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Channel blocker
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Tetrodotoxin, an example of a channel block molecule.
A channel blocker is the biological mechanism in which a particular molecule is used to prevent the opening of ion channels in order to produce a physiological response in a cell. Channel blocking is conducted by different types of molecules, such as cations, anions, amino acids, and other chemicals. These blockers act as ion channel antagonists, preventing the response that is normally provided by the opening of the channel.
Ion channels permit the selective passage of ions through cell membranes by utilizing proteins that function as pores, which allow for the passage of electrical charge in and out of the cell.[1] These ion channels are most often gated, meaning they require a specific stimulus to cause the channel to open and close. These ion channel types regulate the flow of charged ions across the membrane and therefore mediate membrane potential of the cell.
Molecules that act as channel blockers are important in the field of pharmacology, as a large portion of drug design is the use of ion channel antagonists in regulating physiological response. The specificity of channel block molecules on certain channels makes it a valuable tool in the treatment of numerous disorders.[2][3]
Contents
1 Background
1.1 Ion channels
1.2 Identity
2 Physiology
2.1 Receptor antagonist
2.2 Specificity of molecules
2.3 Kinetics
3 Clinical significance
3.1 Therapeutic uses
3.1.1 Alzheimer's disease
3.1.2 Cystic fibrosis
3.2 Pharmacology
3.2.1 Anesthetics
3.2.2 Alzheimer's disease
3.2.3 CFTR channel dysfunction
4 Types
5 See also
6 References
Background[edit]
Ion channels[edit]
Main article: Ion channel
Play media
Example of voltage-dependent potassium ion channel in relation to changing ion concentrations
To comprehend the mechanism of channel blockers, it is critical to understand the composition of ion channels. Their main function is to contribute to the resting membrane potential of a cell via the flow of ions through a cell membrane. To accomplish this task, ions must be able to cross the hydrophobic region of a lipid bilayer membrane, an unfavorable process. To assist in ion transport, ion channels form a hydrophilic pore through the membrane which allows for the usually unfavorable transfer of hydrophilic molecules.[4] Various ion channels have varying mechanisms of function. They include:
voltage-gated ion channels
Ion channels that are activated by changes in membrane potential
ligand-gated ion channel
Ion channels mediated by the binding of small molecules to the channel protein
mechanosensitive ion channels
Ion channels that respond to stretch, vibration, or temperature changes
light-gated ion channels
Ion channels that open or close in response to light
Molecules that act as ion channel blockers can be used in relation to any of these various channels. For example, sodium channels, which are essential to the production of action potentials, are affected by many different toxins. Tetrodotoxin (TTX), a toxin found in pufferfish, completely blocks sodium ion transportation by blocking the selectivity filter region of the channel.[5] Much of the structure of the pores of ion channels has been elucidated from studies that used toxins to inhibit channel function.[6][7][8]
Identity[edit]
Tools such as X-ray crystallography and electrophysiology have been essential in locating the binding sites of open channel block molecules. By studying the biological and chemical makeup of ion channels, researchers can determine the makeup of the molecules that bind to certain regions. X-ray crystallography provides a structural image of the channel and molecule in question.[9] Determining the hydrophobicity of channel domains through hydrophobicity plots also provides clues to the chemical makeup of the molecule and why it binds to a certain region. For example, if a protein binds to a hydrophobic region of the channel (and therefore, has a transmembrane region), the molecule in question might be composed of the amino acids alanine, leucine, or phenylalanine, as they are all hydrophobic themselves.[10] Electrophysiology is also an important tool in identifying channel structure, as analyzing the ionic factors that lead to channel activation can be critical to understanding the inhibiting actions of open channel block molecules.[3][9]
Physiology[edit]
This diagram of a NMDA receptor shows the binding points for a diverse array of molecules which can affect the receptor function. Legend: 1. Cell membrane 2. Channel blocked by Mg2+ at the block site (3) 3. Block site by Mg2+ 4. Hallucinogen compounds binding site 5. Binding site for Zn2+ 6. Binding site for agonists(glutamate) and/or antagonist ligands(APV) 7. Glycosylation sites 8. Proton biding sites 9. Glycine binding sites 10. Polyamines binding site 11. Extracellular space 12. Intracellular space
Receptor antagonist[edit]
Channel blockers are antagonists for the channels required to produce normal physiological function in cells. Many channels have binding spots for regulatory elements which can promote or repress normal function depending on the requirements within the cell and organism. The normal function of agonist binding is the generation of cellular changes leading to various downstream effects; these effects range from altering membrane potential to initiation of signaling cascades.[11] Conversely, when open channel blockers bind to the cell they prevent the normal function of agonist binding. For example, voltage-gated channels open and close based on membrane potential and are critical in the generation of action potentials by their allowance of ions to flow down established gradients. However, open channels blockers can bind to these channels to prevent ions from flowing, thus inhibiting the initiation of an action potential.[12]
Specificity of molecules[edit]
Many different organic compounds can act as channel blockers despite channel specificity. Channels have evolved structures that, due to their membrane spanning regions, can discriminate between various ions or compounds. For example, some objects are too large for to fit into channels that are structurally specified to transport smaller objects, such as a potassium ion attempting to fit into a sodium channel. Conversely, some objects are too small to be properly stabilized by certain channel pores, such as a sodium ion attempting to pass through a potassium channel.[11][13] In both cases, channel flux is not permitted. However, as long as a particular compound possesses adequate chemical affinity to a channel, that compound may be able to bind and block the channel pore. For example, TTX can bind and inactivate voltage-gated sodium channels, despite the fact that TTX is much larger and chemically different than sodium ions. Given the disparities in size and chemical properties between TTX and a sodium ion, this is an example of structure being used to block usually specific channels. [14]
Kinetics[edit]
A channel block can be induced by many different types of organic compounds as long as they can bind to some portion of the target channel's pore. The kinetics of channel blockers are primarily understood though their use as anesthetics. Local anesthetics work by inducing a phasic block state in the targeted neurons.[13] Initially, open channel blockers do not effectively prevent action potentials, as few channels are blocked and the blocker itself can be released from the channel either quickly or slowly depending on its characteristics. However, phasic blocks occur as repeated depolarization increases blockers’ affinity for channels in the neuron.The combination of an increase in available channels and the change in channel conformation to increase blocker binding affinity are responsible for this action.[13][15][16]
Clinical significance[edit]
Therapeutic uses[edit]
Various neurodegenerative diseases have been associated with excessive NMDA receptor activation meant to mediate calcium dependent neurotoxicity. Researchers have examined many different NMDA antagonists and their therapeutic efficacy, none of which have concluded to be both safe and effective.[17] For years, researchers have been investigating the effects of an open channel block, memantine, as a treatment option for neurotoxicity. They hypothesized that the faster blocking and unblocking rates, and overall kinetics, of memantine could be the underlying reason for the clinical tolerance.[17][3] As an uncompetitive antagonist, memantine should bring NMDA levels close to normal despite high glutamate concentration. Based on this information, researchers speculated that some day memantine could be used as an open channel block to prevent increasing glutamate levels associated with neurotoxicity with little to no side effects compared to other treatment options.[17]
Alzheimer's disease[edit]
Alzheimer's disease, a specific neurodegenerative disorder, is linked to glutaminergic neurotransmission interruptions that are believed to result in the staple cognitive symptoms of Alzheimer's.[18][2][3] Researchers suggest that noncompetitive NMDA receptor agonists can be used to aid in the management of these symptoms without producing severe side effects.[18] As one of the only drugs approved for Alzheimer's treatment, memantine has been shown to allow excitatory post synaptic currents to remain unaffected while decreasing the incidence and amplitude of inhibitory post-synatpic currents.[19] Evidence supports the hypothesis that both the strong voltage dependency and fast kinetics of memantine may be responsible for the decreased side effects and cognitive progress.[20]
Cystic fibrosis[edit]
Cystic fibrosis is a progressive, genetic disease that is linked to CF transmembrane regulator (CFTR) dysfunction.[21] Blockage of this channel by certain cytoplasmic, negatively-charged substances results in reduced chloride ion and bicarbonate anion transport, as well as reduced fluid and salt secretion. This results in a buildup of thick mucus, which is characteristic of cystic fibrosis.[21]
Pharmacology[edit]
Anesthetics[edit]
Channel blockers are essential in the field of anesthetics. Sodium channel inhibitors are used as both antiepileptics and antiarrhythmics, as they can inhibit the hyper-excitable tissues in a patient.[22] Introducing specific sodium channel blockers into a tissue allows for the preferential binding of the blocker to sodium channels, which results in an ultimate inhibition of the flow of sodium into the tissue. Over time, this mechanism leads to an overall decrease in tissue excitation. Prolonged hyperpolarization interrupts normal channel recovery and allows for constant inhibition, providing dynamic control of the anesthetics in a given setting.[22]
Alzheimer's disease[edit]
Excessive exposure to glutamate leads to neurotoxicity in patients with Alzheimer's disease. Specifically, over-activation of NMDA-type glutamate receptors have been linked to neural cell excitotoxicity and cell death.[18][2] A potential solution to this is a decrease in NMDA receptor activity, without interfering so drastically as to cause clinical side effects.[23]
In an attempt to prevent further neurodegeneration, researchers have used memantine, an open channel block, as a form of treatment. Thus far, the use of memantine in patients with Alzheimer's disease quickly results in clinical progress across many different symptoms. Memantine is thought to work effectively due to its ability to quickly modify its kinetics, which prevents buildup in the channel and allows normal synaptic transmission. Other channel blockers have been found to block all NMDA receptor activity, leading to adverse clinical side effects.[3]
CFTR channel dysfunction[edit]
Cystic Fibrosis transmembrane regulators (CFTRs) function in chloride ion, bicarbonate anion, and fluid transport.[24] They are expressed primarily in apical membranes of epithelial cells in respiratory, pancreatic, gastrointestinal, and reproductive tissues.[21][24] Abnormally-elevated CFTR function results in excessive fluid secretion. High-affinity CFTR inhibitors, such as CFTRinh-172 and GlyH-101, have been shown to be efficient in treatment of secretory diarrheas.[25][26] Theoretically, CFTR channel blockers may also be useful as male contraceptives. CFTR channels mediate bicarbonate anion entry which is essential for sperm capacitation.[27]
Various types of substances have been known to block CFTR chloride ion channels. Some of the best-known and studied substances include sulfonylureas, arylaminobenzenoates, and disulfonic stilbenes.[28][29][30] These blockers are side-dependent as they enter the pore exclusively from the cytoplasmic side, voltage-dependent as hyperpolarized membrane potentials favor negatively-charged substance entry into the pore from the cytoplasmic side, and chloride ion concentration-dependent as high extracellular chloride ions electrostatically repel negatively-charged blockers back into the cytoplasm.[31]
Types[edit]
There are several different major classes of channel blockers, including:
Calcium (Ca2+) channel blockers
Chloride (Cl−) channel blockers
Potassium (K+) channel blockers
Sodium (Na+) channel blockers
The following types which act on ligand-gated ion channels (LGICs) via binding to their pore also exist:
5-HT3 receptor antagonists
GABAA receptor antagonists
nACh receptor antagonists
NMDA receptor antagonists
Channel blockers are also known to act at AMPA receptors, Glycine receptors, Kainate receptors, P2X receptors and Zinc (Zn2+)-activated channels. The type of inhibition mediated by channel blockers may be referred to as noncompetitive or uncompetitive.
See also[edit]
Ion channel
Channel opener
References[edit]
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^ Jump up to: a b c Kocahan S, Doğan Z (February 2017). "Mechanisms of Alzheimer's Disease Pathogenesis and Prevention: The Brain, Neural Pathology, N-methyl-D-aspartate Receptors, Tau Protein and Other Risk Factors". Clinical Psychopharmacology and Neuroscience. 15 (1): 1–8. doi:10.9758/cpn.2017.15.1.1. PMC 5290713. PMID 28138104.
^ Jump up to: a b c d e Lipton SA (January 2004). "Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults". NeuroRx. Neuroprotection. 1 (1): 101–10. doi:10.1602/neurorx.1.1.101. PMC 534915. PMID 15717010.
Jump up ^ Ahern CA, Payandeh J, Bosmans F, Chanda B (January 2016). "The hitchhiker's guide to the voltage-gated sodium channel galaxy". The Journal of General Physiology. 147 (1): 1–24. doi:10.1085/jgp.201511492. PMC 4692491. PMID 26712848.
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Jump up ^ Miller C (December 1988). "Competition for block of a Ca2(+)-activated K+ channel by charybdotoxin and tetraethylammonium". Neuron. 1 (10): 1003–6. doi:10.1016/0896-6273(88)90157-2. PMID 2483092.
Jump up ^ Aiyar J, Withka JM, Rizzi JP, Singleton DH, Andrews GC, Lin W, Boyd J, Hanson DC, Simon M, Dethlefs B (November 1995). "Topology of the pore-region of a K+ channel revealed by the NMR-derived structures of scorpion toxins". Neuron. 15 (5): 1169–81. doi:10.1016/0896-6273(95)90104-3. PMID 7576659.
^ Jump up to: a b Findeisen F, Campiglio M, Jo H, Abderemane-Ali F, Rumpf CH, Pope L, Rossen ND, Flucher BE, DeGrado WF, Minor DL (March 2017). "Stapled Voltage-Gated Calcium Channel (CaV) α-Interaction Domain (AID) Peptides Act As Selective Protein-Protein Interaction Inhibitors of CaV Function". ACS Chemical Neuroscience. 8: 1313–1326. doi:10.1021/acschemneuro.6b00454. PMC 5481814. PMID 28278376.
Jump up ^ Phoenix DA, Harris F (2002-01-01). "The hydrophobic moment and its use in the classification of amphiphilic structures (review)". Molecular Membrane Biology. 19 (1): 1–10. doi:10.1080/09687680110103631. PMID 11989818.
^ Jump up to: a b Jackson MB (February 2010). "Open channel block and beyond". The Journal of Physiology. 588 (Pt 4): 553–4. doi:10.1113/jphysiol.2009.183210. PMC 2828128. PMID 20173077.
Jump up ^ Ahern CA, Payandeh J, Bosmans F, Chanda B (January 2016). "The hitchhiker's guide to the voltage-gated sodium channel galaxy". The Journal of General Physiology. 147 (1): 1–24. doi:10.1085/jgp.201511492. PMC 4692491. PMID 26712848.
^ Jump up to: a b c Butterworth JF, Strichartz GR (April 1990). "Molecular mechanisms of local anesthesia: a review". Anesthesiology. 72 (4): 711–34. doi:10.1097/00000542-199004000-00022. PMID 2157353.
Jump up ^ Evans MH (September 1969). "Mechanism of saxitoxin and tetrodotoxin poisoning". British Medical Bulletin. 25 (3): 263–7. doi:10.1093/oxfordjournals.bmb.a070715. PMID 5812102.
Jump up ^ Mert T, Gunes Y, Guven M, Gunay I, Ozcengiz D (March 2002). "Comparison of nerve conduction blocks by an opioid and a local anesthetic". European Journal of Pharmacology. 439 (1–3): 77–81. doi:10.1016/S0014-2999(02)01368-7. PMID 11937095.
Jump up ^ Mitolo-Chieppa D, Carratu MR (May 1983). "Anaesthetic drugs: electrophysiological bases of their conduction blocking effect". Pharmacological Research Communications. 15 (5): 439–50. doi:10.1016/s0031-6989(83)80064-2. PMID 6351107.
^ Jump up to: a b c Chen HS, Pellegrini JW, Aggarwal SK, Lei SZ, Warach S, Jensen FE, Lipton SA (November 1992). "Open-channel block of N-methyl-D-aspartate (NMDA) responses by memantine: therapeutic advantage against NMDA receptor-mediated neurotoxicity". The Journal of Neuroscience. 12 (11): 4427–36. PMID 1432103.
^ Jump up to: a b c Müller WE, Mutschler E, Riederer P (July 1995). "Noncompetitive NMDA receptor antagonists with fast open-channel blocking kinetics and strong voltage-dependency as potential therapeutic agents for Alzheimer's dementia". Pharmacopsychiatry. 28 (4): 113–24. doi:10.1055/s-2007-979603. PMID 7491365.
Jump up ^ Povysheva NV, Johnson JW (December 2016). "Effects of memantine on the excitation-inhibition balance in prefrontal cortex". Neurobiology of Disease. 96: 75–83. doi:10.1016/j.nbd.2016.08.006. PMC 5102806. PMID 27546057.
Jump up ^ Dominguez, Evangelyn; Chin, Ting-Yu; Chen, Chih-Ping; Wu, Tzong-Yuan (2011-12-01). "Management of moderate to severe Alzheimer's disease: Focus on memantine". Taiwanese Journal of Obstetrics and Gynecology. 50 (4): 415–423. doi:10.1016/j.tjog.2011.10.004. ISSN 1028-4559. PMID 22212311.
^ Jump up to: a b c Lubamba B, Dhooghe B, Noel S, Leal T (October 2012). "Cystic fibrosis: insight into CFTR pathophysiology and pharmacotherapy". Clinical Biochemistry. 45 (15): 1132–44. doi:10.1016/j.clinbiochem.2012.05.034. PMID 22698459.
^ Jump up to: a b Ramos E, O'leary ME (October 2004). "State-dependent trapping of flecainide in the cardiac sodium channel". The Journal of Physiology. 560 (Pt 1): 37–49. doi:10.1113/jphysiol.2004.065003. PMC 1665201. PMID 15272045.
Jump up ^ Lipton SA (May 2007). "Pathologically-activated therapeutics for neuroprotection: mechanism of NMDA receptor block by memantine and S-nitrosylation". Current Drug Targets. 8 (5): 621–32. doi:10.2174/138945007780618472. PMID 17504105.
^ Jump up to: a b Frizzell RA, Hanrahan JW (June 2012). "Physiology of epithelial chloride and fluid secretion". Cold Spring Harbor Perspectives in Medicine. 2 (6): a009563. doi:10.1101/cshperspect.a009563. PMC 3367533. PMID 22675668.
Jump up ^ Muanprasat C, Sonawane ND, Salinas D, Taddei A, Galietta LJ, Verkman AS (August 2004). "Discovery of glycine hydrazide pore-occluding CFTR inhibitors: mechanism, structure-activity analysis, and in vivo efficacy". The Journal of General Physiology. 124 (2): 125–37. doi:10.1085/jgp.200409059. PMC 2229623. PMID 15277574.
Jump up ^ Ma T, Thiagarajah JR, Yang H, Sonawane ND, Folli C, Galietta LJ, Verkman AS (December 2002). "Thiazolidinone CFTR inhibitor identified by high-throughput screening blocks cholera toxin-induced intestinal fluid secretion". The Journal of Clinical Investigation. 110 (11): 1651–8. doi:10.1172/JCI16112. PMC 151633. PMID 12464670.
Jump up ^ Chen H, Ruan YC, Xu WM, Chen J, Chan HC (2012-11-01). "Regulation of male fertility by CFTR and implications in male infertility". Human Reproduction Update. 18 (6): 703–13. doi:10.1093/humupd/dms027. PMID 22709980.
Jump up ^ Schultz BD, DeRoos AD, Venglarik CJ, Singh AK, Frizzell RA, Bridges RJ (August 1996). "Glibenclamide blockade of CFTR chloride channels". The American Journal of Physiology. 271 (2 Pt 1): L192–200. doi:10.1152/ajplung.1996.271.2.L192. PMID 8770056.
Jump up ^ Zhang ZR, Zeltwanger S, McCarty NA (May 2000). "Direct comparison of NPPB and DPC as probes of CFTR expressed in Xenopus oocytes". The Journal of Membrane Biology. 175 (1): 35–52. doi:10.1007/s002320001053. PMID 10811966.
Jump up ^ Linsdell P, Hanrahan JW (November 1996). "Disulphonic stilbene block of cystic fibrosis transmembrane conductance regulator Cl- channels expressed in a mammalian cell line and its regulation by a critical pore residue". The Journal of Physiology. 496 (Pt 3): 687–93. doi:10.1113/jphysiol.1996.sp021719. PMC 1160856. PMID 8930836.
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show
v
t
e
Pharmacomodulation
Types
♦ Enzyme: Inducer
Inhibitor
♦ Ion channel: Opener
Blocker
♦ Receptor: Agonist
Partial agonist
Antagonist
Inverse agonist
Positive allosteric modulator (PAM)
Negative allosteric modulator (NAM)
♦ Transporter [Reuptake vs Efflux]: Enhancer (RE)
Inhibitor (RI)
Releaser (RA)
♦ Miscellaneous: Precursor
Cofactor
Classes
Enzyme
see Enzyme inhibition
Ion channel
Calcium channel blocker (CCB)
Potassium channel blocker (PCB)
Sodium channel blocker (SCB)
Potassium channel opener (PCO)
Receptor &
transporter
BA/M
Adrenergic
Adrenergic receptor agonist (α
β (1
2))
Adrenergic receptor antagonist (α (1
2)
β)
Norepinephrine reuptake inhibitor (NRI)
Dopaminergic
Dopamine receptor agonist
Dopamine receptor antagonist
Dopamine reuptake inhibitor (DRI)
Histaminergic
Histamine receptor agonist
Histamine receptor antagonist (H1
H2
H3)
Serotonergic
Serotonin receptor agonist
Serotonin receptor antagonist (5-HT3)
Serotonin reuptake inhibitor (SRI)
AA
GABAergic
GABA receptor agonist
GABA receptor antagonist
GABA reuptake inhibitor (GRI)
Glutamatergic
Glutamate receptor agonist (AMPA)
Glutamate receptor antagonist (NMDA)
Glutamate reuptake inhibitor
Cholinergic
Acetylcholine receptor agonist (Muscarinic
Nicotinic)
Acetylcholine receptor antagonist (Muscarinic
Nicotinic (Ganglionic
Muscular))
Cannabinoidergic
Cannabinoid receptor agonist
Cannabinoid receptor antagonist
Endocannabinoid enhancer (eCBE)
Endocannabinoid reuptake inhibitor (eCBRI)
Opioidergic
Opioid modulator
Opioid receptor agonist
Opioid receptor antagonist
Enkephalinase inhibitor
Other
Adenosine reuptake inhibitor (AdoRI)
Angiotensin II receptor antagonist
Endothelin receptor antagonist
NK1 receptor antagonist
Vasopressin receptor antagonist
Miscellaneous
Cofactor (see Enzyme cofactors)
Precursor (see Amino acids)
show
v
t
e
Ion channel modulators
Calcium
VDCCs
Blockers
L-type-selective: Dihydropyridines: Amlodipine
Aranidipine
Azelnidipine
Barnidipine
Clevidipine
Cronidipine
Darodipine
Dexniguldipine
Elgodipine
Elnadipine
Felodipine
Flordipine
Furnidipine
Iganidipine
Isradipine
Lacidipine
Lemildipine
Lercanidipine
Levamlodipine
Levniguldipine
Manidipine
Mepirodipine
Mesudipine
Nicardipine
Nifedipine
Niguldipine
Niludipine
Nilvadipine
Nimodipine
Nisoldipine
Nitrendipine
Olradipine
Oxodipine
Palonidipine
Pranidipine
Ryodipine (riodipine)
Sagandipine
Sornidipine
Teludipine
Tiamdipine
Trombodipine
Vatanidipine; Diltiazem derivatives: Clentiazem
Diltiazem
Iprotiazem
Nictiazem
Siratiazem; Phenylalkylamines: Anipamil
Dagapamil
Devapamil
Dexverapamil
Emopamil
Etripamil
Falipamil
Gallopamil
Levemopamil
Nexopamil
Norverapamil
Ronipamil
Tiapamil
Verapamil; Others: AH-1058
Brinazarone
Budiodarone
Celivarone
Cyproheptadine
Dronedarone
Fantofarone
SR-33805
Tetrahydropalmatine
N-type-selective: ω-Conotoxins
ω-Conotoxin GVIA
Caroverine
Huwentoxin XVI
Leconotide (ω-conotoxin CVID)
PD-173212
Ralfinamide
Safinamide
Z160
Ziconotide (ω-conotoxin MVIIA)
P-type-selective: ω-Agatoxin IVA
ω-Agatoxin IVB
R-type-selective: SNX-482
T-type-selective: ABT-639
ML-218
Niflumic acid
NNC 55-0396
ProTx I
Z944
Zonisamide
Non-selective: ω-Agatoxin TK
ω-Conotoxin MVIIC
Benidipine
Bepridil
Cilnidipine
Cinnarizine
Dotarizine
Efonidipine
Flunarizine
Lamotrigine
Levetiracetam
Lomerizine
Loperamide
Mibefradil
NP078585
Ruthenium red
TROX-1
α2δ subunit-selective (gabapentinoids): 4-Methylpregabalin
Arbaclofen
Arbaclofen placarbil
Atagabalin
Baclofen
Gabapentin
Gabapentin enacarbil
Imagabalin
Mirogabalin
PD-200,347
PD-217,014
PD-299,685
Phenibut
Pregabalin
Others/unsorted: Bencyclane
Berbamine
Bevantolol
Canadine
Carboxyamidotriazole
Cycleanine
Dauricine
Dimeditiapramine
Diproteverine
Enpiperate
Eperisone
Elpetrigine
Ethadione
Ethanol (alcohol)
Ethosuximide
Fasudil
Fendiline
Fostedil
Imepitoin
JTV-519
Lidoflazine
Magnesium
Manoalide
Mesuximide
Monatepil
Naftopidil
Ochratoxin A
Osthol
Otilonium bromide
Paramethadione
Phensuximide
Pinaverium bromide
Prenylamine
Rhynchophylline
Sesamodil
Silperisone
Sipatrigine
Terodiline
Tetrandrine
Tolperisone
Trimethadione
Valperinol
Activators
L-type-selective: Bay K8644
Potassium
VGKCs
Blockers
3,4-Diaminopyridine (amifampridine)
4-Aminopyridine (fampridine/dalfampridine)
Adekalant
Almokalant
Amiodarone
Azimilide
Bretylium
Bunaftine
Charybdotoxin
Clamikalant
Conotoxins
Dalazatide
Dendrotoxin
Dofetilide
Dronedarone
E-4031
Hanatoxin
HgeTx1
HsTx1
Ibutilide
Inakalant
Kaliotoxin
Linopirdine
Lolitrem B
Maurotoxin
Nifekalant
Notoxin
Paxilline
Pinokalant
Quinidine
ShK-186
Sotalol
Tedisamil
Terikalant
Tetraethylammonium
Vernakalant
hERG (KCNH2, Kv11.1)-specific: Ajmaline
Amiodarone
AmmTX3
Astemizole
Azaspiracid
AZD1305
Azimilide
Bedaquiline
BeKm-1
BmTx3
BRL-32872
Chlorpromazine
Cisapride
Clarithromycin
Darifenacin
Dextropropoxyphene
Diallyl trisulfide
Domperidone
E-4031
Ergtoxins
Erythromycin
Gigactonine
Haloperidol
Ketoconazole
Norpropoxyphene
Orphenadrine
Pimozide
PNU-282,987
Promethazine
Quinidine
Ranolazine
Roxithromycin
Sertindole
Solifenacin
Tamulotoxin
Terodiline
Terfenadine
Thioridazine
Tolterodine
Vanoxerine
Vernakalant
KCNQ (Kv7)-specific: Linopirdine
XE-991
Spooky toxin (SsTx)
Activators
KCNQ (Kv7)-specific: Flupirtine
Retigabine
IRKs
Blockers
KATP-specific: Acetohexamide
Carbutamide
Chlorpropamide
Glibenclamide (glyburide)
Glibornuride
Glicaramide
Gliclazide
Glimepiride
Glipizide
Gliquidone
Glisoxepide
Glyclopyramide
Glycyclamide
Metahexamide
Mitiglinide
Nateglinide
Repaglinide
Tolazamide
Tolbutamide
GIRK-specific: Barium
Caramiphen
Cloperastine
Clozapine
Dextromethorphan
Ethosuximide
Ifenprodil
Tertiapin
Tipepidine
Activators
KATP-specific: Aprikalim
Bimakalim
Cromakalim
Diazoxide
Emakalim
Levcromakalim
Mazokalim
Minoxidil
Naminidil
Nicorandil
Pinacidil
Rilmakalim
Sarakalim
GIRK-specific: ML-297 (VU0456810)
KCa
Blockers
BKCa-specific: Ethanol (alcohol)
GAL-021
Activators
BKCa-specific: Flufenamic acid
Meclofenamic acid
Niflumic acid
Nimesulide
Rottlerin (mallotoxin)
Tolfenamic acid
K2Ps
Blockers
12-O-Tetradecanoylphorbol-13-acetate
Arachidonic acid
Fluoxetine
Norfluoxetine
Activators
Riluzole
Sodium
VGSCs
Blockers
Antianginals: Ranolazine
Antiarrhythmics (class I): Ajmaline
Aprindine
Disopyramide
Dronedarone
Encainide
Flecainide
Lidocaine
Lorajmine
Lorcainide
Mexiletine
Moricizine
Pilsicainide
Prajmaline
Procainamide
Propafenone
Quinidine
Sparteine
Tocainide
Anticonvulsants: Acetylpheneturide
Carbamazepine
Cenobamate
Chlorphenacemide
Elpetrigine
Eslicarbazepine acetate
Ethotoin
Fosphenytoin
Lacosamide
Licarbazepine
Mephenytoin
Oxcarbazepine
Oxitriptyline
Phenacemide
Pheneturide
Phenytoin
Rufinamide
Sipatrigine
Topiramate
Sodium valproate
Valnoctamide
Valproate pivoxil
Valproate semisodium
Valproic acid
Valpromide
Zonisamide
Local anesthetics: pFBT
Amylocaine
Articaine
Benzocaine
Bupivacaine (Levobupivacaine, Ropivacaine)
Butacaine
Butamben
Chloroprocaine
Cinchocaine
Cocaine
Cyclomethycaine
Dimethocaine
Diphenhydramine
Etidocaine
Hexylcaine
Iontocaine
Lidocaine
Mepivacaine
Meprylcaine
Metabutoxycaine
Orthocaine
Piperocaine
Prilocaine
Procaine
Propoxycaine
Proxymetacaine
Risocaine
Tetracaine
Trimecaine
Analgesics: AZD-3161
DSP-2230
Funapide
GDC-0276
NKTR-171
PF-04531083
PF-05089771
Ralfinamide
Raxatrigine
RG7893 (GDC-0287)
Toxins: Conotoxins
Neosaxitoxin
Saxitoxin
Tetrodotoxin
Zetekitoxin AB
Others: Buprenorphine
Evenamide
Menthol (mint)
Safinamide
Tricyclic antidepressants
Activators
Aconitine
Atracotoxins (Robustoxin, Versutoxin)
Batrachotoxin
Ciguatoxins
Grayanotoxins
Poneratoxin
ENaC
Blockers
Amiloride
Benzamil
Triamterene
Activators
Solnatide
ASICs
Blockers
A-317567
Amiloride
Aspirin
Ibuprofen
PcTX1
Chloride
CaCCs
Blockers
Crofelemer
DIDS
Ethacrynic acid
Flufenamic acid
Fluoxetine
Furosemide
Glibenclamide
Mefloquine
Mibefradil
Niflumic acid
Activators
Carbachol
CFTR
Blockers
Glibenclamide
Lonidamine
Piretanide
Activators
1,7-Phenanthroline
1,10-Phenanthroline
4,7-Phenanthroline
7,8-Benzoquinoline
Ivacaftor
Phenanthridine
Unsorted
Blockers
Bumetanide
Flufenamic acid
Meclofenamic acid
Mefenamic acid
Mepacrine
Niflumic acid
Talniflumate
Tolfenamic acid
Trifluoperazine
Others
TRPs
See here instead.
See also: Receptor/signaling modulators • Transient receptor potential channel modulators
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text:
Badminton at the 2018 Commonwealth Games – Women's singles
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Badminton – Women's singles
at the 2018 Commonwealth Games
Venue
Carrara Sports and Leisure Centre, Gold Coast
Dates
10 – 15 April 2018
Medalists
Saina Nehwal India
P. V. Sindhu India
Kirsty Gilmour Scotland
← 2014
2022 →
Badminton at the
2018 Commonwealth Games
Singles
men women
Doubles
men women
Mixed
doubles team
v
t
e
The women's singles badminton event at the 2018 Commonwealth Games was held from 10 to 15 April 2018 at the Carrara Sports and Leisure Centre on the Gold Coast, Australia.[1] The defending gold medalist was Michelle Li of Canada.
The athletes were drawn into an elimination stage draw. Once a player lost a match, she will no longer be able to compete. Each match was contested as the best of three games.
The draw for the competition was done on 2 April 2018.[2]
Contents
1 Seeds
2 Results
2.1 Finals
2.2 Top Half
2.2.1 Section 1
2.2.2 Section 2
2.3 Bottom Half
2.3.1 Section 3
2.3.2 Section 4
3 References
Seeds[edit]
The seeds for the tournament were:[3]
01. P. V. Sindhu (IND) (Silver medal)
02. Saina Nehwal (IND) (Gold medal)
03. Michelle Li (CAN) (Fourth place)
04. Kirsty Gilmour (SCO) (Bronze medal)
05. Soniia Cheah (MAS) (Quarterfinals)
06. Rachel Honderich (CAN) (Quarterfinals)
07. Brittney Tam (CAN) (Quarterfinals)
08. Gadde Ruthvika Shivani (IND) (Quarterfinals)
Click on the seed number of a player to go to their draw section.
Results[edit]
Finals[edit]
Semifinals Final
1 P. V. Sindhu (IND) 21 21
3 Michelle Li (CAN) 18 8
1 P. V. Sindhu (IND) 18 21
2 Saina Nehwal (IND) 21 23
4 Kirsty Gilmour (SCO) 14 21 17
2 Saina Nehwal (IND) 21 18 21 Bronze medal match
3 Michelle Li (CAN) 11 16
4 Kirsty Gilmour (SCO) 21 21
Top Half[edit]
Section 1[edit]
Round of 64 Round of 32 Round of 16 Quarterfinals
1 P. V. Sindhu (IND) 21 21
Andra Whiteside (FIJ) 6 3
1 P. V. Sindhu (IND) 21 21
Wendy Chen Hsuan-yu (AUS) 15 9
Zoe Morris (FAI) 3 2
Eyram Migbodzi (GHA) 2 3 Wendy Chen Hsuan-yu (AUS) 21 21
Wendy Chen Hsuan-yu (AUS) 21 21 1 P. V. Sindhu (IND) 21 21
7 Brittney Tam (CAN) 14 17
7 Brittney Tam (CAN) 21 21
Palwasha Bashir (PAK) 18 12 Nicki Chan-Lam (MRI) 14 13
Nicki Chan-Lam (MRI) 21 21 7 Brittney Tam (CAN) 21 16 21
Kate Foo Kune (MRI) 16 21 16
Kate Foo Kune (MRI) 21 21
Hasini Ambalangodage (SRI) 21 21 Hasini Ambalangodage (SRI) 12 12
Emily Temple Redshaw (JER) 18 11
Section 2[edit]
Round of 64 Round of 32 Round of 16 Quarterfinals
3 Michelle Li (CAN) 21 21
Everlyn Siamupangila (ZAM) 11 9 Kimberley Clague (IOM) 7 7
Kimberley Clague (IOM) 21 21 3 Michelle Li (CAN) 21 21
Katherine Wynter (JAM) 10 7
Aisha Nakiyemba (UGA) 18 15
Katherine Wynter (JAM) 21 21 Katherine Wynter (JAM) 21 21
Chloe le Tissier (GUE) 18 16 3 Michelle Li (CAN) 21 21
5 Soniia Cheah (MAS) 12 19
5 Soniia Cheah (MAS) 21 21
Rachael Darragh (NIR) 21 21 Rachael Darragh (NIR) 5 12
Stella Ngadjui (CMR) 6 3 5 Soniia Cheah (MAS) 21 21
Grace Chua Hui Zen (SGP) 11 12
Michelle Butler-Emmett (RSA) 5 12
Cheryl March (FAI) 1 0 Grace Chua Hui Zen (SGP) 21 21
Grace Chua Hui Zen (SGP) 21 21
Bottom Half[edit]
Section 3[edit]
Round of 64 Round of 32 Round of 16 Quarterfinals
Karyn Gibson (FIJ) 6 6
Yeo Jia Min (SGP) 21 21 Yeo Jia Min (SGP) w / o
Shamim Bangi (UGA)
Yeo Jia Min (SGP) 10 23 10
Grace Atipaka (GHA) 21 21 8 Gadde Ruthvika Shivani (IND) 21 21 21
Juliette Ah-Wan (SEY) 17 19 Grace Atipaka (GHA) 5 7
8 Gadde Ruthvika Shivani (IND) 21 21
8 Gadde Ruthvika Shivani (IND) 5r
Chloe Birch (ENG) 21 21 4 Kirsty Gilmour (SCO) 9
Johanita Scholtz (RSA) 5 8 Chloe Birch (ENG) 21 21
Elise Dixon (JER) 2 5
Chloe Birch (ENG) 20 12
Aurelie Marie Elisa Allet (MRI) 21 21 4 Kirsty Gilmour (SCO) 22 21
Alana Bailey (JAM) 7 12 Aurelie Marie Elisa Allet (MRI) 3 4
4 Kirsty Gilmour (SCO) 21 21
Section 4[edit]
Round of 64 Round of 32 Round of 16 Quarterfinals
Alissa Dean (FIJ) 12 3
Mahoor Shahzad (PAK) 21 21 Mahoor Shahzad (PAK) 21 21
Cristen Marritt (IOM) 14 10
Mahoor Shahzad (PAK) 17 10
Mercy Joseph (KEN) 6 Rachel Honderich (CAN) 21 21
Allisen Camille (SEY) w / o Allisen Camille (SEY)
6 Rachel Honderich (CAN) w / o
6 Rachel Honderich (CAN) 8 13
Ogar Siamupangila (ZAM) 21 21 2 Saina Nehwal (IND) 21 21
Stella Koteikai Amasah (GHA) 6 12 Ogar Siamupangila (ZAM) 9 13
Jessica Li (IOM) 21 21
Jessica Li (IOM) 4 0r
2 Saina Nehwal (IND) 21 2
Elsie de Villiers (RSA) 3 1
2 Saina Nehwal (IND) 21 21
References[edit]
Jump up ^ "Badminton". gc2018.com. Gold Coast 2018. Retrieved 8 April 2017.
Jump up ^ Draw
Jump up ^ Seeding List
Retrieved from "https://en.wikipedia.org/w/index.php?title=Badminton_at_the_2018_Commonwealth_Games_–_Women%27s_singles&oldid=836477068"
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History of the United Nations
From Wikipedia, the free encyclopedia
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A map of the world showing when countries joined the United Nations
The founding of the United Nations
The history of the United Nations as an international organization has its origins in World War II. Since then its aims and activities have expanded to make it the archetypal international body in the early 21st century.
Contents
[hide]
1 Origins
1.1 1942 "Declaration of United Nations"
1.2 Planning
2 Establishment
3 Activities
4 Facilities
5 Structure and associated organizations
6 Milestones
7 See also
8 Further reading
8.1 Primary sources
9 References
10 External links
Origins[edit]
The earliest concrete plan for a new world organization to replace the ineffective League of Nations began under the aegis of the US State Department in 1939.[1] On 12 June 1941, representatives of the United Kingdom, Canada, Australia, New Zealand, the Union of South Africa, and of the exiled governments of Belgium, Czechoslovakia, Greece, Luxembourg, Netherlands, Norway, Poland, and Yugoslavia, as well as General de Gaulle of France, met in London and signed the Declaration of St. James's Palace. This was the first of six conferences that led up to the founding of the United Nations and the Charter of the United Nations.[2]
U.S. President Franklin Roosevelt first suggested using the name United Nations, to refer to the Allies of World War II, to British Prime Minister Winston Churchill during the latter's three-week visit to the White House in December 1941. Roosevelt suggested the name as an alternative to "Associated Powers", a term the U.S. used in the First World War (the U.S. was never formally a member of the Allies of World War I but entered the war in 1917 as a self-styled "Associated Power"). Churchill accepted the idea and cited Lord Byron's use of the phrase "United Nations" in the poem Childe Harold's Pilgrimage, which referred to the Allies at the Battle of Waterloo in 1815.[3][4]
1942 "Declaration of United Nations"[edit]
Poster for the founding of the United Nations
Main article: Declaration by United Nations
The text of the "Declaration of United Nations" was drafted by U.S. President Franklin D. Roosevelt, British Prime Minister Winston Churchill, and Roosevelt aide Harry Hopkins, while meeting at the White House on 29 December 1941. It incorporated Soviet suggestions, but left no role for France. The first official use of the term "United Nations" was on 1–2 January 1942 when 26 Governments signed the Declaration. One major change from the Atlantic Charter was the addition of a provision for religious freedom, which Stalin approved after Roosevelt insisted.[5][6] By early 1945 it had been signed by 21 more states.[7]
A JOINT DECLARATION BY THE UNITED STATES OF AMERICA, THE UNITED KINGDOM OF GREAT BRITAIN AND NORTHERN IRELAND, THE UNION OF SOVIET SOCIALIST REPUBLICS, CHINA, AUSTRALIA, BELGIUM, CANADA, COSTA RICA, CUBA, CZECHOSLOVAKIA, DOMINICAN REPUBLIC, EL SALVADOR, GREECE, GUATEMALA, HAITI, HONDURAS, INDIA, LUXEMBOURG, NETHERLANDS, NEW ZEALAND, NICARAGUA, NORWAY, PANAMA, POLAND, SOUTH AFRICA, YUGOSLAVIA
The Governments signatory hereto,
Having subscribed to a common program of purposes and principles embodied in the Joint Declaration of the President of the United States of America and the Prime Minister of Great Britain dated August 14, 1941, known as the Atlantic Charter,
Being convinced that complete victory over their enemies is essential to defend life, liberty, independence and religious freedom, and to preserve human rights and justice in their own lands as well as in other lands, and that they are now engaged in a common struggle against savage and brutal forces seeking to subjugate the world,
DECLARE:
(1) Each Government pledges itself to employ its full resources, military or economic, against those members of the Tripartite Pact and its adherents with which such government is at war.
(2) Each Government pledges itself to cooperate with the Governments signatory hereto and not to make a separate armistice or peace with the enemies.
The foregoing declaration may be adhered to by other nations which are, or which may be, rendering material assistance and contributions in the struggle for victory over Hitlerism.[8]
During the war, the United Nations became the official term for the Allies. To join countries had to sign the Declaration and declare war on the Axis.[9]
Planning[edit]
Early United Nations official's passport from World War Two - working for UNRRA, issued in 1944 for the Middle East.
The idea for the future United Nations as an international organization emerged in declarations signed at the wartime Allied conferences: the Moscow Conference and the Tehran Conference in 1943.
US President Franklin D. Roosevelt considered his most important legacy the creation of the United Nations, making a permanent organization out of the wartime Alliance of the same name. He provided continuous backstage political support inside the United States, and with Churchill and Stalin abroad. He made sure that leading Republicans were on board, especially Senators Arthur Vandenberg of Michigan,[10] and Warren Austin of Vermont.[11] He went public with strong advocacy in the 1944 presidential campaign, and turned detailed planning over to the State Department, where Sumner Welles and Secretary Cordell Hull worked on the project. The United States, Britain, Soviet Union and China made the major decisions and became permanent members of the all-powerful Security Council. Roosevelt made sure that each (including France) had a veto power, thus avoiding the fatal weakness of the League of Nations, which theoretically could order its members to act in defiance of their own parliaments.[12]
From August to October 1944, representatives of the Republic of China, Britain, the US and the USSR met to elaborate plans at the Dumbarton Oaks Conference in Washington, D.C. Those and later talks produced proposals outlining the purposes of the United Nations organization, its membership and organs, as well as arrangements to maintain international peace and security and international economic and social cooperation. Governments and private citizens worldwide discussed and debated these proposals.[13] Winston Churchill urged Roosevelt to restore France to its status of a major Power after the liberation of Paris in August 1944.
At the Yalta Conference it was agreed that membership would be open to nations that had joined the Allies by 1 March 1945.[14] Brazil, Syria and a number of other countries qualified for membership by declarations of war on either Germany or Japan in the first three months of 1945 – in some cases retroactively.
Establishment[edit]
Insignia of the Conference of San Francisco, prototype of the current logo of the United Nations
The UN in 1945. In light blue, the founding members. In dark blue, protectorates and colonies of the founding members.
On 25 April 1945, the United Nations Conference on International Organization began in San Francisco. In addition to Governments, a number of non-government organizations, including Rotary International and Lions Clubs International received invitations to assist in the drafting of a charter. After working for two months, the fifty nations represented at the conference signed the Charter of the United Nations on 26 June. Poland, which was unable to send a representative to the conference due to political instability, signed the charter on 15 October 1945. The charter stated that before it would come into effect, it must be ratified by the Governments of the Republic of China, France, the USSR, the United Kingdom, and the United States, and by a majority of the other 46 signatories. This occurred on 24 October 1945, and the United Nations was officially formed.[15]
The date each founding member state deposited their ratification of the UN Charter is as follows:[16]
USA – 8 Aug 1945
France – 31 Aug 1945
Dominican Rep. – 4 Sep 1945
Nicaragua – 6 Sep 1945
New Zealand – 19 Sep 1945
Brazil – 21 Sep 1945
Argentina – 24 Sep 1945
El Salvador – 26 Sep 1945
Haiti – 27 Sep 1945
China – 28 Sep 1945
Turkey – 28 Sep 1945
Denmark – 9 October 1945
Chile – 11 Oct 1945
Philippines – 11 Oct 1945
Paraguay – 12 Oct 1945
Cuba – 15 Oct 1945
Lebanon – 15 Oct 1945
Iran – 16 Oct 1945
Luxembourg – 17 Oct 1945
Saudi Arabia – 18 Oct 1945
Czechoslovakia – 19 Oct 1945
Syria – 19 Oct 1945
Yugoslavia – 19 Oct 1945
UK – 20 Oct 1945
Egypt – 22 Oct 1945
Byelorussia – 24 Oct 1945
Poland – 24 Oct 1945
Ukraine – 24 Oct 1945
USSR – 24 Oct 1945 (note - the United Nations is established on this date)
Greece – 25 Oct 1945
India – 30 Oct 1945
Peru – 31 Oct 1945
Australia – 1 Nov 1945
Costa Rica – 2 Nov 1945
Liberia – 2 Nov 1945
Colombia – 5 Nov 1945
Mexico – 7 Nov 1945
South Africa – 7 Nov 1945
Canada – 9 Nov 1945
Ethiopia – 13 Nov 1945
Panama – 13 Nov 1945
Bolivia – 14 Nov 1945
Venezuela – 15 Nov 1945
Honduras – 17 Nov 1945
Guatemala – 21 Nov 1945
Norway – 27 Nov 1945
Netherlands – 10 Dec 1945
Uruguay – 18 Dec 1945
Ecuador – 21 Dec 1945
Iraq – 21 Dec 1945
Belgium – 27 Dec 1945
Plaques unveiled in 1996 to commemorate the first meeting of the General Assembly
The first meeting of the General Assembly was held in Westminster Central Hall, London, on 10 January 1946.[17] The Security Council met for the first time a week later in Church House, Westminster.[18] The League of Nations formally dissolved itself on 18 April 1946 and transferred its mission to the United Nations.
Activities[edit]
See also: History of United Nations Peacekeeping
The United Nations has achieved considerable prominence in the social arena, fostering human rights, economic development, decolonization, health and education, for example, and interesting itself in refugees and trade.
The leaders of the UN had high hopes that it would act to prevent conflicts between nations and make future wars impossible. Those hopes have obviously not fully come to pass. From about 1947 until 1991 the division of the world into hostile camps during the Cold War made agreement on peacekeeping matters extremely difficult. Following the end of the Cold War, renewed calls arose for the UN to become the agency for achieving world peace and co-operation, as several dozen active military conflicts continued to rage across the globe. The breakup of the Soviet Union has also left the United States in a unique position of global dominance, creating a variety of new problems for the UN (See the United States and the United Nations).
Facilities[edit]
UN headquarters in New York City
UN building in Vienna
In December 1945, the US Senate and the US House of Representatives, by unanimous votes, requested that the UN make its headquarters in the United States. The UN accepted this suggestion and, after considering sites in the Black Hills, Flushing Meadows–Corona Park, Navy Island and what would become the World Trade Center site, constructed the United Nations headquarters building in New York City in 1949 and 1950 beside the East River on land purchased with an $8.5 million donation from John D. Rockefeller, Jr. The UN headquarters officially opened on January 9, 1951, although construction was not formally completed until October 9, 1952.[19]
Under special agreement with the United States, the UN enjoys certain diplomatic privileges and immunities, but generally the laws of New York City, New York State, and the United States apply.
While the principal headquarters of the UN remain in New York City, major agencies base themselves in Geneva, The Hague, Vienna, Nairobi and elsewhere.
Structure and associated organizations[edit]
This section needs expansion. You can help by adding to it. (January 2011)
The basic constitutional makeup of the United Nations has changed little, though vastly increased membership has altered the functioning of some elements. The UN as a whole has generated a rich assortment of non-governmental organizations and special bodies over the years: some with a regional focus, some specific to the various peacekeeping missions, and others of global scope and importance. Other bodies (such as the International Labour Organization) formed prior to the establishment of the United Nations and only subsequently became associated with it.
Milestones[edit]
In October 2015 over 350 landmarks in 60 countries were lit in blue to commemorate the 70th anniversary of the world body.[20][21][22]
See also[edit]
United Nations portal
Growth in United Nations membership
List of members of the United Nations Security Council
Timeline of UN peacekeeping missions
List of UN Secretaries-General
Attacks on humanitarian workers
Reform of the United Nations
Further reading[edit]
Baehr, Peter R., and Leon Gordenker. The United Nations in the 1990s (St. Martin's Press, 1992)
Bellamy, Alex J., and Paul D. Williams, eds. Providing Peacekeepers: The Politics, Challenges, and Future of United Nations Peacekeeping Contributions (Oxford University Press, 2013)
Bergesen, Helge Ole, and Leiv Lunde. Dinosaurs or Dynamos: the United Nations and the World Bank at the turn of the century (Routledge, 2013)
Bosco, David L. Five to rule them all: the UN Security Council and the making of the modern world (Oxford University Press, 2009)
Clark, Ian, and Christian Reus-Smit. "Liberal internationalism, the practice of special responsibilities and evolving politics of the security council." International Politics (2013) 50#1 pp: 38-56.
Ferdinand, Peter. "Rising powers at the UN: an analysis of the voting behaviour of brics in the General Assembly." Third World Quarterly (2014) 35#3 pp: 376-391.
Hiscocks, Richard. The Security Council: A study in adolescence (Simon and Schuster, 1974)
Luck, Edward C. UN Security Council: practice and promise (Routledge, 2006)
Meisler, Stanley. United Nations: The First Fifty Years (1995)
Rusell, Ruth B. A History of the United Nations Charter: The Role of the United Staes, 1940-1945 (Washington: Brookings Institution, 1958.)
O'Sullivan, Christopher D. The United Nations: A Concise History (The Anvil Series, Krieger Publishing Company, 2005)
Phillips, Walter Ray. "United Nations Educational, Scientific and Cultural Organization." Montana Law Review 24.1 (2014): 2.
Roberts, Adam, and Dominik Zaum. Selective security: war and the United Nations Security Council since 1945 (Routledge, 2013)
Saltford, John. The United Nations and the Indonesian takeover of West Papua, 1962-1969: the anatomy of betrayal (Routledge, 2013)
Vreeland, James Raymond, and Axel Dreher. The Political Economy of the United Nations Security Council: Money and Influence (Cambridge University Press, 2014)
Weiss, Thomas G. What's Wrong with the United Nations and how to Fix it (John Wiley & Sons, 2013)
Wuthnow, Joel. Chinese diplomacy and the UN Security Council: beyond the veto (Routledge, 2012)
Primary sources[edit]
Cordier, Andrew W., and Wilder Foote, eds. Public Papers of the Secretaries General of the United Nations (4 vol; Columbia University Press, 2013)
References[edit]
Jump up ^ Townsend Hoopes and Douglas Brinkley, FDR and the Creation of the U.N. (1997) pp 1-55
Jump up ^ "1941: The Declaration of St. James' Palace". United Nations. Retrieved 28 March 2016.
Jump up ^ "United Nations". Wordorigins.org. 3 February 2007. Retrieved 28 March 2016.
Jump up ^ Ward, Geoffrey C.; Burns, Ken (2014). "Nothing to Conceal". The Roosevelts: An Intimate History. Knopf Doubleday Publishing Group. ISBN 0385353065.
Jump up ^ David Roll, The Hopkins Touch: Harry Hopkins and the Forging of the Alliance to Defeat Hitler (2013) pp 172-75
Jump up ^ Robert E. Sherwood, Roosevelt and Hopkins, An Intimate History (1948) pp 447-53
Jump up ^ Edmund Jan Osmańczyk (2003). Encyclopedia of the United Nations and International Agreements: T to Z. Taylor & Francis. p. 2445. ISBN 9780415939249.
Jump up ^ Text from "The Washington Conference 1941-1942"
Jump up ^ Stephen C. Schlesinger, Act of creation: The founding of the United Nations: A story of superpowers, secret agents, wartime allies and enemies, and their quest for a peaceful world (2003)
Jump up ^ James A. Gazell, "Arthur H. Vandenberg, Internationalism, and the United Nations." Political Science Quarterly 88#3 (1973): 375-394. online
Jump up ^ George T. Mazuzan. Warren R. Austin at the U. N., 1946-1953 (Kent State UP, 1977).
Jump up ^ Townsend Hoopes and Douglas Brinkley, FDR and the Creation of the U. N. (1997)
Jump up ^ [1][dead link]
Jump up ^ Robert C. Hilderbrand, Dumbarton Oaks: The Origins of the United Nations and the Search for Postwar Security (UNC Press, 2001)
Jump up ^ https://www.un.org/aboutun/sanfrancisco/history.html The 60th Anniversary of the San Francisco Conference
Jump up ^ Division, United Nations, Department of Public Information, Outreach (2009-09-28). "UN|DPI — OD|Dag Hammarskjöld Library: Member States|On the Record". www.un.org.
Jump up ^ "History of the United Nations 1941 - 1950". United Nations. Archived from the original on 12 March 2015. Retrieved 12 March 2015.
Jump up ^ "What is the Security Council?". United Nations. Retrieved 12 March 2015.
Jump up ^ Hamilton, Thomas J. (1952-10-10). "WORK COMPLETED ON U. N. BUILDINGS; $68,000,000 Plant Finished -- Lie Announces a Plan to Reorganize Top Staff WORK COMPLETED ON U. N. BUILDINGS". The New York Times. ISSN 0362-4331. Retrieved 2018-03-29.
Jump up ^ "World lights up in UN blue to mark Organization's milestone anniversary". UN News Centre. 22 October 2015. Retrieved 25 October 2015.
Jump up ^ "Over 200 Landmarks to Light Up UN Blue on 70th Anniversary". The New York Times. 23 October 2015. Retrieved 25 October 2015.
Jump up ^ "Turn the World #UNBlue". United Nations Information Centres. Retrieved 25 October 2015.
External links[edit]
UN Intellectual History Project – Academic study of UN history
United Nations Events Timeline
Declaration by United Nations, January 1, 1942
UN History Project – Website providing resources, timelines, lectures, and bibliographies of UN history
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Secretaries-General of the League of Nations and the United Nations
League of Nations
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United Nations
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Gladwyn Jebb1 (United Kingdom)
Trygve Lie (Norway)
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Javier Pérez de Cuéllar (Peru)
Boutros Boutros-Ghali (Egypt)
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Ban Ki-moon (South Korea)
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1 Provisional Secretary-General prior to the election of Trygve Lie.
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International years proclaimed by the United Nations
Human Rights (1968)
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Struggle against Slavery and its Abolition (2004)
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Polar (2007–2008)
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