Lead azide (CED0017976)

Record Information
Version1.0
Creation Date2009-03-06 18:58:31 UTC
Update Date2026-08-26 17:01:19 UTC
SynCED IDCED0017976
Secondary Accession Numbers
  • CHEM000270
  • T3D0321
Identification
Common NameLead azide
ClassSmall Molecule
Description
Lead azide is an exogenous inorganic compound with the formula N6Pb and an average molecular weight of 291.20 g/mol. At room temperature, it exists as a solid. Lead azide belongs to the post-transition metal nitrides, a subclass of post-transition metal organides within the inorganic compounds. It is used mainly in detonators and has been recorded as being found in or released from electrical and electronic equipment, specifically antennas, cores yokes or armatures, and electric switches. The compound interacts with 24 recorded protein targets. Lead binds to the acyl-CoA-binding protein (DBI), which regulates processes including insulin secretion, steroidogenesis, GABA-A/benzodiazepine receptor modulation, intestinal cholecystokinin release, and acyl-CoA metabolism. It binds to sodium/potassium-transporting ATPases, including subunits FXYD2, ATP1A1, ATP1A2, and ATP1A3. Additionally, lead binds to thymosin beta-4, an immunotransmitter that functions in the stimulation of CaM-dependent kinases, modulation of the cytoskeleton, and GABA-A receptor complex function. Lead azide exhibits competitive inhibition at several sites. It competitively inhibits calcium's binding of calmodulin, which alters cAMP messenger pathways and interferes with neurotransmitter release. It also competitively inhibits calcium at protein kinase C (including types PRKCA, PRKCB, PRKCD, and PRKCE), altering the blood-brain barrier and impairing brain microvascular function and formation. Competitive inhibition also occurs at the NMDA receptor, affecting proteins GRIN2A, GRIN2B, GRIN2C, and GRIN3A, which affects neurotransmitter release. Finally, lead inhibits ferrochelatase (FECH) and delta-aminolevulinic acid dehydratase (ALAD), both of which prevents the biosynthesis of heme, a necessary cofactor of hemoglobin.
Contaminant Type
  • Industrial/Workplace Toxin
  • Inorganic Compound
  • Lead Compound
  • Pollutant
  • Synthetic Compound
Chemical Structure
SynonymsNot Available
Chemical FormulaN6Pb
Average Molecular Mass291.200 g/mol
Monoisotopic Mass291.995 g/mol
CAS Registry Number13424-46-9
IUPAC Namediazidoplumbane
Traditional Namediazidoplumbane
SMILES[N-]=[N+]=N[Pb]N=[N+]=[N-]
InChI IdentifierInChI=1S/2N3.Pb/c2*1-3-2;/q2*-1;+2
InChI KeyISEQAARZRCDNJH-UHFFFAOYSA-N
Chemical Taxonomy
Description Belongs to the class of inorganic compounds known as post-transition metal nitrides. These are inorganic compounds of nitrogen where nitrogen has a formal oxidation state of -3, and the heaviest metal atom is a post-transition metal.
KingdomInorganic compounds
Super ClassMixed metal/non-metal compounds
ClassPost-transition metal organides
Sub ClassPost-transition metal nitrides
Direct ParentPost-transition metal nitrides
Alternative Parents
Substituents
  • Post-transition metal nitride
  • Inorganic azide
  • Inorganic lead salt
  • Inorganic nitride
  • Inorganic salt
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid LocationsNot Available
Tissue LocationsNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Organoleptic EffectsNot Available
Physical Properties
StateSolid
AppearanceWhite powder.
Experimental Properties
PropertyValue
Melting Point190°C
Boiling PointNot Available
SolubilityNot Available
Predicted Properties
PropertyValueSource
logP1.47ChemAxon
pKa (Strongest Basic)-9.1ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count4ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area58.86 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity21.74 m³·mol⁻¹ChemAxon
Polarizability8.03 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyDeposition DateView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-0090000000-288a19beb0e855e900e9Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-0090000000-288a19beb0e855e900e9Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-0090000000-288a19beb0e855e900e9Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-0090000000-c808d2d68eed4c8e37dcNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-0090000000-c808d2d68eed4c8e37dcNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-0090000000-c808d2d68eed4c8e37dcNot AvailableView Spectrum
Toxicity Profile
Toxicity ValuesNot Available
Toxicity / Toxin ClassNot Available
Mechanism of ToxicityLead mimics other biologically important metals, such as zinc, calcium, and iron, competing as cofactors for many of their respective enzymatic reactions. For example, lead has been shown to competitively inhibit calcium's binding of calmodulin, interferring with neurotransmitter release. It exhibits similar competitive inhibition at the NMDA receptor and protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. Lead also affects the nervous system by impairing regulation of dopamine synthesis and blocking evoked release of acetylcholine. However, it's main mechanism of action occurs by inhibiting delta-aminolevulinic acid dehydratase, an enzyme vital in the biosynthesis of heme, which is a necesssary cofactor of hemoglobin. (9, 2, 3, 7)
Carcinogenicity (IARC Classification)2A, probably carcinogenic to humans. (6)
Minimum Risk LevelChronic Inhalation: 0.05 mg/m3 (5)
SymptomsSymptions of chronic lead poisoning include reduced cognitive abilities, nausea, abdominal pain, irritability, insomnia, metal taste in the mouth, excess lethargy or hyperactivity, chest pain, headache and, in extreme cases, seizures, comas, and death. There are also associated gastrointestinal problems, such as constipation, diarrhea, vomiting, poor appetite, weight loss, which are common in acute poisoning. (1, 4)
TreatmentLead poisoning is usually treated with chelation therapy using DMSA, EDTA, or dimercaprol. (4)
Health Effects
Health EffectRelationshipDirectionDescriptionReference
Exposure Sources
Source IDSourceSectorReference
CEDs000506Antennas?Antennas, commonly used in communication technologies, can be a source of synthetic chemical contamination through the materials and coatings used in their construction.Electrical & Electronic EquipmentPubChem
CEDs000511Conductors Or Conductive Bodies Characterised By The Conductive Materials?Conductors, or conductive bodies, are materials that allow the flow of electrical current, typically made from metals such as copper, aluminum, or silver.Electrical & Electronic EquipmentPubChem
CEDs000513Cores Yokes Or Armatures?Cores, yokes, or armatures are components commonly found in electrical devices, used to facilitate the magnetic and electrical functions within motors, transformers, and generators.Electrical & Electronic EquipmentPubChem
CEDs000517Electric Switches?Electric switches, integral components in numerous devices, can be a source of synthetic chemical contamination due to the materials and manufacturing processes involved in their production.Electrical & Electronic EquipmentPubChem
CEDs000519Electrodes?Electrodes, used in various electrical and electronic applications, can be a source of synthetic chemical contamination due to the materials from which they are constructed and the processes involved in their manufacturing.Electrical & Electronic EquipmentPubChem
CEDs000581Paper Making Machines?Paper making machines utilize various synthetic chemicals throughout the production process, including additives, coatings, and bleaching agents.Industrial manufacturing & chemical processingPubChem
CEDs000583Anchoring Equipment?Anchoring equipment, commonly used in marine applications, can be a source of synthetic chemical contamination due to the materials and coatings utilized in their manufacturing.Marine, shipping & aquaculturePubChem
CEDs000588Inflatable Life Saving Equipment?Inflatable Life Saving Equipment (ILSE) is commonly made from synthetic materials such as polyvinyl chloride (PVC), thermoplastic polyurethane (TPU), or nylon coated with polymer films.Marine, shipping & aquaculturePubChem
CEDs000589Life Buoys?Life buoys, commonly used in marine environments for safety and rescue operations, can be a source of synthetic chemical contamination due to the materials used in their production.Marine, shipping & aquaculturePubChem
CEDs000665Fire Extinguishers?Fire extinguishers contain various synthetic chemicals designed to suppress flames and prevent the spread of fire.Fire suppression systems & agentsPubChem
CEDs000671Airplanes And Helicopters?Airplanes and helicopters are significant sources of synthetic chemical contamination primarily through the use of aviation fuels, lubricants, and de-icing agents.Aviation & AerospacePubChem
CEDs000678Nitrogenous Fertilisers?Nitrogenous fertilizers are synthetic chemical compounds primarily used to enhance plant growth by supplying essential nitrogen, a crucial nutrient for photosynthesis and protein synthesis.Agriculture & land managementPubChem
CEDs000686Clay Wares?Clay wares are ceramic products made from natural clay, often utilized in various construction applications such as tiles, bricks, and sanitary ware.Building & ConstructionPubChem
CEDs000696Nanotechnology?Nanotechnology involves the manipulation of materials at the molecular or atomic level, typically within the range of 1 to 100 nanometers.Industrial manufacturing & chemical processingPubChem
CEDs000698Jewellery?Jewellery production often involves the use of various synthetic chemicals during the extraction and processing of metals.Mining & metal processingPubChem
CEDs000699Mining Or Quarrying?Mining and quarrying operations can lead to synthetic chemical contamination through the release of various pollutants associated with the extraction and processing of minerals.Mining & metal processingPubChem
CEDs000735Explosives?Explosives are chemical compounds or mixtures designed to undergo rapid decomposition, releasing energy in the form of gas and heat.Defense & military infrastructurePubChem
CEDs000736Fuses?Fuses are safety devices designed to protect electrical circuits by breaking the circuit when excessive current flows through.Electrical & Electronic EquipmentPubChem
CEDs000737Chemical Igniters?Chemical igniters are substances or devices designed to initiate combustion in various applications, often found in products like lighters, candles, and certain household cleaning agents.Household itemsPubChem
CEDs000740Paper?Paper production involves the processing of wood fibers and the use of various chemicals, which can lead to synthetic chemical contamination.Paper, pulp & fiber productsPubChem
CEDs000744Water, Wastewater, & Sewage Treatment?Water, wastewater, and sewage treatment processes are critical for managing and mitigating pollutants in water systems.Wastewater, sanitation & biosolidsPubChem
Pathways
0 pathwaysPathway Source: PathBank

No pathways found

No metabolic pathways have been associated with this synthetic chemical

Targets
StructureProteinUniProt IDOrganismRelationshipDetails
Carbonic anhydrase 9 structureClick to view 3D structureCarbonic anhydrase 9Q16790HumansPredicted (SEA)
Prediction Confidence Score
0.102
Applicability Domain
0.231 Low confidence
Statistical Significance
0.9998
Supporting Reference Compounds
372
E-value
7783.37
Carbonic anhydrase 1 structureClick to view 3D structureCarbonic anhydrase 1P00915HumansPredicted (SEA)
Prediction Confidence Score
0.102
Applicability Domain
0.231 Low confidence
Statistical Significance
0.9998
Supporting Reference Compounds
407
E-value
7783.37
Reverse transcriptase/RNaseH structureClick to view 3D structureReverse transcriptase/RNaseHQ72547Human immunodeficiency virus 1Predicted (SEA)
Prediction Confidence Score
0.082
Applicability Domain
0.096 Low confidence
Statistical Significance
0.9997
Supporting Reference Compounds
79
E-value
7782.82
DNA polymerase delta catalytic subunit structureClick to view 3D structureDNA polymerase delta catalytic subunitP28340HumansPredicted (SEA)
Prediction Confidence Score
0.079
Applicability Domain
0.079 Low confidence
Statistical Significance
0.6951
Supporting Reference Compounds
1
E-value
5411.07
DNA-directed RNA polymerase, mitochondrial structureClick to view 3D structureDNA-directed RNA polymerase, mitochondrialO00411HumansPredicted (SEA)
Prediction Confidence Score
0.074
Applicability Domain
0.074 Low confidence
Statistical Significance
0.887
Supporting Reference Compounds
1
E-value
6905.3
Click to view 3D structureGag-Pol polyproteinQ7ZJM1Human immunodeficiency virus 1Predicted (SEA)
Prediction Confidence Score
0.065
Applicability Domain
0.231 Low confidence
Statistical Significance
0.9999
Supporting Reference Compounds
96
E-value
7784.07
Neurotrophic factor BDNF precursor form structureClick to view 3D structureNeurotrophic factor BDNF precursor formP23560HumansPredicted (SEA)
Prediction Confidence Score
0.065
Applicability Domain
0.065 Low confidence
Statistical Significance
0.4334
Supporting Reference Compounds
2
E-value
3373.99
Pleiotrophin structureClick to view 3D structurePleiotrophinP21246HumansPredicted (SEA)
Prediction Confidence Score
0.065
Applicability Domain
0.065 Low confidence
Statistical Significance
0.4334
Supporting Reference Compounds
1
E-value
3373.99
Carbonic anhydrase 2 structureClick to view 3D structureCarbonic anhydrase 2P00918HumansPredicted (SEA)
Prediction Confidence Score
0.062
Applicability Domain
0.167 Low confidence
Statistical Significance
1.0
Supporting Reference Compounds
472
E-value
7784.77
4-hydroxy-3-methylbut-2-enyl diphosphate reductase structureClick to view 3D structure4-hydroxy-3-methylbut-2-enyl diphosphate reductaseO67625Aquifex aeolicus (strain VF5)Predicted (SEA)
Prediction Confidence Score
0.061
Applicability Domain
0.061 Low confidence
Statistical Significance
0.2035
Supporting Reference Compounds
1
E-value
1583.92
Click to view 3D structureCarbonic anhydrase 5A, mitochondrialP35218HumansPredicted (SEA)
Prediction Confidence Score
0.057
Applicability Domain
0.167 Low confidence
Statistical Significance
1.0
Supporting Reference Compounds
165
E-value
7784.61
Click to view 3D structureCarbonic anhydrase 5B, mitochondrialQ9Y2D0HumansPredicted (SEA)
Prediction Confidence Score
0.056
Applicability Domain
0.167 Low confidence
Statistical Significance
0.9999
Supporting Reference Compounds
157
E-value
7784.53
Sialic acid-binding Ig-like lectin 7 structureClick to view 3D structureSialic acid-binding Ig-like lectin 7Q9Y286HumansPredicted (SEA)
Prediction Confidence Score
0.055
Applicability Domain
0.055 Low confidence
Statistical Significance
0.658
Supporting Reference Compounds
1
E-value
5122.32
DEP domain-containing mTOR-interacting protein structureClick to view 3D structureDEP domain-containing mTOR-interacting proteinQ8TB45HumansPredicted (SEA)
Prediction Confidence Score
0.054
Applicability Domain
0.065 Low confidence
Statistical Significance
0.4699
Supporting Reference Compounds
2
E-value
3658.45
Triosephosphate isomerase structureClick to view 3D structureTriosephosphate isomeraseP00939Oryctolagus cuniculusPredicted (SEA)
Prediction Confidence Score
0.05
Applicability Domain
0.067 Low confidence
Statistical Significance
0.5708
Supporting Reference Compounds
2
E-value
4444.02
Click to view 3D structurePol polyproteinQ72874Human immunodeficiency virus 1Predicted (SEA)
Prediction Confidence Score
0.048
Applicability Domain
0.096 Low confidence
Statistical Significance
0.9999
Supporting Reference Compounds
54
E-value
7784.53
Click to view 3D structureType IV secretion-like conjugative transfer relaxase protein TraIB1LRJ1Escherichia coli (strain SMS-3-5 / SECEC)Predicted (SEA)
Prediction Confidence Score
0.045
Applicability Domain
0.045 Low confidence
Statistical Significance
0.2585
Supporting Reference Compounds
1
E-value
2012.4
Click to view 3D structureSphingosine-1-phosphate lyase 1Q8CHN6Rattus norvegicusPredicted (SEA)
Prediction Confidence Score
0.043
Applicability Domain
0.043 Low confidence
Statistical Significance
0.779
Supporting Reference Compounds
1
E-value
6064.38
Click to view 3D structureHemagglutinin-neuraminidaseQ06992Human parainfluenza virus 1Predicted (SEA)
Prediction Confidence Score
0.043
Applicability Domain
0.109 Low confidence
Statistical Significance
0.9822
Supporting Reference Compounds
3
E-value
7646.66
Click to view 3D structureAldehyde dehydrogenase 1A1P51647Rattus norvegicusPredicted (SEA)
Prediction Confidence Score
0.042
Applicability Domain
0.042 Low confidence
Statistical Significance
0.9396
Supporting Reference Compounds
1
E-value
7314.87
Cyclin-dependent kinase 2 structureClick to view 3D structureCyclin-dependent kinase 2P24941HumansPredicted (SEA)
Prediction Confidence Score
0.041
Applicability Domain
0.045 Low confidence
Statistical Significance
1.0
Supporting Reference Compounds
1029
E-value
7784.69
Adenosine receptor A2a structureClick to view 3D structureAdenosine receptor A2aP29274HumansPredicted (SEA)
Prediction Confidence Score
0.041
Applicability Domain
0.068 Low confidence
Statistical Significance
1.0
Supporting Reference Compounds
303
E-value
7784.69
Luciferin 4-monooxygenase structureClick to view 3D structureLuciferin 4-monooxygenaseP08659Photinus pyralisPredicted (SEA)
Prediction Confidence Score
0.041
Applicability Domain
0.044 Low confidence
Statistical Significance
1.0
Supporting Reference Compounds
114
E-value
7784.61
Cyclin-dependent kinase 1 structureClick to view 3D structureCyclin-dependent kinase 1P06493HumansPredicted (SEA)
Prediction Confidence Score
0.041
Applicability Domain
0.045 Low confidence
Statistical Significance
1.0
Supporting Reference Compounds
715
E-value
7784.69
Click to view 3D structurePoly(ADP-ribose) glycohydrolaseO02776Bos taurusPredicted (SEA)
Prediction Confidence Score
0.04
Applicability Domain
0.067 Low confidence
Statistical Significance
0.9959
Supporting Reference Compounds
2
E-value
7753.0
Acyl-CoA-binding protein structureClick to view 3D structureAcyl-CoA-binding proteinP07108HumansKnownLead is known to bind ACBP, which is responsible for the regulation of various processes such as acyl-CoA metabolism, GABA-A/benzodiazepine receptor modulation, steroidogenesis, intestinal cholecystokinin release, and insulin secretion. (A21)
Delta-aminolevulinic acid dehydratase structureClick to view 3D structureDelta-aminolevulinic acid dehydrataseP13716HumansKnownLead inhibition of ALAD prevents the biosynthesis of heme, which is a necesssary cofactor of hemoglobin. (L21)
Ferrochelatase, mitochondrial structureClick to view 3D structureFerrochelatase, mitochondrialP22830HumansKnownLead inhibition of ferrochelatase prevents the biosynthesis of heme, which is a necesssary cofactor of hemoglobin. (L21)
Glutamate receptor ionotropic, NMDA 1 structureClick to view 3D structureGlutamate receptor ionotropic, NMDA 1Q05586HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Glutamate receptor ionotropic, NMDA 2A structureClick to view 3D structureGlutamate receptor ionotropic, NMDA 2AQ12879HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Glutamate receptor ionotropic, NMDA 2B structureClick to view 3D structureGlutamate receptor ionotropic, NMDA 2BQ13224HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Glutamate receptor ionotropic, NMDA 2C structureClick to view 3D structureGlutamate receptor ionotropic, NMDA 2CQ14957HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Glutamate receptor ionotropic, NMDA 2D structureClick to view 3D structureGlutamate receptor ionotropic, NMDA 2DO15399HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Glutamate receptor ionotropic, NMDA 3A structureClick to view 3D structureGlutamate receptor ionotropic, NMDA 3AQ8TCU5HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Click to view 3D structureGlutamate receptor ionotropic, NMDA 3BO60391HumansKnownLead exhibits competitive inhibition at the NMDA receptor, affecting neurotransmitter release. (A22)
Protein kinase C alpha type structureClick to view 3D structureProtein kinase C alpha typeP17252HumansKnownLead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Protein kinase C beta type structureClick to view 3D structureProtein kinase C beta typeP05771HumansKnownLead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Protein kinase C delta type structureClick to view 3D structureProtein kinase C delta typeQ05655HumansKnownLead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Protein kinase C epsilon type structureClick to view 3D structureProtein kinase C epsilon typeQ02156HumansKnownLead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Protein kinase C iota type structureClick to view 3D structureProtein kinase C iota typeP41743HumansKnownLead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Protein kinase C theta type structureClick to view 3D structureProtein kinase C theta typeQ04759HumansKnownLead exhibits competitive inhibition with calcium at protein kinase C, which impairs brain microvascular formation and function, as well as alters the blood-brain barrier. (L136)
Sodium/potassium-transporting ATPase subunit alpha-1 structureClick to view 3D structureSodium/potassium-transporting ATPase subunit alpha-1P05023HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structureSodium/potassium-transporting ATPase subunit alpha-2P50993HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Sodium/potassium-transporting ATPase subunit alpha-3 structureClick to view 3D structureSodium/potassium-transporting ATPase subunit alpha-3P13637HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Sodium/potassium-transporting ATPase subunit alpha-4 structureClick to view 3D structureSodium/potassium-transporting ATPase subunit alpha-4Q13733HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Sodium/potassium-transporting ATPase subunit beta-1 structureClick to view 3D structureSodium/potassium-transporting ATPase subunit beta-1P05026HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structureSodium/potassium-transporting ATPase subunit beta-2P14415HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Click to view 3D structureSodium/potassium-transporting ATPase subunit beta-3P54709HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Sodium/potassium-transporting ATPase subunit gamma structureClick to view 3D structureSodium/potassium-transporting ATPase subunit gammaP54710HumansKnownLead binds to sodium/potassium-transporting ATPases. (A24)
Concentrations
Not Available
External Links
DrugBank IDNot Available
HMDB IDNot Available
FooDB IDNot Available
Phenol Explorer IDNot Available
KNApSAcK IDNot Available
BiGG IDNot Available
BioCyc IDNot Available
METLIN IDNot Available
PDB IDNot Available
Wikipedia LinkLead(II) azide
Chemspider IDNot Available
ChEBI IDNot Available
PubChem Compound ID61600
Kegg Compound IDNot Available
YMDB IDNot Available
ECMDB IDNot Available
References
Synthesis ReferenceNot Available
MSDSNot Available
General References
  1. Needleman HL, Schell A, Bellinger D, Leviton A, Allred EN: The long-term effects of exposure to low doses of lead in childhood. An 11-year follow-up report. N Engl J Med. 1990 Jan 11;322(2):83-8. [PubMed: 2294437]
  2. Gill KD, Gupta V, Sandhir R: Ca2+/calmodulin-mediated neurotransmitter release and neurobehavioural deficits following lead exposure. Cell Biochem Funct. 2003 Dec;21(4):345-53. [PubMed: 14624473]
  3. Hashemzadeh-Gargari H, Guilarte TR: Divalent cations modulate N-methyl-D-aspartate receptor function at the glycine site. J Pharmacol Exp Ther. 1999 Sep;290(3):1356-62. [PubMed: 10454514]
  4. Wikipedia. Lead poisoning. Last Updated 3 March 2009. - http://en.wikipedia.org/wiki/Lead_poisoning
  5. ATSDR - Agency for Toxic Substances and Disease Registry (2001). Minimal Risk Levels (MRLs) for Hazardous Substances. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). - http://www.atsdr.cdc.gov/mrls/
  6. International Agency for Research on Cancer (2014). IARC Monographs on the Evaluation of Carcinogenic Risks to Humans. - http://monographs.iarc.fr/index.php
  7. ATSDR - Agency for Toxic Substances and Disease Registry (2007). Toxicological profile for lead. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). - http://www.atsdr.cdc.gov/toxprofiles/tp13.html
  8. Wikipedia. Lead(II) azide. Last Updated 26 May 2009. - http://en.wikipedia.org/wiki/Lead_azide
  9. Ellenhorn MJ and Barceloux DG (1988). Diagnosis and treatment of human poisoning. Medical Toxicology. New York, New York: Elsevier Science Publishing Company, Inc.
  10. Baselt RC (2000). Disposition of Toxic Drugs and Chemicals in Man, 5th ed. Foster City, CA: Chemical Toxicology Institute.