Identification

Name
Cysteine
Accession Number
DB00151
Description

A thiol-containing non-essential amino acid that is oxidized to form cystine.

Type
Small Molecule
Groups
Approved, Nutraceutical
Structure
Thumb
Weight
Average: 121.158
Monoisotopic: 121.019749163
Chemical Formula
C3H7NO2S
Synonyms
  • (2R)-2-amino-3-mercaptopropanoic acid
  • (2R)-2-amino-3-sulfanylpropanoic acid
  • (R)-2-Amino-3-mercaptopropanoic acid
  • Cisteina
  • Cisteinum
  • Cys
  • Cysteine
  • Cysteinum
  • Free Cysteine
  • L-2-Amino-3-mercaptopropionic acid
  • L-Cys
  • L-Cystein
  • L-Zystein
External IDs
  • E 920
  • E-920
  • E920
  • FEMA NO. 3263
  • NSC-8746

Pharmacology

Indication

For the prevention of liver damage and kidney damage associated with overdoses of acetaminophen

Associated Therapies
Contraindications & Blackbox Warnings
Learn about our commercial Contraindications & Blackbox Warnings data.
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Pharmacodynamics

Due to this ability to undergo redox reactions, cysteine has antioxidant properties. Cysteine is an important source of sulfur in human metabolism, and although it is classified as a non-essential amino acid, cysteine may be essential for infants, the elderly, and individuals with certain metabolic disease or who suffer from malabsorption syndromes. Cysteine may at some point be recognized as an essential or conditionally essential amino acid.

Mechanism of action

Cysteine can usually be synthesized by the human body under normal physiological conditions if a sufficient quantity of methionine is available. Cysteine is typically synthesized in the human body when there is sufficient methionine available. Cysteine exhibits antioxidant properties and participates in redox reactions. Cysteine's antioxidant properties are typically expressed in the tripeptide glutathione, which occurs in humans as well as other organisms. Glutathione (GSH) typically requires biosynthesis from its constituent amino acids, cysteine, glycine, and glutamic acid, due to its limited systemic availability. Glutamic acid and glycine are readily available in the diets of most industrialized countries, but the availability of cysteine can be the limiting substrate. In human metabolism, cysteine is also involved in the generation of sulfide present in iron-sulfur clusters and nitrogenase by acting as a precursor. In a 1994 report released by five top cigarette companies, cysteine is one of the 599 additives to cigarettes. Its use or purpose, however, is unknown, like most cigarette additives. Its inclusion in cigarettes could offer two benefits: Acting as an expectorant, since smoking increases mucus production in the lungs; and increasing the beneficial antioxidant glutathione (which is diminished in smokers).

TargetActionsOrganism
UGlutamate--cysteine ligase regulatory subunitNot AvailableHumans
UGlutamate--cysteine ligase catalytic subunitNot AvailableHumans
UAspartate aminotransferase, cytoplasmic
substrate
Humans
UAspartate aminotransferase, mitochondrial
substrate
Humans
UCystathionine gamma-lyaseNot AvailableHumans
UCystathionine beta-synthaseNot AvailableHumans
UCysteine--tRNA ligase, cytoplasmic
substrate
Humans
UMethylated-DNA--protein-cysteine methyltransferaseNot AvailableHumans
UGlutathione synthetaseNot AvailableHumans
UProbable cysteine--tRNA ligase, mitochondrial
substrate
Humans
UCysteine sulfinic acid decarboxylaseNot AvailableHumans
UCysteine desulfurase, mitochondrialNot AvailableHumans
UCysteine dioxygenase type 1Not AvailableHumans
Absorption
Not Available
Volume of distribution
Not Available
Protein binding
Not Available
Metabolism
Not Available
Route of elimination
Not Available
Half-life
Not Available
Clearance
Not Available
Adverse Effects
Learn about our commercial Adverse Effects data.
Learn More
Toxicity
Not Available
Affected organisms
  • Humans and other mammals
Pathways
PathwayCategory
Glycine and Serine MetabolismMetabolic
Taurine and Hypotaurine MetabolismMetabolic
Glutamate MetabolismMetabolic
Polythiazide Action PathwayDrug action
Bumetanide Action PathwayDrug action
Quinethazone Action PathwayDrug action
Indapamide Action PathwayDrug action
Trichlormethiazide Action PathwayDrug action
Spironolactone Action PathwayDrug action
Eplerenone Action PathwayDrug action
Cystathionine beta-Synthase DeficiencyDisease
Hyperinsulinism-Hyperammonemia SyndromeDisease
gamma-Glutamyltranspeptidase DeficiencyDisease
Pantothenate and CoA BiosynthesisMetabolic
Methionine MetabolismMetabolic
Chlorothiazide Action PathwayDrug action
Bendroflumethiazide Action PathwayDrug action
Ethacrynic Acid Action PathwayDrug action
Cyclothiazide Action PathwayDrug action
Hydroflumethiazide Action PathwayDrug action
Chlorthalidone Action PathwayDrug action
Amiloride Action PathwayDrug action
2-Hydroxyglutric Aciduria (D and L Form)Disease
gamma-Glutamyltransferase DeficiencyDisease
Glucose Transporter Defect (SGLT2)Disease
IminoglycinuriaDisease
Methionine Adenosyltransferase DeficiencyDisease
Non-Ketotic HyperglycinemiaDisease
4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase DeficiencyDisease
SarcosinemiaDisease
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Not Available
Food Interactions
No interactions found.

Products

Product Ingredients
IngredientUNIICASInChI Key
Cysteine hydrochlorideZT934N0X4W7048-04-6QIJRTFXNRTXDIP-JIZZDEOASA-N
International/Other Brands
Nouress
Brand Name Prescription Products
NameDosageStrengthRouteLabellerMarketing StartMarketing EndRegionImage
Cysteine HydrochlorideInjection, solution0.5 g/10mLIntravenousHospira, Inc.2006-07-182007-10-01US flag
ElcysInjection, solution10 mg/1mLIntravenousExela Pharma Sciences, LLC2019-05-28Not applicableUS flag
L Cysteine HCl Inj 50mg/mlLiquidIntravenousAbbott1984-12-311997-08-18Canada flag
L-Cysteine HydrochlorideInjection, solution50 mg/1mLIntravenousAmerican Regent2000-01-012016-11-09US flag
L-Cysteine HydrochlorideInjection, solution50 mg/1mLIntravenousSandoz2008-12-012016-07-15US flag
L-Cysteine HydrochlorideInjection, solution50 mg/1mLIntravenousAmerican Regent1990-09-302016-11-09US flag
L-Cysteine HydrochlorideInjection, solution50 mg/1mLIntravenousSandoz Inc2016-06-142021-06-30US flag
L-Cysteine HydrochlorideInjection, solution50 mg/1mLIntravenousSandoz2008-12-012016-07-01US flag
NouressInjection34.5 mg/1mLIntravenousAvadel Legacy Pharmaceuticals, Llc2020-04-01Not applicableUS flag
Additional Data Available
  • Application Number
    Application Number

    A unique ID assigned by the FDA when a product is submitted for approval by the labeller.

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  • Product Code
    Product Code

    A governmentally-recognized ID which uniquely identifies the product within its regulatory market.

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Mixture Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
8.5% Freamine IIICysteine (13.9 mg) + Alanine (600 mg) + Arginine (810 mg) + Glycine (1.19 g) + Histidine (240 mg) + Isoleucine (590 mg) + L-Lysine (620 mg) + Leucine (770 mg) + Phenylalanine (480 mg) + Proline (950 mg) + Racemethionine (450 mg) + Serine (500 mg) + Threonine (340 mg) + Tryptophan (130 mg) + Valine (560 mg)LiquidIntravenousB. Braun Medical Inc.1999-05-172012-04-16Canada flag
Aminoderm PoudreCysteine (2 mg) + Glycine (10 mg) + Neomycin sulfate (5 mg) + Threonine (1 mg)PowderTopicalDesbergers LtÉe, Division Of Technilab Inc.1968-12-312004-08-09Canada flag
Aminosyn HFCysteine hydrochloride (20 mg/100mL) + Alanine (770 mg/100mL) + Arginine (600 mg/100mL) + Glycine (900 mg/100mL) + Histidine (240 mg/100mL) + Isoleucine (900 mg/100mL) + L-Lysine acetate (610 mg/100mL) + Leucine (1100 mg/100mL) + Methionine (100 mg/100mL) + Phenylalanine (100 mg/100mL) + Proline (800 mg/100mL) + Serine (500 mg/100mL) + Threonine (450 mg/100mL) + Tryptophan (66 mg/100mL) + Valine (840 mg/100mL)Injection, solutionIntravenousHospira, Inc.2006-01-302010-03-01US flag
Cicatrin PowderCysteine (2 mg) + Bacitracin zinc (250 unit) + Glycine (10 mg) + Neomycin sulfate (3300 unit) + Threonine (1 mg)PowderTopicalGlaxosmithkline Inc1987-12-312009-01-19Canada flag
Distilpure MsmCysteine (0.02 g/100g) + Biotin (0.02 g/100g) + Cystine (0.05 g/100g) + Methionine (0.02 g/100g) + Thiamine chloride (0.02 g/100g)PowderTopicalMbg Inc (Korea Institute of Science Development)2017-09-162018-09-16US flag
FreAmine HBCCysteine hydrochloride (0.014 g/100mL) + Alanine (0.4 g/100mL) + Arginine (0.58 g/100mL) + Glycine (0.33 g/100mL) + Histidine (0.16 g/100mL) + Isoleucine (0.76 g/100mL) + L-Lysine acetate (0.41 g/100mL) + Leucine (1.37 g/100mL) + Methionine (0.25 g/100mL) + Phenylalanine (0.32 g/100mL) + Proline (0.63 g/100mL) + Serine (0.33 g/100mL) + Threonine (0.2 g/100mL) + Tryptophan (0.09 g/100mL) + Valine (0.88 g/100mL)Injection, solutionIntravenousB. Braun Medical Inc.1971-09-24Not applicableUS flag
FreAmine IIICysteine hydrochloride (0.016 g/100mL) + Alanine (0.71 g/100mL) + Arginine (0.95 g/100mL) + Glycine (1.4 g/100mL) + Histidine (0.28 g/100mL) + Isoleucine (0.69 g/100mL) + L-Lysine acetate (0.73 g/100mL) + Leucine (0.91 g/100mL) + Methionine (0.53 g/100mL) + Phenylalanine (0.56 g/100mL) + Phosphoric acid (0.12 g/100mL) + Proline (1.12 g/100mL) + Serine (0.59 g/100mL) + Threonine (0.4 g/100mL) + Tryptophan (0.15 g/100mL) + Valine (0.66 g/100mL)Injection, solutionIntravenousB. Braun Medical Inc.1971-09-242012-05-01US flag
FreAmine IIICysteine hydrochloride (0.014 g/100mL) + Alanine (0.21 g/100mL) + Arginine (0.29 g/100mL) + Glycine (0.42 g/100mL) + Histidine (0.085 g/100mL) + Isoleucine (0.21 g/100mL) + L-Lysine acetate (0.22 g/100mL) + Leucine (0.27 g/100mL) + Magnesium acetate (0.054 g/100mL) + Methionine (0.16 g/100mL) + Phenylalanine (0.17 g/100mL) + Phosphoric acid (0.040 g/100mL) + Potassium chloride (0.15 g/100mL) + Proline (0.34 g/100mL) + Serine (0.18 g/100mL) + Sodium acetate trihydrate (0.2 g/100mL) + Sodium chloride (0.12 g/100mL) + Threonine (0.12 g/100mL) + Tryptophan (0.046 g/100mL) + Valine (0.2 g/100mL)Injection, solutionIntravenousB. Braun Medical Inc.1971-09-242013-08-01US flag
FreAmine IIICysteine hydrochloride (0.016 g/100mL) + Alanine (0.71 g/100mL) + Arginine (0.95 g/100mL) + Glycine (1.4 g/100mL) + Histidine (0.28 g/100mL) + Isoleucine (0.69 g/100mL) + L-Lysine acetate (0.73 g/100mL) + Leucine (0.91 g/100mL) + Methionine (0.53 g/100mL) + Phenylalanine (0.56 g/100mL) + Phosphoric acid (0.12 g/100mL) + Proline (1.12 g/100mL) + Serine (0.59 g/100mL) + Threonine (0.4 g/100mL) + Tryptophan (0.15 g/100mL) + Valine (0.66 g/100mL)Injection, solutionIntravenousB. Braun Medical Inc.1971-09-24Not applicableUS flag
FreAmine IIICysteine hydrochloride (0.014 g/100mL) + Alanine (0.6 g/100mL) + Arginine (0.81 g/100mL) + Glycine (1.19 g/100mL) + Histidine (0.24 g/100mL) + Isoleucine (0.59 g/100mL) + L-Lysine acetate (0.62 g/100mL) + Leucine (0.77 g/100mL) + Methionine (0.45 g/100mL) + Phenylalanine (0.48 g/100mL) + Phosphoric acid (0.115 g/100mL) + Proline (0.95 g/100mL) + Serine (0.5 g/100mL) + Threonine (0.34 g/100mL) + Tryptophan (0.13 g/100mL) + Valine (0.56 g/100mL)Injection, solutionIntravenousB. Braun Medical Inc.1971-09-242013-05-01US flag
Unapproved/Other Products
NameIngredientsDosageRouteLabellerMarketing StartMarketing EndRegionImage
Distilpure MsmCysteine (0.02 g/100g) + Biotin (0.02 g/100g) + Cystine (0.05 g/100g) + Methionine (0.02 g/100g) + Thiamine chloride (0.02 g/100g)PowderTopicalMbg Inc (Korea Institute of Science Development)2017-09-162018-09-16US flag
L-Cysteine HydrochlorideCysteine hydrochloride (50 mg/1mL)Injection, solutionIntravenousSandoz2008-12-012016-07-15US flag
L-Cysteine HydrochlorideCysteine hydrochloride (50 mg/1mL)Injection, solutionIntravenousAmerican Regent2000-01-012016-11-09US flag
L-Cysteine HydrochlorideCysteine hydrochloride (50 mg/1mL)Injection, solutionIntravenousSandoz Inc2016-06-142021-06-30US flag
L-Cysteine HydrochlorideCysteine hydrochloride (50 mg/1mL)Injection, solutionIntravenousSandoz2008-12-012016-07-01US flag
L-Cysteine HydrochlorideCysteine hydrochloride (50 mg/1mL)Injection, solutionIntravenousAmerican Regent1990-09-302016-11-09US flag
Medi Msm (methyl Sulfonyl Methane)Cysteine (0.02 g/100g) + Biotin (0.02 g/100g) + Cystine (0.05 g/100g) + Methionine (0.02 g/100g) + Thiamine chloride (0.02 g/100g)PowderTopicalMbg Inc (Korea Institute of Science Development)2016-09-162016-09-16US flag
PrimeneCysteine (0.47 g/250mL) + Alanine (2 g/250mL) + Arginine (2.1 g/250mL) + Aspartic acid (1.5 g/250mL) + Glutamic acid (2.5 g/250mL) + Glycine (1 g/250mL) + Histidine (0.95 g/250mL) + Isoleucine (1.675 g/250mL) + L-Lysine (2.75 g/250mL) + Leucine (2.5 g/250mL) + Methionine (0.6 g/250mL) + Ornithine hydrochloride (0.8 g/250mL) + Phenylalanine (1.05 g/250mL) + Proline (0.75 g/250mL) + Serine (1 g/250mL) + Taurine (0.15 g/250mL) + Threonine (0.9 g/250mL) + Tryptophan (0.5 g/250mL) + Tyrosine (0.11 g/250mL) + Valine (1.9 g/250mL)Injection, solutionIntravenousBaxter Healthcare Corporation2017-11-222019-05-31US flag

Categories

Drug Categories
Chemical TaxonomyProvided by Classyfire
Description
This compound belongs to the class of organic compounds known as cysteine and derivatives. These are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
Kingdom
Organic compounds
Super Class
Organic acids and derivatives
Class
Carboxylic acids and derivatives
Sub Class
Amino acids, peptides, and analogues
Direct Parent
Cysteine and derivatives
Alternative Parents
L-alpha-amino acids / Amino acids / Monocarboxylic acids and derivatives / Carboxylic acids / Alkylthiols / Organopnictogen compounds / Organic oxides / Monoalkylamines / Hydrocarbon derivatives / Carbonyl compounds
Substituents
Aliphatic acyclic compound / Alkylthiol / Alpha-amino acid / Amine / Amino acid / Carbonyl group / Carboxylic acid / Cysteine or derivatives / Hydrocarbon derivative / L-alpha-amino acid
Molecular Framework
Aliphatic acyclic compounds
External Descriptors
proteinogenic amino acid, L-alpha-amino acid, cysteine, serine family amino acid (CHEBI:17561) / Common amino acids (C00097)

Chemical Identifiers

UNII
K848JZ4886
CAS number
52-90-4
InChI Key
XUJNEKJLAYXESH-REOHCLBHSA-N
InChI
InChI=1S/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1
IUPAC Name
(2R)-2-amino-3-sulfanylpropanoic acid
SMILES
N[[email protected]@H](CS)C(O)=O

References

Synthesis Reference

Alfred Maierhofer, Hans Wagner, "Process for the production of high purity S-carboxymethyl-L-cysteine." U.S. Patent US4129593, issued May, 1965.

US4129593
General References
  1. Bulaj G, Kortemme T, Goldenberg DP: Ionization-reactivity relationships for cysteine thiols in polypeptides. Biochemistry. 1998 Jun 23;37(25):8965-72. [PubMed:9636038]
  2. Baker DH, Czarnecki-Maulden GL: Pharmacologic role of cysteine in ameliorating or exacerbating mineral toxicities. J Nutr. 1987 Jun;117(6):1003-10. [PubMed:3298579]
Human Metabolome Database
HMDB0000574
KEGG Drug
D00026
KEGG Compound
C00097
PubChem Compound
5862
PubChem Substance
46506553
ChemSpider
5653
BindingDB
50109609
RxNav
3024
ChEBI
17561
ChEMBL
CHEMBL863
ZINC
ZINC000000895042
PharmGKB
PA449173
PDBe Ligand
CYS
Wikipedia
Cysteine
AHFS Codes
  • 40:20.00 — Caloric Agents
MSDS
Download (73.2 KB)

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount
4CompletedPreventionSystemic Inflammatory Response Syndrome (SIRS)1
4CompletedTreatmentCystinosis, Nephropathic / Kidney Diseases1
4CompletedTreatmentDetection of Different Prognostic Factors and Their Relation With the Outcome / Using New Protocol to Prove the Role of N-acetyl Cysteine and Adequate Supportive Measures in Aluminum Phosphide Poisoning1
4CompletedTreatmentPolycystic Ovaries Syndrome1
4CompletedTreatmentPostoperative pain1
4CompletedTreatmentPsychotic Disorder NOS / Schizoaffective Disorders / Schizophrenia / Schizophreniform1
4Not Yet RecruitingPreventionOtotoxic Hearing Loss / Ototoxic Hearing Loss, Bilateral / Ototoxicity / Tinnitus1
4Not Yet RecruitingSupportive CareThe Study Focus to Improve the Standard of Care Used for Aluminuim Phosphide Poisoning and to Save Patients With the Minimal Organ Damage1
4Not Yet RecruitingTreatmentCarpal Tunnel / Carpal Tunnel Release / Carpal Tunnel Syndrome (CTS) / Hand Injuries and Disorders / Nerve Compression / Splints1
4Not Yet RecruitingTreatmentFlu caused by Influenza1

Pharmacoeconomics

Manufacturers
  • Hospira inc
Packagers
  • Amend
  • American Regent
  • Spectrum Pharmaceuticals
Dosage Forms
FormRouteStrength
LiquidIntravenous
Injection, solutionIntravenous0.5 g/10mL
PowderTopical
Injection, solutionIntravenous10 mg/1mL
Injection, solutionIntravenous
SolutionIntravenous0.69 %
SolutionIntravenous0.59 %
InjectionIntravenous
LiquidIntravenous
Injection, solutionIntravenous50 mg/1mL
InjectionIntravenous34.5 mg/1mL
EmulsionIntravenous1.83 g
InjectionIntravenous1.03 g
Injection, solutionIntravenous0.69 %
Injection, solutionIntravenous0.59 %
Injection, solutionIntravenous0.9 %
Injection, solutionIntravenous0.56 %
Injection, solutionIntravenous0.49 %
InjectionIntravenous0.67 g/100ml
SolutionParenteral3 g/100ml
Injection, solutionIntravenous0.76 g/100mL
SolutionIntravenous12 g/L
SolutionIntravenous16 g/L
SolutionIntravenous5.1 g/16g N
SolutionIntravenous
Prices
Unit descriptionCostUnit
L-cysteine powder1.65USD g
L-cysteine 50 mg/ml vial0.4USD ml
L-cysteine hcl powder0.3USD g
DrugBank does not sell nor buy drugs. Pricing information is supplied for informational purposes only.
Patents
Patent NumberPediatric ExtensionApprovedExpires (estimated)Region
US10478453No2019-11-192039-01-15US flag
US10493051No2019-12-032039-03-15US flag
US10543186No2019-03-152039-03-15US flag
US10583155No2019-01-152039-01-15US flag
US10653719No2019-01-152039-01-15US flag
US10702490No2019-03-152039-03-15US flag
Additional Data Available
  • Filed On
    Filed On

    The date on which a patent was filed with the relevant government.

    Learn more

Properties

State
Solid
Experimental Properties
PropertyValueSource
melting point (°C)240 dec °CPhysProp
water solubility2.77E+005 mg/L (at 25 °C)BEILSTEIN
logP-2.49HANSCH,C ET AL. (1995)
pKa1.71MERCK INDEX (1996); pK1
Predicted Properties
PropertyValueSource
Water Solubility23.1 mg/mLALOGPS
logP-2.6ALOGPS
logP-2.8ChemAxon
logS-0.72ALOGPS
pKa (Strongest Acidic)2.35ChemAxon
pKa (Strongest Basic)9.05ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count3ChemAxon
Polar Surface Area63.32 Å2ChemAxon
Rotatable Bond Count2ChemAxon
Refractivity28.22 m3·mol-1ChemAxon
Polarizability11.41 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleNoChemAxon
Predicted ADMET Features
PropertyValueProbability
Human Intestinal Absorption+0.9698
Blood Brain Barrier+0.5918
Caco-2 permeable-0.721
P-glycoprotein substrateNon-substrate0.8141
P-glycoprotein inhibitor INon-inhibitor0.984
P-glycoprotein inhibitor IINon-inhibitor0.9903
Renal organic cation transporterNon-inhibitor0.9462
CYP450 2C9 substrateNon-substrate0.8473
CYP450 2D6 substrateNon-substrate0.8141
CYP450 3A4 substrateNon-substrate0.8245
CYP450 1A2 substrateNon-inhibitor0.94
CYP450 2C9 inhibitorNon-inhibitor0.9584
CYP450 2D6 inhibitorNon-inhibitor0.9665
CYP450 2C19 inhibitorNon-inhibitor0.9634
CYP450 3A4 inhibitorNon-inhibitor0.9602
CYP450 inhibitory promiscuityLow CYP Inhibitory Promiscuity0.9888
Ames testAMES toxic0.9107
CarcinogenicityNon-carcinogens0.7998
BiodegradationReady biodegradable0.7577
Rat acute toxicity1.7757 LD50, mol/kg Not applicable
hERG inhibition (predictor I)Weak inhibitor0.9891
hERG inhibition (predictor II)Non-inhibitor0.9684
ADMET data is predicted using admetSAR, a free tool for evaluating chemical ADMET properties. (23092397)

Spectra

Mass Spec (NIST)
Download (8.4 KB)
Spectra
SpectrumSpectrum TypeSplash Key
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)GC-MSsplash10-00kb-0950000000-df7e91c95b610ff21c79
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)GC-MSsplash10-00kb-0940000000-aefe34765fb447090a23
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)GC-MSsplash10-00kb-0970000000-10a155c40ea499023052
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)GC-MSsplash10-00kb-0940000000-037a3a34651c3154b3b3
GC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (4 TMS)GC-MSsplash10-00di-9850000000-118c43e33861a6baa8d2
Predicted GC-MS Spectrum - GC-MSPredicted GC-MSNot Available
GC-MS Spectrum - EI-BGC-MSsplash10-014j-0690100000-0aeb88fd507505e6b718
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-00kb-0950000000-df7e91c95b610ff21c79
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-00kb-0940000000-aefe34765fb447090a23
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-00kb-0970000000-10a155c40ea499023052
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-00kb-0940000000-037a3a34651c3154b3b3
GC-MS Spectrum - GC-EI-QQGC-MSsplash10-0uk9-5619100000-8cb2558373966174ced3
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-00di-9850000000-118c43e33861a6baa8d2
GC-MS Spectrum - GC-EI-TOFGC-MSsplash10-0gi0-0960000000-03b2097de6f9637d29cb
MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)LC-MS/MSsplash10-00b9-9600000000-374c5872d68662832769
MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)LC-MS/MSsplash10-0a4i-9000000000-ddbd3df6b8dbb280ffba
MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)LC-MS/MSsplash10-0a4i-9000000000-320a2c77443b80ebf733
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0089-0900000000-9dcd3d757c5cd11eb18e
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0udi-3900000000-212e081fe83ad70de0ad
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-000i-9000000000-2eb01f41c225f614db24
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-001i-0900000000-a19834eb7cb9f211fdf2
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-00di-0900000000-2458f2587761e779ed93
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0a4i-9000000000-77e590f0ed26f69b31c0
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0udi-3900000000-7b1857997392b006b95f
LC-MS/MS Spectrum - LC-ESI-ITFT (LTQ Orbitrap XL, Thermo Scientfic) , PositiveLC-MS/MSsplash10-0a4i-3900000000-bc268c27ed5706a4bbd2
MS/MS Spectrum - CE-ESI-TOF (CE-system connected to 6210 Time-of-Flight MS, Agilent) , PositiveLC-MS/MSsplash10-00di-0900000000-4573390bccc238e3c91b
Predicted MS/MS Spectrum - 10V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Positive (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 10V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 20V, Negative (Annotated)Predicted LC-MS/MSNot Available
Predicted MS/MS Spectrum - 40V, Negative (Annotated)Predicted LC-MS/MSNot Available
LC-MS/MS Spectrum - LC-ESI-ITFT , positiveLC-MS/MSsplash10-0udi-3900000000-212e081fe83ad70de0ad
LC-MS/MS Spectrum - LC-ESI-ITFT , positiveLC-MS/MSsplash10-0udi-3900000000-7b1857997392b006b95f
13C NMR Spectrum1D NMRNot Applicable
1H NMR Spectrum1D NMRNot Applicable
1H NMR Spectrum1D NMRNot Applicable
[1H,1H] 2D NMR Spectrum2D NMRNot Applicable
[1H,13C] 2D NMR Spectrum2D NMRNot Applicable

Targets

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Glutamate-cysteine ligase catalytic subunit binding
Specific Function
Not Available
Gene Name
GCLM
Uniprot ID
P48507
Uniprot Name
Glutamate--cysteine ligase regulatory subunit
Molecular Weight
30726.745 Da
References
  1. Ashida H, Sawa Y, Shibata H: Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant Cell Physiol. 2005 Apr;46(4):557-62. Epub 2005 Feb 2. [PubMed:15695431]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Magnesium ion binding
Specific Function
Not Available
Gene Name
GCLC
Uniprot ID
P48506
Uniprot Name
Glutamate--cysteine ligase catalytic subunit
Molecular Weight
72765.14 Da
References
  1. Ashida H, Sawa Y, Shibata H: Cloning, biochemical and phylogenetic characterizations of gamma-glutamylcysteine synthetase from Anabaena sp. PCC 7120. Plant Cell Physiol. 2005 Apr;46(4):557-62. Epub 2005 Feb 2. [PubMed:15695431]
  2. Srivastava S, Chan C: Application of metabolic flux analysis to identify the mechanisms of free fatty acid toxicity to human hepatoma cell line. Biotechnol Bioeng. 2008 Feb 1;99(2):399-410. [PubMed:17615559]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Pyridoxal phosphate binding
Specific Function
Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a sca...
Gene Name
GOT1
Uniprot ID
P17174
Uniprot Name
Aspartate aminotransferase, cytoplasmic
Molecular Weight
46247.14 Da
References
  1. Wen YD, Wang H, Zhu YZ: The Drug Developments of Hydrogen Sulfide on Cardiovascular Disease. Oxid Med Cell Longev. 2018 Jul 29;2018:4010395. doi: 10.1155/2018/4010395. eCollection 2018. [PubMed:30151069]
  2. Cooper AJ, Bruschi SA, Iriarte A, Martinez-Carrion M: Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions. Biochem J. 2002 Nov 15;368(Pt 1):253-61. doi: 10.1042/BJ20020531. [PubMed:12137566]
  3. Gaskin PJ, Adcock HJ, Buckberry LD, Teesdale-Spittle PH, Shaw PN: The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes. Hum Exp Toxicol. 1995 May;14(5):422-7. doi: 10.1177/096032719501400506. [PubMed:7612304]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange betwe...
Gene Name
GOT2
Uniprot ID
P00505
Uniprot Name
Aspartate aminotransferase, mitochondrial
Molecular Weight
47517.285 Da
References
  1. Gaskin PJ, Adcock HJ, Buckberry LD, Teesdale-Spittle PH, Shaw PN: The C-S lysis of L-cysteine conjugates by aspartate and alanine aminotransferase enzymes. Hum Exp Toxicol. 1995 May;14(5):422-7. doi: 10.1177/096032719501400506. [PubMed:7612304]
  2. Cooper AJ, Bruschi SA, Iriarte A, Martinez-Carrion M: Mitochondrial aspartate aminotransferase catalyses cysteine S-conjugate beta-lyase reactions. Biochem J. 2002 Nov 15;368(Pt 1):253-61. doi: 10.1042/BJ20020531. [PubMed:12137566]
  3. Wen YD, Wang H, Zhu YZ: The Drug Developments of Hydrogen Sulfide on Cardiovascular Disease. Oxid Med Cell Longev. 2018 Jul 29;2018:4010395. doi: 10.1155/2018/4010395. eCollection 2018. [PubMed:30151069]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two c...
Gene Name
CTH
Uniprot ID
P32929
Uniprot Name
Cystathionine gamma-lyase
Molecular Weight
44507.64 Da
References
  1. Fiorucci S, Antonelli E, Mencarelli A, Orlandi S, Renga B, Rizzo G, Distrutti E, Shah V, Morelli A: The third gas: H2S regulates perfusion pressure in both the isolated and perfused normal rat liver and in cirrhosis. Hepatology. 2005 Sep;42(3):539-48. [PubMed:16108046]
  2. Zhang H, Zhi L, Moore PK, Bhatia M: Role of hydrogen sulfide in cecal ligation and puncture-induced sepsis in the mouse. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1193-201. Epub 2006 Jan 20. [PubMed:16428267]
  3. Wallace JL, Dicay M, McKnight W, Martin GR: Hydrogen sulfide enhances ulcer healing in rats. FASEB J. 2007 Dec;21(14):4070-6. Epub 2007 Jul 18. [PubMed:17634391]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Ubiquitin protein ligase binding
Specific Function
Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, th...
Gene Name
CBS
Uniprot ID
P35520
Uniprot Name
Cystathionine beta-synthase
Molecular Weight
60586.05 Da
References
  1. Zhang H, Zhi L, Moore PK, Bhatia M: Role of hydrogen sulfide in cecal ligation and puncture-induced sepsis in the mouse. Am J Physiol Lung Cell Mol Physiol. 2006 Jun;290(6):L1193-201. Epub 2006 Jan 20. [PubMed:16428267]
  2. Lowicka E, Beltowski J: Hydrogen sulfide (H2S) - the third gas of interest for pharmacologists. Pharmacol Rep. 2007 Jan-Feb;59(1):4-24. [PubMed:17377202]
  3. Tamizhselvi R, Moore PK, Bhatia M: Hydrogen sulfide acts as a mediator of inflammation in acute pancreatitis: in vitro studies using isolated mouse pancreatic acinar cells. J Cell Mol Med. 2007 Mar-Apr;11(2):315-26. [PubMed:17488480]
  4. Oh GS, Pae HO, Lee BS, Kim BN, Kim JM, Kim HR, Jeon SB, Jeon WK, Chae HJ, Chung HT: Hydrogen sulfide inhibits nitric oxide production and nuclear factor-kappaB via heme oxygenase-1 expression in RAW264.7 macrophages stimulated with lipopolysaccharide. Free Radic Biol Med. 2006 Jul 1;41(1):106-19. Epub 2006 Apr 25. [PubMed:16781459]
  5. Bhatia M, Wong FL, Fu D, Lau HY, Moochhala SM, Moore PK: Role of hydrogen sulfide in acute pancreatitis and associated lung injury. FASEB J. 2005 Apr;19(6):623-5. Epub 2005 Jan 25. [PubMed:15671155]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Trna binding
Specific Function
Not Available
Gene Name
CARS
Uniprot ID
P49589
Uniprot Name
Cysteine--tRNA ligase, cytoplasmic
Molecular Weight
85472.665 Da
References
  1. Kuo ME, Theil AF, Kievit A, Malicdan MC, Introne WJ, Christian T, Verheijen FW, Smith DEC, Mendes MI, Hussaarts-Odijk L, van der Meijden E, van Slegtenhorst M, Wilke M, Vermeulen W, Raams A, Groden C, Shimada S, Meyer-Schuman R, Hou YM, Gahl WA, Antonellis A, Salomons GS, Mancini GMS: Cysteinyl-tRNA Synthetase Mutations Cause a Multi-System, Recessive Disease That Includes Microcephaly, Developmental Delay, and Brittle Hair and Nails. Am J Hum Genet. 2019 Mar 7;104(3):520-529. doi: 10.1016/j.ajhg.2019.01.006. Epub 2019 Feb 26. [PubMed:30824121]
  2. Davidson E, Caffarella J, Vitseva O, Hou YM, King MP: Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase. Biol Chem. 2001 Mar;382(3):399-406. [PubMed:11347887]
  3. Akaike T, Ida T, Wei FY, Nishida M, Kumagai Y, Alam MM, Ihara H, Sawa T, Matsunaga T, Kasamatsu S, Nishimura A, Morita M, Tomizawa K, Nishimura A, Watanabe S, Inaba K, Shima H, Tanuma N, Jung M, Fujii S, Watanabe Y, Ohmuraya M, Nagy P, Feelisch M, Fukuto JM, Motohashi H: Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Nat Commun. 2017 Oct 27;8(1):1177. doi: 10.1038/s41467-017-01311-y. [PubMed:29079736]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Methyltransferase activity
Specific Function
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 p...
Gene Name
MGMT
Uniprot ID
P16455
Uniprot Name
Methylated-DNA--protein-cysteine methyltransferase
Molecular Weight
21645.83 Da
References
  1. Niture SK, Velu CS, Smith QR, Bhat GJ, Srivenugopal KS: Increased expression of the MGMT repair protein mediated by cysteine prodrugs and chemopreventative natural products in human lymphocytes and tumor cell lines. Carcinogenesis. 2007 Feb;28(2):378-89. Epub 2006 Aug 31. [PubMed:16950796]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Protein homodimerization activity
Specific Function
Not Available
Gene Name
GSS
Uniprot ID
P48637
Uniprot Name
Glutathione synthetase
Molecular Weight
52384.325 Da
References
  1. Tanaka T, Halicka HD, Huang X, Traganos F, Darzynkiewicz Z: Constitutive histone H2AX phosphorylation and ATM activation, the reporters of DNA damage by endogenous oxidants. Cell Cycle. 2006 Sep;5(17):1940-5. Epub 2006 Sep 1. [PubMed:16940754]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Substrate
General Function
Metal ion binding
Specific Function
Not Available
Gene Name
CARS2
Uniprot ID
Q9HA77
Uniprot Name
Probable cysteine--tRNA ligase, mitochondrial
Molecular Weight
62223.345 Da
References
  1. Akaike T, Ida T, Wei FY, Nishida M, Kumagai Y, Alam MM, Ihara H, Sawa T, Matsunaga T, Kasamatsu S, Nishimura A, Morita M, Tomizawa K, Nishimura A, Watanabe S, Inaba K, Shima H, Tanuma N, Jung M, Fujii S, Watanabe Y, Ohmuraya M, Nagy P, Feelisch M, Fukuto JM, Motohashi H: Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. Nat Commun. 2017 Oct 27;8(1):1177. doi: 10.1038/s41467-017-01311-y. [PubMed:29079736]
  2. Kuo ME, Theil AF, Kievit A, Malicdan MC, Introne WJ, Christian T, Verheijen FW, Smith DEC, Mendes MI, Hussaarts-Odijk L, van der Meijden E, van Slegtenhorst M, Wilke M, Vermeulen W, Raams A, Groden C, Shimada S, Meyer-Schuman R, Hou YM, Gahl WA, Antonellis A, Salomons GS, Mancini GMS: Cysteinyl-tRNA Synthetase Mutations Cause a Multi-System, Recessive Disease That Includes Microcephaly, Developmental Delay, and Brittle Hair and Nails. Am J Hum Genet. 2019 Mar 7;104(3):520-529. doi: 10.1016/j.ajhg.2019.01.006. Epub 2019 Feb 26. [PubMed:30824121]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Sulfinoalanine decarboxylase activity
Specific Function
Not Available
Gene Name
CSAD
Uniprot ID
Q9Y600
Uniprot Name
Cysteine sulfinic acid decarboxylase
Molecular Weight
55022.79 Da
References
  1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed:17139284]
  2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed:17016423]
  3. Chan-Palay V, Lin CT, Palay S, Yamamoto M, Wu JY: Taurine in the mammalian cerebellum: demonstration by autoradiography with [3H]taurine and immunocytochemistry with antibodies against the taurine-synthesizing enzyme, cysteine-sulfinic acid decarboxylase. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2695-9. [PubMed:6953423]
  4. Guion-Rain M-C, Portemer C, Chatagner F: Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties. Biochim Biophys Acta. 1975 Mar 28;384(1):265-76. [PubMed:236774]
  5. Daniels KM, Stipanuk MH: The effect of dietary cysteine level on cysteine metabolism in rats. J Nutr. 1982 Nov;112(11):2130-41. [PubMed:7131091]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Pyridoxal phosphate binding
Specific Function
Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofac...
Gene Name
NFS1
Uniprot ID
Q9Y697
Uniprot Name
Cysteine desulfurase, mitochondrial
Molecular Weight
50195.21 Da
References
  1. You D, Wang L, Yao F, Zhou X, Deng Z: A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans. Biochemistry. 2007 May 22;46(20):6126-33. Epub 2007 May 1. [PubMed:17469805]
  2. Ding H, Harrison K, Lu J: Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. J Biol Chem. 2005 Aug 26;280(34):30432-7. Epub 2005 Jun 28. [PubMed:15985427]
  3. Ding B, Smith ES, Ding H: Mobilization of the iron centre in IscA for the iron-sulphur cluster assembly in IscU. Biochem J. 2005 Aug 1;389(Pt 3):797-802. [PubMed:15828873]
  4. Yang J, Bitoun JP, Ding H: Interplay of IscA and IscU in biogenesis of iron-sulfur clusters. J Biol Chem. 2006 Sep 22;281(38):27956-63. Epub 2006 Jul 27. [PubMed:16877383]
  5. Layer G, Ollagnier-de Choudens S, Sanakis Y, Fontecave M: Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CYaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU. J Biol Chem. 2006 Jun 16;281(24):16256-63. Epub 2006 Apr 9. [PubMed:16603772]
Kind
Protein
Organism
Humans
Pharmacological action
Unknown
General Function
Ferrous iron binding
Specific Function
Initiates several important metabolic pathways related to pyruvate and several sulfurate compounds including sulfate, hypotaurine and taurine. Critical regulator of cellular cysteine concentrations...
Gene Name
CDO1
Uniprot ID
Q16878
Uniprot Name
Cysteine dioxygenase type 1
Molecular Weight
22971.745 Da
References
  1. Roopnarinesingh ES, Steventon GB, Harris RM, Waring RH, Mitchell SC: Induction of cysteine dioxygenase activity by oral administration of cysteine analogues to the rat: implications for drug efficacy and safety. Drug Metabol Drug Interact. 2005;21(2):75-86. [PubMed:16355974]
  2. McCoy JG, Bailey LJ, Bitto E, Bingman CA, Aceti DJ, Fox BG, Phillips GN Jr: Structure and mechanism of mouse cysteine dioxygenase. Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3084-9. Epub 2006 Feb 21. [PubMed:16492780]
  3. Ye S, Wu X, Wei L, Tang D, Sun P, Bartlam M, Rao Z: An insight into the mechanism of human cysteine dioxygenase. Key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem. 2007 Feb 2;282(5):3391-402. Epub 2006 Nov 29. [PubMed:17135237]
  4. Jin HF, DU SX, Zhao X, Zhang SQ, Tian Y, Bu DF, Tang CS, DU JB: [Significance of endogenous sulfur dioxide in the regulation of cardiovascular system]. Beijing Da Xue Xue Bao. 2007 Aug 18;39(4):423-5. [PubMed:17657274]

Transporters

Kind
Protein
Organism
Humans
Pharmacological action
Unknown
Actions
Inhibitor
General Function
Transporter activity
Specific Function
Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells (By similarity).
Gene Name
SLC16A10
Uniprot ID
Q8TF71
Uniprot Name
Monocarboxylate transporter 10
Molecular Weight
55492.07 Da
References
  1. Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. [PubMed:11278508]

Drug created on June 13, 2005 07:24 / Updated on October 21, 2020 01:55

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