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  1. Article ; Online: Co-option of a conserved host glutamine transporter facilitates aphid/

    Duncan, Rebecca P / Anderson, Catriona M H / Thwaites, David T / Luetje, Charles W / Wilson, Alex C C

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 43, Page(s) e2308448120

    Abstract: Organisms across the tree of life colonize novel environments by partnering with bacterial symbionts. These symbioses are characterized by intimate integration of host/endosymbiont biology at multiple levels, including metabolically. Metabolic ... ...

    Abstract Organisms across the tree of life colonize novel environments by partnering with bacterial symbionts. These symbioses are characterized by intimate integration of host/endosymbiont biology at multiple levels, including metabolically. Metabolic integration is particularly important for sap-feeding insects and their symbionts, which supplement nutritionally unbalanced host diets. Many studies reveal parallel evolution of host/endosymbiont metabolic complementarity in amino acid biosynthesis, raising questions about how amino acid metabolism is regulated, how regulatory mechanisms evolve, and the extent to which similar mechanisms evolve in different systems. In the aphid/
    MeSH term(s) Animals ; Glutamine/metabolism ; Aphids/microbiology ; Buchnera/genetics ; Buchnera/metabolism ; Amino Acids/metabolism ; Membrane Transport Proteins/metabolism ; Arginine/metabolism ; Symbiosis/physiology
    Chemical Substances Glutamine (0RH81L854J) ; Amino Acids ; Membrane Transport Proteins ; Arginine (94ZLA3W45F)
    Language English
    Publishing date 2023-10-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2308448120
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  2. Article ; Online: Reshaping the Binding Pocket of the Neurotransmitter:Solute Symporter (NSS) Family Transporter SLC6A14 (ATB<sup>0,+</sup>) Selectively Reduces Access for Cationic Amino Acids and Derivatives.

    Anderson, Catriona M H / Edwards, Noel / Watson, Andrew K / Althaus, Mike / Thwaites, David T

    Biomolecules

    2022  Volume 12, Issue 10

    Abstract: SLC6A14 (ATB ... 0,+ ... ) is unique among SLC proteins in its ability to transport 18 of the 20 proteinogenic (dipolar and cationic) amino acids and naturally occurring and synthetic analogues (including anti-viral prodrugs and nitric oxide synthase ( ... ...

    Abstract SLC6A14 (ATB<sup>0,+</sup>) is unique among SLC proteins in its ability to transport 18 of the 20 proteinogenic (dipolar and cationic) amino acids and naturally occurring and synthetic analogues (including anti-viral prodrugs and nitric oxide synthase (NOS) inhibitors). SLC6A14 mediates amino acid uptake in multiple cell types where increased expression is associated with pathophysiological conditions including some cancers. Here, we investigated how a key position within the core LeuT-fold structure of SLC6A14 influences substrate specificity. Homology modelling and sequence analysis identified the transmembrane domain 3 residue V128 as equivalent to a position known to influence substrate specificity in distantly related SLC36 and SLC38 amino acid transporters. SLC6A14, with and without V128 mutations, was heterologously expressed and function determined by radiotracer solute uptake and electrophysiological measurement of transporter-associated current. Substituting the amino acid residue occupying the SLC6A14 128 position modified the binding pocket environment and selectively disrupted transport of cationic (but not dipolar) amino acids and related NOS inhibitors. By understanding the molecular basis of amino acid transporter substrate specificity we can improve knowledge of how this multi-functional transporter can be targeted and how the LeuT-fold facilitates such diversity in function among the SLC6 family and other SLC amino acid transporters.
    MeSH term(s) Amino Acids/metabolism ; Prodrugs ; Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Nitric Oxide Synthase/metabolism ; Neurotransmitter Agents
    Chemical Substances Amino Acids ; Prodrugs ; Amino Acid Transport Systems ; Nitric Oxide Synthase (EC 1.14.13.39) ; Neurotransmitter Agents
    Language English
    Publishing date 2022-10-01
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom12101404
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  3. Article ; Online: The SLC36 family of proton-coupled amino acid transporters and their potential role in drug transport.

    Thwaites, David T / Anderson, Catriona M H

    British journal of pharmacology

    2011  Volume 164, Issue 7, Page(s) 1802–1816

    Abstract: Members of the solute carrier (SLC) 36 family are involved in transmembrane movement of amino acids and derivatives. SLC36 consists of four members. SLC36A1 and SLC36A2 both function as H(+) -coupled amino acid symporters. SLC36A1 is expressed at the ... ...

    Abstract Members of the solute carrier (SLC) 36 family are involved in transmembrane movement of amino acids and derivatives. SLC36 consists of four members. SLC36A1 and SLC36A2 both function as H(+) -coupled amino acid symporters. SLC36A1 is expressed at the luminal surface of the small intestine but is also commonly found in lysosomes in many cell types (including neurones), suggesting that it is a multipurpose carrier with distinct roles in different cells including absorption in the small intestine and as an efflux pathway following intralysosomal protein breakdown. SLC36A1 has a relatively low affinity (K(m) 1-10 mM) for its substrates, which include zwitterionic amino and imino acids, heterocyclic amino acids and amino acid-based drugs and derivatives used experimentally and/or clinically to treat epilepsy, schizophrenia, bacterial infections, hyperglycaemia and cancer. SLC36A2 is expressed at the apical surface of the human renal proximal tubule where it functions in the reabsorption of glycine, proline and hydroxyproline. SLC36A2 also transports amino acid derivatives but has a narrower substrate selectivity and higher affinity (K(m) 0.1-0.7 mM) than SLC36A1. Mutations in SLC36A2 lead to hyperglycinuria and iminoglycinuria. SLC36A3 is expressed only in testes and is an orphan transporter with no known function. SLC36A4 is widely distributed at the mRNA level and is a high-affinity (K(m) 2-3 µM) transporter for proline and tryptophan. We have much to learn about this family of transporters, but from current knowledge, it seems likely that their function will influence the pharmacokinetic profiles of amino acid-based drugs by mediating transport in both the small intestine and kidney.
    MeSH term(s) Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Amino Acids/metabolism ; Animals ; Biological Transport ; Humans ; Intestine, Small/metabolism ; Kidney/metabolism ; Pharmaceutical Preparations/metabolism ; Tissue Distribution
    Chemical Substances Amino Acid Transport Systems ; Amino Acids ; Pharmaceutical Preparations
    Language English
    Publishing date 2011-06-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 80081-8
    ISSN 1476-5381 ; 0007-1188
    ISSN (online) 1476-5381
    ISSN 0007-1188
    DOI 10.1111/j.1476-5381.2011.01438.x
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  4. Article ; Online: Hijacking solute carriers for proton-coupled drug transport.

    Anderson, Catriona M H / Thwaites, David T

    Physiology (Bethesda, Md.)

    2010  Volume 25, Issue 6, Page(s) 364–377

    Abstract: The physiological role of mammalian solute carrier (SLC) proteins is to mediate transmembrane movement of electrolytes, nutrients, micronutrients, vitamins, and endogenous metabolites from one cellular compartment to another. Many transporters in the ... ...

    Abstract The physiological role of mammalian solute carrier (SLC) proteins is to mediate transmembrane movement of electrolytes, nutrients, micronutrients, vitamins, and endogenous metabolites from one cellular compartment to another. Many transporters in the small intestine, kidney, and solid tumors are H(+)-coupled, driven by local H(+)-electrochemical gradients, and transport numerous drugs. These transporters include PepT1 and PepT2 (SLC15A1/2), PCFT (SLC46A1), PAT1 (SLC36A1), OAT10 (SLC22A13), OATP2B1 (SLCO2B1), MCT1 (SLC16A1), and MATE1 and MATE2-K (SLC47A1/2).
    MeSH term(s) Animals ; Antiporters/metabolism ; Biological Transport ; Humans ; Hydrogen-Ion Concentration ; Intestine, Small/metabolism ; Kidney Tubules, Proximal/metabolism ; Neoplasms/metabolism ; Pharmaceutical Preparations/metabolism ; Protons ; Symporters/metabolism
    Chemical Substances Antiporters ; Pharmaceutical Preparations ; Protons ; Symporters
    Language English
    Publishing date 2010-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2158667-6
    ISSN 1548-9221 ; 1548-9213
    ISSN (online) 1548-9221
    ISSN 1548-9213
    DOI 10.1152/physiol.00027.2010
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    Zs.A 2164: Show issues Location:
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  5. Article ; Online: Resculpting the binding pocket of APC superfamily LeuT-fold amino acid transporters.

    Edwards, Noel / Anderson, Catriona M H / Conlon, Nichola J / Watson, Andrew K / Hall, Rebecca J / Cheek, Timothy R / Embley, T Martin / Thwaites, David T

    Cellular and molecular life sciences : CMLS

    2017  Volume 75, Issue 5, Page(s) 921–938

    Abstract: Amino acid transporters are essential components of prokaryote and eukaryote cells, possess distinct physiological functions, and differ markedly in substrate specificity. Amino acid transporters can be both drug targets and drug transporters ( ... ...

    Abstract Amino acid transporters are essential components of prokaryote and eukaryote cells, possess distinct physiological functions, and differ markedly in substrate specificity. Amino acid transporters can be both drug targets and drug transporters (bioavailability, targeting) with many monogenic disorders resulting from dysfunctional membrane transport. The largest collection of amino acid transporters (including the mammalian SLC6, SLC7, SLC32, SLC36, and SLC38 families), across all kingdoms of life, is within the Amino acid-Polyamine-organoCation (APC) superfamily. The LeuT-fold is a paradigm structure for APC superfamily amino acid transporters and carriers of sugars, neurotransmitters, electrolytes, osmolytes, vitamins, micronutrients, signalling molecules, and organic and fatty acids. Each transporter is specific for a unique sub-set of solutes, specificity being determined by how well a substrate fits into each binding pocket. However, the molecular basis of substrate selectivity remains, by and large, elusive. Using an integrated computational and experimental approach, we demonstrate that a single position within the LeuT-fold can play a crucial role in determining substrate specificity in mammalian and arthropod amino acid transporters within the APC superfamily. Systematic mutation of the amino acid residue occupying the equivalent position to LeuT V104 titrates binding pocket space resulting in dramatic changes in substrate selectivity in exemplar APC amino acid transporters including PAT2 (SLC36A2) and SNAT5 (SLC38A5). Our work demonstrates how a single residue/site within an archetypal structural motif can alter substrate affinity and selectivity within this important superfamily of diverse membrane transporters.
    MeSH term(s) Amino Acid Transport Systems/chemistry ; Amino Acid Transport Systems/genetics ; Amino Acid Transport Systems/metabolism ; Amino Acids/metabolism ; Animals ; Biological Transport ; Catalytic Domain/genetics ; Humans ; Models, Molecular ; Multigene Family ; Mutagenesis, Site-Directed ; Phylogeny ; Protein Interaction Domains and Motifs/genetics ; Substrate Specificity/genetics
    Chemical Substances Amino Acid Transport Systems ; Amino Acids
    Language English
    Publishing date 2017-10-23
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1358415-7
    ISSN 1420-9071 ; 1420-682X
    ISSN (online) 1420-9071
    ISSN 1420-682X
    DOI 10.1007/s00018-017-2677-8
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  6. Article ; Online: The Concise Guide to PHARMACOLOGY 2023/24: Transporters.

    Alexander, Stephen P H / Fabbro, Doriano / Kelly, Eamonn / Mathie, Alistair A / Peters, John A / Veale, Emma L / Armstrong, Jane F / Faccenda, Elena / Harding, Simon D / Davies, Jamie A / Amarosi, Laura / Anderson, Catriona M H / Beart, Philip M / Broer, Stefan / Dawson, Paul A / Gyimesi, Gergely / Hagenbuch, Bruno / Hammond, James R / Hancox, Jules C /
    Hershfinkel, Michal / Inui, Ken-Ichi / Kanai, Yoshikatsu / Kemp, Stephan / Kunji, Edmund R S / Stewart, Gavin / Tavoulari, Sotiria / Thwaites, David T / Verri, Tiziano

    British journal of pharmacology

    2023  Volume 180 Suppl 2, Page(s) S374–S469

    Abstract: The Concise Guide to PHARMACOLOGY 2023/24 is the sixth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of approximately 1800 drug targets, and over 6000 interactions ... ...

    Abstract The Concise Guide to PHARMACOLOGY 2023/24 is the sixth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of approximately 1800 drug targets, and over 6000 interactions with about 3900 ligands. There is an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (https://www.guidetopharmacology.org/), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes almost 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.16182. Transporters are one of the six major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ion channels, nuclear hormone receptors, catalytic receptors and enzymes. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2023, and supersedes data presented in the 2021/22, 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
    MeSH term(s) Humans ; Databases, Pharmaceutical ; Ligands ; Ion Channels/chemistry ; Receptors, G-Protein-Coupled ; Receptors, Cytoplasmic and Nuclear ; Pharmacology
    Chemical Substances Ligands ; Ion Channels ; Receptors, G-Protein-Coupled ; Receptors, Cytoplasmic and Nuclear
    Language English
    Publishing date 2023-12-19
    Publishing country England
    Document type Journal Article
    ZDB-ID 80081-8
    ISSN 1476-5381 ; 0007-1188
    ISSN (online) 1476-5381
    ISSN 0007-1188
    DOI 10.1111/bph.16182
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  7. Article ; Online: Trading amino acids at the aphid-

    Feng, Honglin / Edwards, Noel / Anderson, Catriona M H / Althaus, Mike / Duncan, Rebecca P / Hsu, Yu-Ching / Luetje, Charles W / Price, Daniel R G / Wilson, Alex C C / Thwaites, David T

    Proceedings of the National Academy of Sciences of the United States of America

    2019  Volume 116, Issue 32, Page(s) 16003–16011

    Abstract: Plant sap-feeding insects are widespread, having evolved to occupy diverse environmental niches despite exclusive feeding on an impoverished diet lacking in essential amino acids and vitamins. Success depends exquisitely on their symbiotic relationships ... ...

    Abstract Plant sap-feeding insects are widespread, having evolved to occupy diverse environmental niches despite exclusive feeding on an impoverished diet lacking in essential amino acids and vitamins. Success depends exquisitely on their symbiotic relationships with microbial symbionts housed within specialized eukaryotic bacteriocyte cells. Each bacteriocyte is packed with symbionts that are individually surrounded by a host-derived symbiosomal membrane representing the absolute host-symbiont interface. The symbiosomal membrane must be a dynamic and selectively permeable structure to enable bidirectional and differential movement of essential nutrients, metabolites, and biosynthetic intermediates, vital for growth and survival of host and symbiont. However, despite this crucial role, the molecular basis of membrane transport across the symbiosomal membrane remains unresolved in all bacteriocyte-containing insects. A transport protein was immunolocalized to the symbiosomal membrane separating the pea aphid
    MeSH term(s) Amino Acid Sequence ; Amino Acids/metabolism ; Animals ; Aphids/metabolism ; Buchnera/metabolism ; Insect Proteins/metabolism ; Models, Biological ; Phylogeny ; Symbiosis
    Chemical Substances Amino Acids ; Insect Proteins
    Language English
    Publishing date 2019-07-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1906223116
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  8. Article ; Online: SLC6A14, a Pivotal Actor on Cancer Stage: When Function Meets Structure.

    Palazzolo, Luca / Paravicini, Chiara / Laurenzi, Tommaso / Adobati, Sara / Saporiti, Simona / Guerrini, Uliano / Gianazza, Elisabetta / Indiveri, Cesare / Anderson, Catriona M H / Thwaites, David T / Eberini, Ivano

    SLAS discovery : advancing life sciences R & D

    2019  Volume 24, Issue 9, Page(s) 928–938

    Abstract: ... SLC6A14 ( ... ...

    Abstract SLC6A14 (ATB
    MeSH term(s) Amino Acid Transport Systems/metabolism ; Amino Acids/metabolism ; Binding Sites/physiology ; Cell Membrane/metabolism ; Humans ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Neoplasm Staging/methods ; Neoplasms/metabolism ; Neoplasms/pathology ; Protein Conformation, alpha-Helical/physiology
    Chemical Substances Amino Acid Transport Systems ; Amino Acids ; SLC6A14 protein, human
    Language English
    Publishing date 2019-08-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2885123-7
    ISSN 2472-5560 ; 2472-5552
    ISSN (online) 2472-5560
    ISSN 2472-5552
    DOI 10.1177/2472555219867317
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  9. Article ; Online: Human solute carrier SLC6A14 is the beta-alanine carrier.

    Anderson, Catriona M H / Ganapathy, Vadivel / Thwaites, David T

    The Journal of physiology

    2008  Volume 586, Issue 17, Page(s) 4061–4067

    Abstract: The beta-alanine carrier was characterized functionally in the 1960s to 1980s at the luminal surface of the ileal mucosal wall and is a Na(+)- and Cl(-)-dependent transporter of a number of essential and non-essential cationic and dipolar amino acids ... ...

    Abstract The beta-alanine carrier was characterized functionally in the 1960s to 1980s at the luminal surface of the ileal mucosal wall and is a Na(+)- and Cl(-)-dependent transporter of a number of essential and non-essential cationic and dipolar amino acids including lysine, arginine and leucine. beta-Alanine carrier-like function has not been demonstrated by any solute carrier transport system identified at the molecular level. A series of experiments were designed to determine whether solute carrier SLC6A14 is the molecular correlate of the intestinal beta-alanine carrier, perhaps the last of the classical intestinal amino acid transport systems to be identified at the molecular level. Following expression of the human SLC6A14 transporter in Xenopus laevis oocytes, the key functional characteristics of the beta-alanine carrier, identified previously in situ in ileum, were demonstrated for the first time. The transport system is both Na(+) and Cl(-) dependent, can transport non-alpha-amino acids such as beta-alanine with low affinity, and has a higher affinity for dipolar and cationic amino acids such as leucine and lysine. N-methylation of its substrates reduces the affinity for transport. These observations confirm the hypothesis that the SLC6A14 gene encodes the transport protein known as the beta-alanine carrier which, due to its broad substrate specificity, is likely to play an important role in absorption of essential nutrients and drugs in the distal regions of the human gastrointestinal tract.
    MeSH term(s) Amino Acid Transport Systems ; Amino Acid Transport Systems, Neutral/metabolism ; Animals ; Gene Expression Regulation/physiology ; Humans ; Oocytes ; Xenopus laevis ; beta-Alanine/metabolism
    Chemical Substances Amino Acid Transport Systems ; Amino Acid Transport Systems, Neutral ; SLC6A14 protein, human ; beta-Alanine (11P2JDE17B)
    Language English
    Publishing date 2008-07-03
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3115-x
    ISSN 1469-7793 ; 0022-3751
    ISSN (online) 1469-7793
    ISSN 0022-3751
    DOI 10.1113/jphysiol.2008.154500
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  10. Article ; Online: THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: Transporters.

    Alexander, Stephen Ph / Kelly, Eamonn / Mathie, Alistair / Peters, John A / Veale, Emma L / Armstrong, Jane F / Faccenda, Elena / Harding, Simon D / Pawson, Adam J / Southan, Christopher / Davies, Jamie A / Amarosi, Laura / Anderson, Catriona M H / Beart, Philip Mark / Broer, Stefan / Dawson, Paul A / Hagenbuch, Bruno / Hammond, James R / Inui, Ken-Ichi /
    Kanai, Yoshikatsu / Kemp, Stephan / Stewart, Gavin / Thwaites, David T / Verri, Tiziano

    British journal of pharmacology

    2021  Volume 178 Suppl 1, Page(s) S412–S513

    Abstract: The Concise Guide to PHARMACOLOGY 2021/22 is the fifth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of nearly 1900 human drug targets with an emphasis on selective ... ...

    Abstract The Concise Guide to PHARMACOLOGY 2021/22 is the fifth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of nearly 1900 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes over 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/bph.15543. Transporters are one of the six major pharmacological targets into which the Guide is divided, with the others being: G protein-coupled receptors, ion channels, nuclear hormone receptors, catalytic receptors and enzymes. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2021, and supersedes data presented in the 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
    MeSH term(s) Databases, Pharmaceutical ; Humans ; Ion Channels ; Ligands ; Pharmacology ; Receptors, Cytoplasmic and Nuclear ; Receptors, G-Protein-Coupled
    Chemical Substances Ion Channels ; Ligands ; Receptors, Cytoplasmic and Nuclear ; Receptors, G-Protein-Coupled
    Language English
    Publishing date 2021-09-16
    Publishing country England
    Document type Journal Article
    ZDB-ID 80081-8
    ISSN 1476-5381 ; 0007-1188
    ISSN (online) 1476-5381
    ISSN 0007-1188
    DOI 10.1111/bph.15543
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