Allergic skin reaction
Possible risks from having open-heart surgery
There are many risks associated with open heart surgery.The postoperative risk factors can be related to various factors including albumin, TLC and BMI. Other possible complications after an  heart surgery include:
- Heart attack or stroke
- Heart rhythm problems; such as atrial fibrillation
- Infection at the site of the incision cut, which is more likely to happen in people who are obese, have diabetes, women, or have already had this surgery
- Memory loss and loss of mental clarity, or "fuzzy thinking" or pump head
- Post-pericardiotomy syndrome, which presents as a low-grade fever and chest pain. This could last for up to 6 months
Prosthetic heart valves are associated with a variety of complications
The complications associated with prosthetic heart valves include:
- Structural deterioration, particularly with bioprosthetic valves
- Valve obstruction due to thrombosis or pannus formation
- Systemic embolization
- Bleeding
- Endocarditis and other infections
- Left ventricular systolic dysfunction, which may be preexisting (Heart failure)
- Hemolytic anemia
Birthmarks-pigmented (patient information)
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# Overview
A birthmark is a skin marking that is present at birth. Birthmarks include cafe-au-lait spots, moles, and mongolian spots.

# What are the symptoms of Birthmarks-pigmented?
Each type of birthmark has its own appearance:
- Cafe-au-lait spots are light tan, the color of coffee with milk.
- Moles are small clusters of colored skin cells.
- Mongolian spots (also called Mongolian blue spots) are usually bluish or bruised-looking. They usually appear over the lower back or buttocks, but can also appear in other areas, including the trunk or arms.
Other symptoms of birthmarks:
- Abnormally dark or light skin
- Contain hair
- Skin lesion
- Skin lumps
- Textured -- smooth, flat, raised, or wrinkled

# Who is at highest risk?
- Cafe-au-lait spots may occur in people with the genetic disorder, neurofibromatosis.
- Nearly everyone has moles, which usually appear after birth.
- Mongolian spots are more commonly seen in darker-skinned populations.

# Diagnosis
Diagnosis is usually made based on the appearance of the skin area. A biopsy may be performed to look for cancerous changes.

# When to seek urgent medical care?
Have any birthmarks examined by a health care provider. Report any changes in the birthmark to your health care provider, including:
- Bleeding
- Color change
- Inflammation
- Itching
- Open sore (ulceration)
- Pain
- Size change
- Texture change

# Treatment options
- Treatment varies depending on the type of birthmark and related conditions. Usually no treatment is needed for the birthmark itself.
- Large birthmarks that affect your appearance and self-esteem may be covered with special cosmetics.
- Moles may be removed surgically if they affect your appearance or have an increased cancer risk. Discuss your options with your doctor to decide how and when to remove any moles.

# Where to find medical care for Birthmarks-pigmented?
Directions to Hospitals Treating Birthmarks-pigmented

# What to expect (Outlook/Prognosis)?
Large moles that are present at birth (congenital nevi) are more likely to become skin cancer (malignant melanoma). This is especially true if the mole covers an area larger than the size of a fist. The cancer risk is related to the size, location, shape, and color of the mole.
Mongolian spots may persist for months or years. They do NOT become cancer or develop other symptoms.

# Possible complications
- Skin cancer
- Psychological effects, if the birthmark is prominent

# Prevention of Birthmarks-pigmented
There is no known way to prevent birthmarks. A person with birthmarks should use a good quality sunscreen when outdoors (to prevent complications).

# Sources
C3orf14-Chromosome 3 open reading frame 14
The human gene Chromosome 3 open reading frame 14 is a gene of uncertain function located at 3p14.2 near fragile site FRBA3which falls between this gene and the centromere. Its protein is expected to localize to the nucleus and bind DNA. Orthologs have been identified in all of the major animal groups, minus amphibians and insects, tracing as far back as the sea anemone; indicating an origin of over 1000 mya, highlighting its importance in the animal genome.

# Gene Aliases
C3orf14 is also known by the aliases LOC57415, FLJ94553 and FLJ17473. Gene orthologs found in other organisms are usually known by the name c3orf14-like, though some are known as LOC57415-like or HT021-like (protein name).

# Protein Properties
The mRNA is composed of 6 exons, and encodes a 15007.84 kD protein known as HT021. This protein has a pre-modification isoelectric point of 5.57 and alpha helices span most of its length. Four sites of possible phosphorylation have been identified, and at least two sites of phosphorylation are conserved in all orthologs, as are two alpha helices. This protein is also predicted as a DNA binding protein. The protein may assume a tertiary structure of a coiled coil.

# Homology
Orthologs of this gene has been identified in most animal groups: mammals, monotremes, aves, reptiles, fish and invertebrates. Transcripts have not been identified in amphibians or insects; however only model organisms have been sequenced from these groups.  Very recently the first ortholog in reptiles was identified in Anolis carolinensis.  The amino acid structure is highly conserved through mammals, and the secondary and tertiary structure is highly conserved in all orthologs, dating as far back as 1000 mya in the sea anemone. No orthologs have been found in plants or bacteria.  Below is a phylogenetic tree generated in SDSC Biology Workbench showing protein similarity among species in which C3orf14 has been identified.

# Expression
This gene was first identified in the hypothalamic-pituitary-adrenal axis (HPA axis). The GEO and EST profiles in NCBI, indicate that its expression level varies from tissue to tissue; however its reported expression is 1.2 times that of the average gene. It has highest expression in the pancreas and nervous tissue (in humans). It is underexpressed in many cancer cell lines, however this may be due to its close proximity to the tumor suppressor gene FHIT, and the chromosomal fragile site FRBA3. Breakage at this site inactivates FHIT and can lead to the loss of C3orf14.

# Function
Because C3orf14 is not ubiquitously expressed, it most likely is not a housekeeping gene. Instead, it more likely plays a role in the function of specific tissues. It seems likely then, that this gene is a transcription factor, which regulates the expression of other genes important for the function of tissues where this gene is expressed highest.