Proteins > Solute carrier family 22 member 1
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Solute carrier family 22 member 1
A solute carrier family 22 member 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O15245]
Synonyms
Organic cation transporter 1;
hOCT1
Research
Bioassay Publications (19)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (15.79) | 18.2507 |
| 2000's | 8 (42.11) | 29.6817 |
| 2010's | 8 (42.11) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Compounds (134)
Drugs with Inhibition Measurements
Drugs with Other Measurements
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2.Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Discovery of potent, selective multidrug and toxin extrusion transporter 1 (MATE1, SLC47A1) inhibitors through prescription drug profiling and computational modeling.Journal of medicinal chemistry, , Feb-14, Volume: 56, Issue:3, 2013
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2.Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2.Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2.Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Discovery of potent, selective multidrug and toxin extrusion transporter 1 (MATE1, SLC47A1) inhibitors through prescription drug profiling and computational modeling.Journal of medicinal chemistry, , Feb-14, Volume: 56, Issue:3, 2013
Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2.Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Profiling of a prescription drug library for potential renal drug-drug interactions mediated by the organic cation transporter 2.Journal of medicinal chemistry, , Jul-14, Volume: 54, Issue:13, 2011
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3.British journal of pharmacology, , Volume: 136, Issue:6, 2002
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3.British journal of pharmacology, , Volume: 136, Issue:6, 2002
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Kinetic and selectivity differences between rodent, rabbit, and human organic cation transporters (OCT1).The Journal of pharmacology and experimental therapeutics, , Volume: 292, Issue:3, 2000
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Cloning and functional expression of a human liver organic cation transporter.Molecular pharmacology, , Volume: 51, Issue:6, 1997
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Kinetic and selectivity differences between rodent, rabbit, and human organic cation transporters (OCT1).The Journal of pharmacology and experimental therapeutics, , Volume: 292, Issue:3, 2000
The interaction of n-tetraalkylammonium compounds with a human organic cation transporter, hOCT1.The Journal of pharmacology and experimental therapeutics, , Volume: 288, Issue:3, 1999
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Kinetic and selectivity differences between rodent, rabbit, and human organic cation transporters (OCT1).The Journal of pharmacology and experimental therapeutics, , Volume: 292, Issue:3, 2000
The interaction of n-tetraalkylammonium compounds with a human organic cation transporter, hOCT1.The Journal of pharmacology and experimental therapeutics, , Volume: 288, Issue:3, 1999
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
Agmatine is efficiently transported by non-neuronal monoamine transporters extraneuronal monoamine transporter (EMT) and organic cation transporter 2 (OCT2).The Journal of pharmacology and experimental therapeutics, , Volume: 304, Issue:2, 2003
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Cloning and functional expression of a human liver organic cation transporter.Molecular pharmacology, , Volume: 51, Issue:6, 1997
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Influence of molecular structure on substrate binding to the human organic cation transporter, hOCT1.Molecular pharmacology, , Volume: 63, Issue:3, 2003
The interaction of n-tetraalkylammonium compounds with a human organic cation transporter, hOCT1.The Journal of pharmacology and experimental therapeutics, , Volume: 288, Issue:3, 1999
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Opioids as Substrates and Inhibitors of the Genetically Highly Variable Organic Cation Transporter OCT1.Journal of medicinal chemistry, , 11-14, Volume: 62, Issue:21, 2019
Structural requirements for drug inhibition of the liver specific human organic cation transport protein 1.Journal of medicinal chemistry, , Oct-09, Volume: 51, Issue:19, 2008
Opioids as Substrates and Inhibitors of the Genetically Highly Variable Organic Cation Transporter OCT1.Journal of medicinal chemistry, , 11-14, Volume: 62, Issue:21, 2019
Discovery of Competitive and Noncompetitive Ligands of the Organic Cation Transporter 1 (OCT1; SLC22A1).Journal of medicinal chemistry, , 04-13, Volume: 60, Issue:7, 2017
Expression and pharmacological profile of the human organic cation transporters hOCT1, hOCT2 and hOCT3.British journal of pharmacology, , Volume: 136, Issue:6, 2002
Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa).The Journal of pharmacology and experimental therapeutics, , Volume: 286, Issue:1, 1998
Cloning and functional expression of a human liver organic cation transporter.Molecular pharmacology, , Volume: 51, Issue:6, 1997
Enables
This protein enables 19 target(s):
| Target | Category | Definition |
|---|
| acetylcholine transmembrane transporter activity | molecular function | Enables the transfer of acetylcholine from one side of a membrane to the other. Acetylcholine is an acetic acid ester of the organic base choline and functions as a neurotransmitter, released at the synapses of parasympathetic nerves and at neuromuscular junctions. [GOC:ai] |
| neurotransmitter transmembrane transporter activity | molecular function | Enables the directed movement of a neurotransmitter into, out of or within a cell, or between cells. Neurotransmitters are any chemical substance that is capable of transmitting (or inhibiting the transmission of) a nerve impulse from a neuron to another cell. [GOC:ai, ISBN:0198506732] |
| dopamine:sodium symporter activity | molecular function | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: dopamine(out) + Na+(out) + Cl-(out)= dopamine(in) + Na+(in) + Cl-(in). [PMID:21752877, PMID:22519513, TC:2.A.22.1.3] |
| norepinephrine:sodium symporter activity | molecular function | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: norepinephrine(out) + Na+(out) + Cl-(out) = norepinephrine(in) + Na+(in) + Cl-(in). [PMID:21752877, PMID:22519513, TC:2.A.22.1.2] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| monoamine transmembrane transporter activity | molecular function | Enables the transfer of monoamines, organic compounds that contain one amino group that is connected to an aromatic ring by an ethylene group (-CH2-CH2-), from one side of a membrane to the other. [GOC:mah] |
| secondary active organic cation transmembrane transporter activity | molecular function | Enables the transfer of organic cations from one side of a membrane to the other, up the solute's concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction. [GOC:curators] |
| organic anion transmembrane transporter activity | molecular function | Enables the transfer of organic anions from one side of a membrane to the other. Organic anions are atoms or small molecules with a negative charge which contain carbon in covalent linkage. [GOC:ai] |
| organic cation transmembrane transporter activity | molecular function | Enables the transfer of organic cations from one side of a membrane to the other. Organic cations are atoms or small molecules with a positive charge that contain carbon in covalent linkage. [GOC:ai, GOC:mtg_transport, ISBN:0815340729] |
| prostaglandin transmembrane transporter activity | molecular function | Enables the transfer of prostaglandins from one side of a membrane to the other. A prostaglandin is any of a group of biologically active metabolites which contain a cyclopentane ring due to the formation of a bond between two carbons of a fatty acid. They have a wide range of biological activities. [GOC:ai] |
| pyrimidine nucleoside transmembrane transporter activity | molecular function | Enables the transfer of a pyrimidine nucleoside, a pyrimidine base covalently bonded to a ribose or deoxyribose sugar from one side of a membrane to the other. [GOC:ai] |
| thiamine transmembrane transporter activity | molecular function | Enables the transfer of thiamine from one side of a membrane to the other. Thiamine is vitamin B1, a water soluble vitamin present in fresh vegetables and meats, especially liver. [GOC:ai, GOC:mtg_transport, ISBN:0815340729] |
| putrescine transmembrane transporter activity | molecular function | Enables the transfer of putrescine from one side of a membrane to the other. Putrescine is 1,4-diaminobutane, the polyamine formed by decarboxylation of ornithine and the metabolic precursor of spermidine and spermine. [GOC:ai] |
| spermidine transmembrane transporter activity | molecular function | Enables the transfer of spermidine, N-(3-aminopropyl)-1,4-diaminobutane, from one side of a membrane to the other. [GOC:ai, RHEA:35039] |
| quaternary ammonium group transmembrane transporter activity | molecular function | Enables the transfer of quaternary ammonium groups from one side of a membrane to the other. Quaternary ammonium groups are any compound that can be regarded as derived from ammonium hydroxide or an ammonium salt by replacement of all four hydrogen atoms of the NH4+ ion by organic groups. [ISBN:0198506732] |
| toxin transmembrane transporter activity | molecular function | Enables the transfer of a toxin from one side of a membrane to the other. A toxin is a poisonous compound (typically a protein) that is produced by cells or organisms and that can cause disease when introduced into the body or tissues of an organism. [ISBN:0198506732] |
| identical protein binding | molecular function | Binding to an identical protein or proteins. [GOC:jl] |
| xenobiotic transmembrane transporter activity | molecular function | Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. [GOC:go_curators, GOC:krc] |
| (R)-carnitine transmembrane transporter activity | molecular function | Enables the transfer of (R)-carnitine from one side of a membrane to the other. [GOC:TermGenie, PMID:16365042, PMID:20357772, PMID:20829798] |
Located In
This protein is located in 7 target(s):
| Target | Category | Definition |
|---|
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| basal plasma membrane | cellular component | The region of the plasma membrane located at the basal end of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis. [GOC:go_curators] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| basolateral plasma membrane | cellular component | The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis. [GOC:go_curators] |
| apical plasma membrane | cellular component | The region of the plasma membrane located at the apical end of the cell. [GOC:curators] |
| lateral plasma membrane | cellular component | The portion of the plasma membrane at the lateral side of the cell. In epithelial cells, lateral plasma membranes are on the sides of cells which lie at the interface of adjacent cells. [GOC:hb, GOC:mah, GOC:pr] |
| presynapse | cellular component | The part of a synapse that is part of the presynaptic cell. [GOC:dos] |
Involved In
This protein is involved in 29 target(s):
| Target | Category | Definition |
|---|
| xenobiotic metabolic process | biological process | The chemical reactions and pathways involving a xenobiotic compound, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. [GOC:cab2, GOC:krc] |
| neurotransmitter transport | biological process | The directed movement of a neurotransmitter into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Neurotransmitters are any chemical substance that is capable of transmitting (or inhibiting the transmission of) a nerve impulse from a neuron to another cell. [GOC:ai] |
| serotonin transport | biological process | The directed movement of serotonin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Serotonin (5-hydroxytryptamine) is a monoamine neurotransmitter occurring in the peripheral and central nervous systems. [GOC:ai] |
| establishment or maintenance of transmembrane electrochemical gradient | biological process | The directed movement of ions to establish or maintain an electrochemical gradient across a membrane by means of some agent such as a transporter or pore. [GOC:mah, GOC:sm] |
| organic cation transport | biological process | The directed movement of organic cations into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Organic cations are atoms or small molecules with a positive charge which contain carbon in covalent linkage. [GOC:ai] |
| quaternary ammonium group transport | biological process | The directed movement into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore of quaternary ammonium compounds, any compound that can be regarded as derived from ammonium hydroxide or an ammonium salt by replacement of all four hydrogen atoms of the NH4+ ion by organic groups. [GOC:ai, ISBN:0198506732] |
| prostaglandin transport | biological process | The directed movement of prostaglandins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:krc] |
| monoamine transport | biological process | The directed movement of monoamines, organic compounds that contain one amino group that is connected to an aromatic ring by an ethylene group (-CH2-CH2-), into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:mah] |
| putrescine transport | biological process | The directed movement of putrescine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Putrescine is 1,4-diaminobutane, the polyamine formed by decarboxylation of ornithine and the metabolic precursor of spermidine and spermine. [GOC:krc, ISBN:0198506732] |
| spermidine transport | biological process | The directed movement of spermidine, N-(3-aminopropyl)-1,4-diaminobutane, a polyamine formed by the transfer of a propylamine group from decarboxylated S-adenosylmethionine to putrescine, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:krc, ISBN:0198506732] |
| acetylcholine transport | biological process | The directed movement of acetylcholine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Acetylcholine is an acetic acid ester of the organic base choline and functions as a neurotransmitter, released at the synapses of parasympathetic nerves and at neuromuscular junctions. [GOC:ai] |
| dopamine transport | biological process | The directed movement of dopamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Dopamine is a catecholamine neurotransmitter and a metabolic precursor of noradrenaline and adrenaline. [GOC:ai] |
| norepinephrine transport | biological process | The directed movement of norepinephrine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Norepinephrine (3,4-dihydroxyphenyl-2-aminoethanol) is a hormone secreted by the adrenal medulla and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts of the CNS. It is also the biosynthetic precursor of epinephrine. [GOC:ai, ISBN:0198506732] |
| thiamine transport | biological process | The directed movement of thiamine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Thiamine is vitamin B1, a water soluble vitamin present in fresh vegetables and meats, especially liver. [GOC:ai] |
| xenobiotic transport | biological process | The directed movement of a xenobiotic into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. A xenobiotic is a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. [GOC:go_curators, GOC:krc] |
| epinephrine transport | biological process | The directed movement of epinephrine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:jid] |
| serotonin uptake | biological process | The directed movement of serotonin into a cell, typically presynaptic neurons or glial cells. Serotonin (5-hydroxytryptamine) is a monoamine neurotransmitter occurring in the peripheral and central nervous systems. [GOC:ai] |
| norepinephrine uptake | biological process | The directed movement of norepinephrine into a cell, typically presynaptic neurons or glial cells. Norepinephrine (3,4-dihydroxyphenyl-2-aminoethanol) is a hormone secreted by the adrenal medulla and a neurotransmitter in the sympathetic peripheral nervous system and in some tracts of the CNS. It is also the biosynthetic precursor of epinephrine. [GOC:ai] |
| thiamine transmembrane transport | biological process | The process in which thiamine is transported across a membrane. Thiamine is vitamin B1, a water soluble vitamin present in fresh vegetables and meats, especially liver. [GOC:mah] |
| metanephric proximal tubule development | biological process | The process whose specific outcome is the progression of the metanephric proximal tubule over time, from its formation to the mature structure. The metanephric proximal tubule is a metanephric nephron tubule that connects Bowman's capsule to the descending thin limb of the loop of Henle in the metanephros. It has a brush border epithelial morphology. [GOC:mtg_kidney_jan10] |
| purine-containing compound transmembrane transport | biological process | The process in which a purine-containing compound is transported across a membrane. A purine-containing compound is any compound that contains purine or a formal derivative thereof. [GOC:mah] |
| dopamine uptake | biological process | The directed movement of dopamine into a cell. [GOC:dph, GOC:tb] |
| monoatomic cation transmembrane transport | biological process | The process in which a monoatomic cation is transported across a membrane. Monatomic cations (also called simple cations) are positively charged ions consisting of exactly one atom. [GOC:dos, GOC:vw] |
| transport across blood-brain barrier | biological process | The directed movement of substances (e.g. macromolecules, small molecules, ions) through the blood-brain barrier. [GOC:aruk, GOC:bc, PMID:29377008] |
| (R)-carnitine transmembrane transport | biological process | The process in which (R)-carnitine is transported across a membrane. [GOC:TermGenie, PMID:23755272] |
| acyl carnitine transmembrane transport | biological process | The process in which acyl carnitine is transported across a membrane. [GO_REF:0000069, GOC:pr, GOC:TermGenie] |
| spermidine transmembrane transport | biological process | The process in which spermidine is transported across a membrane. [GO_REF:0000069, GOC:TermGenie, PMID:15637075] |
| cellular detoxification | biological process | Any process carried out at the cellular level that reduces or removes the toxicity of a toxic substance. These may include transport of the toxic substance away from sensitive areas and to compartments or complexes whose purpose is sequestration of the toxic substance. [GOC:vw] |
| xenobiotic transport across blood-brain barrier | biological process | The directed movement of a xenobiotic through the blood-brain barrier. [PMID:25053619] |