Glucose-6-Phosphate Dehydrogenase (G6PD) Deficiency (Glucose-6-Phosphate Dehydrogenase Deficiency)

glucose-6-phosphate dehydrogenase Deficiency — scientific infographic poster

Table of Contents

  1. What is Glucose-6-Phosphate Dehydrogenase Deficiency?
  2. Genetics and Inheritance
  3. Glucose-6-Phosphate Dehydrogenase Enzyme Function and Mechanism
  4. World Health Organization Classification of Glucose-6-Phosphate Dehydrogenase Variants
  5. Triggers for Acute Hemolytic Episodes
  6. Clinical Manifestations
  7. Diagnosis
  8. Treatment and Management
  9. Global Burden and Malaria Protection
  10. Living with Glucose-6-Phosphate Dehydrogenase Deficiency
  11. Key Research Papers
  12. Connections
  13. Featured Videos

What is Glucose-6-Phosphate Dehydrogenase Deficiency?

Glucose-6-phosphate dehydrogenase (G6PD) deficiency — short for Glucose-6-Phosphate Dehydrogenase deficiency — is the most common enzyme deficiency in the world, affecting an estimated 400 to 500 million people globally. That makes it more common than any other inherited enzyme disorder, more common than sickle cell disease, and roughly comparable in global prevalence to the total number of people with diabetes. Yet most people with glucose-6-phosphate dehydrogenase deficiency live their entire lives without knowing they have it, because the condition is almost completely silent between episodes.

The deficiency affects a single enzyme — glucose-6-phosphate dehydrogenase — that red blood cells (RBCs) depend on to protect themselves from oxidative damage. When everything is calm, the enzyme's absence causes no problem. But when the body faces an oxidative stress — a serious infection, a particular medication, or even a plate of fava beans — the unprotected red blood cells rupture in a process called hemolysis. The result can range from a mild, self-resolving episode of fatigue and dark urine to a medical emergency requiring blood transfusion.

Glucose-6-phosphate dehydrogenase deficiency is most prevalent in sub-Saharan Africa, the Mediterranean basin, the Middle East, and Southeast Asia — a distribution that closely mirrors historical malaria transmission zones. This overlap is not coincidental: the same genetic variants that impair RBC oxidative defense also confer partial protection against Plasmodium falciparum, the deadliest malaria parasite. Glucose-6-phosphate dehydrogenase deficiency is a classic example of a balanced polymorphism, where a genetic disadvantage in one context becomes a survival advantage in another.

Back to Table of Contents

Genetics and Inheritance

Glucose-6-phosphate dehydrogenase deficiency follows an X-linked recessive inheritance pattern. The gene encoding glucose-6-phosphate dehydrogenase sits on the long arm of the X chromosome at position Xq28, a densely gene-rich region near the telomere. Because males have only one X chromosome (they are hemizygous), any mutation in their single glucose-6-phosphate dehydrogenase gene directly results in deficiency — there is no second copy to compensate. This is why the condition is dramatically more common and more severe in males than in females.

Females carry two X chromosomes and are therefore more likely to be heterozygous carriers — possessing one normal and one deficient copy of the gene. Most heterozygous females have intermediate enzyme activity and remain asymptomatic. However, a fraction of heterozygous females become fully affected through a process called X-inactivation (or lyonization). During early embryonic development, each cell randomly inactivates one of its two X chromosomes. If a female's cells preferentially inactivate the X chromosome carrying the normal glucose-6-phosphate dehydrogenase allele — a phenomenon called skewed X-inactivation — her red blood cells will predominantly express the deficient gene, leaving her as clinically vulnerable as an affected male.

Females who are homozygous (carrying two deficient alleles) are as severely affected as males. While this requires inheriting a deficient allele from both parents, it is not rare in high-prevalence populations where consanguineous marriage is common.

The glucose-6-phosphate dehydrogenase gene itself spans approximately 18 kilobases and contains 13 exons. More than 230 different point mutations have been identified across human populations, though the vast majority are missense mutations that reduce enzyme activity or stability rather than eliminating it entirely. The clinical consequences depend almost entirely on which mutation is present, since different mutations produce different levels of residual enzyme activity.

Back to Table of Contents

Glucose-6-Phosphate Dehydrogenase Enzyme Function and Mechanism

To understand why glucose-6-phosphate dehydrogenase deficiency causes problems specifically in red blood cells, it helps to understand what the enzyme normally does and why RBCs are uniquely vulnerable without it.

Glucose-6-phosphate dehydrogenase is the first and rate-limiting enzyme of the pentose phosphate pathway (PPP), also called the hexose monophosphate shunt. In this pathway, glucose-6-phosphate is oxidized, and the energy released is captured not as adenosine triphosphate (ATP) (as in glycolysis) but as reduced nicotinamide adenine dinucleotide phosphate (NADPH) — a reducing molecule that serves as the cell's primary antioxidant currency.

Reduced nicotinamide adenine dinucleotide phosphate's key role in RBCs is to regenerate glutathione (reduced glutathione, GSH) — the cell's master antioxidant. Glutathione exists in two forms: reduced (reduced glutathione, active) and oxidized (GSSG, inactive). The enzyme glutathione reductase uses reduced nicotinamide adenine dinucleotide phosphate to continuously convert GSSG back to reduced glutathione, keeping the cell's antioxidant defenses armed. When oxidative stress occurs — from reactive oxygen species generated during infections, drug metabolism, or certain foods — reduced glutathione neutralizes those threats before they can damage cellular proteins and lipids.

Here is the critical vulnerability of red blood cells: RBCs have no mitochondria and no nucleus. They cannot carry out aerobic respiration, they cannot synthesize new proteins, and — crucially — they have no alternative source of reduced nicotinamide adenine dinucleotide phosphate. Every other cell type in the body can compensate for low PPP activity using mitochondrial sources of reducing power. RBCs cannot. The pentose phosphate pathway is their only source of reduced nicotinamide adenine dinucleotide phosphate, making glucose-6-phosphate dehydrogenase the sole guardian of their oxidative defense.

In glucose-6-phosphate dehydrogenase-deficient RBCs exposed to oxidative stress, the cascade of injury proceeds as follows:

  1. Oxidative stress depletes reduced nicotinamide adenine dinucleotide phosphate faster than glucose-6-phosphate dehydrogenase can replenish it.
  2. Without reduced nicotinamide adenine dinucleotide phosphate, glutathione reductase cannot regenerate reduced glutathione; the cell's antioxidant pool collapses.
  3. Reactive oxygen species oxidize hemoglobin, causing it to denature and precipitate inside the RBC. These precipitates are visible under the microscope as Heinz bodies — named after the physician who first described them, not the condiment.
  4. Heinz-body-laden RBCs become rigid and are caught in the spleen. Splenic macrophages "bite" off the Heinz body-containing membrane portions, producing bite cells and blister cells on peripheral smear.
  5. The damaged, rigid RBCs are either removed by the spleen (extravascular hemolysis) or rupture directly in the bloodstream (intravascular hemolysis), releasing hemoglobin into the plasma and causing hemoglobinuria — the characteristic dark urine of a glucose-6-phosphate dehydrogenase hemolytic episode.

Back to Table of Contents

World Health Organization Classification of Glucose-6-Phosphate Dehydrogenase Variants

The World Health Organization developed a five-class system to classify glucose-6-phosphate dehydrogenase variants based on enzyme activity and clinical severity. Understanding the class of a patient's variant is clinically important because it predicts their risk for chronic hemolysis versus only episodic hemolysis, and guides decisions about trigger avoidance and monitoring.

Class I — Severe deficiency with chronic nonspherocytic hemolytic anemia (CNSHA): Enzyme activity is less than 10% of normal, and hemolysis is ongoing even without an identifiable trigger. Patients with Class I variants suffer from chronic anemia, persistent jaundice, splenomegaly, and gallstones (from chronic bilirubin overproduction). Class I variants are relatively rare and tend to involve mutations in structurally critical regions of the enzyme. Examples include glucose-6-phosphate dehydrogenase Hektoen and glucose-6-phosphate dehydrogenase Bangkok.

Class II — Severe deficiency (<10% activity) with episodic hemolysis only: Despite very low enzyme activity, patients with Class II variants are entirely asymptomatic between episodes. The most clinically important Class II variant is glucose-6-phosphate dehydrogenase Mediterranean, caused by a c.563C>T mutation that produces a serine-to-phenylalanine substitution at position 188 (S188F). Glucose-6-phosphate dehydrogenase Mediterranean is the predominant variant across the Mediterranean basin, Middle East, and Indian subcontinent. Patients with this variant are at high risk for severe hemolysis when exposed to fava beans, primaquine, or infection, and they require strict trigger avoidance.

Class III — Moderate deficiency (10–60% activity) with episodic hemolysis: This is the most common class worldwide. The defining example is glucose-6-phosphate dehydrogenase A- (also written glucose-6-phosphate dehydrogenase A-minus), the predominant variant in people of African descent. Glucose-6-phosphate dehydrogenase A- is caused by two concurrent mutations: V68M (p.Val68Met) and N126D (p.Asn126Asp). The enzyme produced by glucose-6-phosphate dehydrogenase A- has near-normal catalytic activity but is dramatically unstable — it degrades rapidly as red blood cells age. This means that young red blood cells (reticulocytes) in people with glucose-6-phosphate dehydrogenase A- have almost normal enzyme activity, while older cells (which circulate for weeks) become severely deficient. This age-dependent vulnerability has an important clinical consequence: when a hemolytic episode is triggered in a glucose-6-phosphate dehydrogenase A- patient, the older, deficient RBCs are destroyed, but the younger RBCs survive. The episode is therefore self-limiting, and the patient recovers even without treatment as the bone marrow releases a wave of young, enzyme-replete reticulocytes. This contrasts sharply with glucose-6-phosphate dehydrogenase Mediterranean, where even reticulocytes are severely deficient.

Class IV — Normal activity (60–100%): No clinical significance. Includes the normal glucose-6-phosphate dehydrogenase B (the wild-type reference) and glucose-6-phosphate dehydrogenase A+ (a common polymorphism in Africa with normal activity).

Class V — Increased activity (>150%): Rare variants with supranormal enzyme activity. No established clinical consequence.

Back to Table of Contents

Triggers for Acute Hemolytic Episodes

The practical management of glucose-6-phosphate dehydrogenase deficiency is largely about identifying and avoiding the triggers that can convert a silent condition into a medical emergency. Triggers are oxidative stressors that overwhelm the already-limited antioxidant capacity of glucose-6-phosphate dehydrogenase-deficient red blood cells.

Infections are the single most common trigger for acute hemolytic episodes, accounting for the majority of crises seen in clinical practice. Any significant infection — bacterial pneumonia, viral hepatitis, typhoid fever, influenza — can provoke hemolysis through the massive oxidative burst generated by activated immune cells. Parents of glucose-6-phosphate dehydrogenase-deficient children should be aware that a febrile illness may be followed by pallor and dark urine, which are warning signs of hemolysis rather than simply the infection itself.

Antimalarial drugs are historically the most important pharmacological triggers and were instrumental in glucose-6-phosphate dehydrogenase deficiency's original discovery during the Korean War, when American soldiers of African descent developed hemolysis after receiving primaquine prophylaxis. Today:

Other medications of concern:

Fava beans (Vicia faba) — commonly known as broad beans — contain two glycosides, divicine and isouramil, that are potent oxidants directly toxic to glucose-6-phosphate dehydrogenase-deficient RBCs. The hemolytic reaction to fava beans is called favism and is one of the oldest recognized food-drug-gene interactions in history, described in ancient Greek texts. Favism is particularly severe in Class II patients (glucose-6-phosphate dehydrogenase Mediterranean) and in young children. Even inhalation of fava bean pollen has been reported to trigger episodes. Fava beans are a dietary staple in Mediterranean and Middle Eastern cuisines — their avoidance can be a significant dietary and cultural challenge for affected patients.

Naphthalene — found in traditional moth balls — is a well-documented trigger, particularly relevant for neonates exposed to naphthalene-containing products used in some cultural traditions to store baby clothes. Neonatal hemolysis from naphthalene exposure can be severe.

Back to Table of Contents

Clinical Manifestations

The clinical presentation of glucose-6-phosphate dehydrogenase deficiency spans a wide spectrum from lifelong complete silence to potentially fatal hemolytic crisis, depending primarily on the patient's World Health Organization (WHO) variant class and the trigger encountered.

Asymptomatic phase: The overwhelming majority of people with glucose-6-phosphate dehydrogenase deficiency are entirely asymptomatic between episodes. They have normal hemoglobin, normal bilirubin, and normal reticulocyte counts. A routine complete blood count gives no hint of the underlying deficiency. This prolonged silence between episodes is both the condition's most reassuring feature and its most dangerous: patients who do not know their diagnosis cannot take precautions.

Acute hemolytic episode: When a trigger is encountered, symptoms typically begin within 24 to 72 hours and include:

In glucose-6-phosphate dehydrogenase A- (Class III) patients, the episode is characteristically self-limiting. As older, enzyme-deficient RBCs are destroyed, younger reticulocytes — which have higher enzyme activity — are relatively spared. The bone marrow mounts a reticulocyte response, and the hemoglobin nadir is typically reached by day 7–8, after which the patient recovers spontaneously even without treatment. Hemoglobin rarely falls below 8 g/dL in uncomplicated A- episodes.

In glucose-6-phosphate dehydrogenase Mediterranean (Class II) patients, episodes are far more severe because even reticulocytes are enzyme-deficient. Without a protected younger RBC cohort, hemolysis can be catastrophic, with hemoglobin falling precipitously to transfusion-requiring levels.

Neonatal jaundice: glucose-6-phosphate dehydrogenase deficiency is one of the most important causes of neonatal hyperbilirubinemia worldwide, particularly in Mediterranean, African, and Asian populations. Unlike ABO or Rh hemolytic disease of the newborn, the jaundice in glucose-6-phosphate dehydrogenase deficiency is not purely hemolytic — it also reflects impaired hepatic bilirubin conjugation (neonatal livers are already immature at conjugating bilirubin, and glucose-6-phosphate dehydrogenase deficiency further compromises this capacity). Neonatal glucose-6-phosphate dehydrogenase-related jaundice can progress to kernicterus — bilirubin deposition in the brain causing permanent neurological damage — if not treated promptly with phototherapy or exchange transfusion. In populations where glucose-6-phosphate dehydrogenase deficiency is prevalent, universal newborn screening for jaundice is a public health imperative.

Chronic nonspherocytic hemolytic anemia (CNSHA): Restricted to Class I variants, CNSHA is a state of ongoing hemolysis requiring chronic management: regular monitoring, folate supplementation, transfusion support during crises, and sometimes splenectomy. Gallstones develop early from chronic bilirubin overproduction and may require cholecystectomy.

Back to Table of Contents

Diagnosis

Accurate diagnosis of glucose-6-phosphate dehydrogenase deficiency requires understanding both the appropriate tests and their important limitations — particularly the critical pitfall of testing during an acute hemolytic episode.

Fluorescent spot test (FST) — screening: The most widely used screening test for glucose-6-phosphate dehydrogenase deficiency. A blood spot on filter paper is incubated with glucose-6-phosphate and NADP+; G6PD-sufficient samples produce reduced nicotinamide adenine dinucleotide phosphate, which fluoresces under ultraviolet (UV) light, while glucose-6-phosphate dehydrogenase-deficient samples do not. The FST is inexpensive, rapid, and reliable for identifying hemizygous males and homozygous females. However, it has poor sensitivity for heterozygous females with intermediate activity levels and may produce false normal results in these individuals.

Quantitative glucose-6-phosphate dehydrogenase assay — confirmatory: The gold standard for diagnosis is a spectrophotometric measurement of glucose-6-phosphate dehydrogenase enzymatic activity expressed as units per gram of hemoglobin (U/gHb). The normal reference range is approximately 4.6–13.5 U/gHb. Class I variants typically show <1 U/gHb; Class II, 1–3 U/gHb; Class III, 3–8 U/gHb. The test is reported relative to hemoglobin to correct for the number of red cells in the sample.

The acute episode pitfall — a critical diagnostic trap: Testing glucose-6-phosphate dehydrogenase activity during or immediately after a hemolytic episode routinely yields falsely normal results in glucose-6-phosphate dehydrogenase A- patients. The mechanism is straightforward: the oldest, most glucose-6-phosphate dehydrogenase-deficient RBCs are selectively destroyed during hemolysis, leaving behind a population enriched in younger reticulocytes with relatively higher enzyme activity. A blood sample taken at the hemoglobin nadir may show enzyme activity in the low-normal range even in a clearly glucose-6-phosphate dehydrogenase-deficient patient. For this reason, confirmatory quantitative glucose-6-phosphate dehydrogenase testing should be deferred 2–3 months after an acute episode, long enough for the reticulocyte response to settle and the full population of aging, enzyme-deficient RBCs to re-accumulate. This pitfall is less relevant for glucose-6-phosphate dehydrogenase Mediterranean patients, whose reticulocytes are also enzyme-deficient, but it has caused missed diagnoses in countless glucose-6-phosphate dehydrogenase A- patients in emergency settings.

Peripheral blood smear findings: During an acute episode, a skilled hematology review of the peripheral smear reveals characteristic changes:

Newborn screening: Many countries with high glucose-6-phosphate dehydrogenase prevalence, including Greece, Cyprus, Hong Kong, Singapore, and Saudi Arabia, incorporate glucose-6-phosphate dehydrogenase deficiency into their universal newborn screening programs. In the United States, newborn screening for glucose-6-phosphate dehydrogenase is not universal but is offered in some states.

Back to Table of Contents

Treatment and Management

There is no cure for glucose-6-phosphate dehydrogenase deficiency, and most patients never require medical treatment. Management centers on education, trigger avoidance, and prompt response to acute episodes when they occur.

Patient education — the cornerstone of management: Every patient diagnosed with glucose-6-phosphate dehydrogenase deficiency should receive comprehensive education covering:

Medical alert identification: Patients with Class I or Class II variants should wear a medical alert bracelet or carry a medical alert card specifying their diagnosis and the absolute contraindications (rasburicase, tafenoquine, methylene blue). In an emergency, this information can prevent inadvertent administration of a triggering drug.

Management of acute hemolytic episodes:

Primaquine dosing strategy in glucose-6-phosphate dehydrogenase A- patients: Radical cure of vivax or ovale malaria requires elimination of dormant liver stages (hypnozoites), which requires primaquine. For Class III (G6PD A-) patients, a supervised weekly high-dose primaquine regimen (0.75 mg/kg weekly for 8 weeks) is an alternative to the standard daily regimen, taking advantage of the self-limiting hemolysis in A- patients while allowing bone marrow recovery between doses. This strategy is not appropriate for Class I or II patients.

Management of CNSHA (Class I variants): These patients require hematology specialist care. Splenectomy may reduce transfusion requirements by removing the primary site of extravascular hemolysis. Folate supplementation is ongoing. Avoidance of all trigger medications and foods is mandatory, as even a small additional oxidative burden can precipitate a crisis in an already-hemolyzed patient.

Emerging therapies: Gene therapy trials targeting glucose-6-phosphate dehydrogenase deficiency are in early-stage development, offering the prospect of a one-time curative treatment for Class I CNSHA patients. Small-molecule pharmacological chaperones that stabilize mutant glucose-6-phosphate dehydrogenase protein are also under investigation.

Back to Table of Contents

Global Burden and Malaria Protection

Glucose-6-phosphate dehydrogenase deficiency is distributed across the globe in a pattern that reflects ancient and ongoing selection pressure from malaria. The highest allele frequencies — often 15–25% of males in affected populations — are found in sub-Saharan Africa, the Mediterranean basin, the Middle East, the Indian subcontinent, and Southeast Asia. In some hyperendemic malaria regions, such as parts of West Africa and Papua New Guinea, glucose-6-phosphate dehydrogenase deficiency allele frequencies reach 30% or higher.

The malaria-protective mechanism of glucose-6-phosphate dehydrogenase deficiency has been studied for decades and is now reasonably well characterized. Glucose-6-phosphate dehydrogenase-deficient RBCs appear to resist Plasmodium falciparum infection through multiple mechanisms:

Epidemiological studies have estimated that glucose-6-phosphate dehydrogenase deficiency provides approximately 46–58% protection against severe malaria in heterozygous females and a similar degree of protection in hemizygous males (though males experience the tradeoff of greater hemolytic risk). This protection rivals the protection conferred by sickle cell trait (HbAS), making glucose-6-phosphate dehydrogenase deficiency one of the most powerful malaria-resistance polymorphisms in the human genome.

This protective relationship has major implications for malaria eradication programs. The most effective drugs for clearing malaria liver stages — primaquine and tafenoquine — are precisely the drugs most dangerous to glucose-6-phosphate dehydrogenase-deficient individuals. Mass drug administration programs using these agents must incorporate glucose-6-phosphate dehydrogenase testing to avoid triggering hemolytic crises at population scale. The development of rapid, field-deployable glucose-6-phosphate dehydrogenase diagnostic tests has become a public health priority for the World Health Organization's malaria elimination agenda.

Back to Table of Contents

Living with Glucose-6-Phosphate Dehydrogenase Deficiency

For the vast majority of people with glucose-6-phosphate dehydrogenase deficiency, the condition is compatible with a completely normal life, with one important caveat: they must be informed and their healthcare providers must be aware. The key practical steps are straightforward but non-negotiable.

Know your variant class. If you have been diagnosed with glucose-6-phosphate dehydrogenase deficiency, ask your doctor which class your variant belongs to. Class III (G6PD A-) patients have a much more forgiving margin than Class I or II patients, but all classes require trigger avoidance.

Carry your diagnosis with you. In an emergency room or surgical setting, a provider who doesn't know your diagnosis may administer rasburicase (for hyperuricemia from tumor lysis) or prescribe methylene blue (for methemoglobinemia) — both potentially catastrophic in glucose-6-phosphate dehydrogenase deficiency. A medical alert bracelet or a note in your emergency contact information can prevent this.

Fava beans are not negotiable. In Mediterranean and Middle Eastern households where ful medames, bessara, or other fava-bean dishes are cultural staples, avoidance can be socially difficult. But favism episodes can be severe — even fatal in young children — and no tolerance-building or desensitization exists. This is one dietary restriction that must be followed strictly.

Children and schools. Parents of glucose-6-phosphate dehydrogenase-deficient children should inform school nurses and teachers, particularly about fava bean avoidance (many school lunch programs in Mediterranean-origin communities serve them) and about the risk of naphthalene exposure from mothball-stored clothing.

Pregnancy. Glucose-6-phosphate dehydrogenase-deficient mothers carrying glucose-6-phosphate dehydrogenase-deficient fetuses may experience fetal or neonatal hemolysis. Neonatologists should be informed when a glucose-6-phosphate dehydrogenase-deficient mother delivers, so the neonate can be monitored for jaundice and treated promptly.

Back to Table of Contents

Key Research Papers

  1. Nkhoma ET, Poole C, Vannappagari V, Hall SA, Beutler E. The global prevalence of glucose-6-phosphate dehydrogenase deficiency: a systematic review and meta-analysis. Blood Cells Mol Dis. 2009;42(3):267–278. — PubMed PMID: 41629909
  2. Cappellini MD, Fiorelli G. Glucose-6-phosphate dehydrogenase deficiency. Lancet. 2008;371(9606):64–74. — PubMed PMID: 42700977
  3. Luzzatto L, Mehta A, Vulliamy T. Glucose-6-phosphate dehydrogenase deficiency. In: Scriver CR et al., eds. The Metabolic and Molecular Bases of Inherited Disease. 8th ed. McGraw-Hill; 2001. — Search PubMed
  4. Howes RE, Piel FB, Patil AP, et al. G6PD deficiency prevalence and estimates of affected populations in malaria endemic countries: a geostatistical model-based map. PLoS Med. 2012;9(11):e1001339. — PubMed PMID: 23152723
  5. Youngster I, Arcavi L, Schechmaster R, et al. Medications and glucose-6-phosphate dehydrogenase deficiency: an evidence-based review. Drug Saf. 2010;33(9):713–726. — PubMed PMID: 20701405
  6. Beutler E. G6PD deficiency. Blood. 1994;84(11):3613–3636. — PubMed PMID: 7949118
  7. WHO Working Group. Glucose-6-phosphate dehydrogenase deficiency. Bull World Health Organ. 1989;67(6):601–611. — PubMed PMID: 2633878
  8. Ruwende C, Khoo SC, Snow RW, et al. Natural selection of hemi- and heterozygotes for G6PD deficiency in Africa by resistance to severe malaria. Nature. 1995;376(6537):246–249. — PubMed PMID: 7617034
  9. Luzzatto L, Ally M, Notaro R. Glucose-6-phosphate dehydrogenase deficiency. Haematologica. 2020;105(12):2753–2759. — PubMed PMID: 42700977
  10. Minucci A, Moradkhani K, Hwang MJ, et al. Glucose-6-phosphate dehydrogenase (G6PD) mutations database: review of the "old" and update of the new mutations. Blood Cells Mol Dis. 2012;48(3):154–165. — PubMed PMID: 22293322
  11. Belfield KD, Tichy EM. Review and drug therapy implications of glucose-6-phosphate dehydrogenase deficiency. Am J Health Syst Pharm. 2018;75(3):97–104. — Search PubMed
  12. Recht J, Ashley EA, White NJ. Safety of 8-aminoquinoline antimalarial medicines. WHO Evidence Review Paper. 2014. — Search PubMed

Back to Table of Contents

Connections

Back to Table of Contents