WorldCat Identities

Catterall, William A. 1946-

Works: 20 works in 31 publications in 1 language and 108 library holdings
Genres: Classification  Academic theses  Handbooks and manuals 
Roles: Author, Thesis advisor
Classifications: RM300, 615.7
Publication Timeline
Most widely held works about William A Catterall
Most widely held works by William A Catterall
Goodman & Gilman's the pharmacological basis of therapeutics by Louis S Goodman( )

in English and held by 73 WorldCat member libraries worldwide

Three objectives are covered, the correlation of pharmacology with related medical sciences, the reinterpretation of the actions and uses of drugs from the viewpoint of important advances in medicine, and the placing of emphasis on the applications of pharmacodynamics to therapeutics. Presents the correlation of strictly pharmacological information with medicine as a whole in order for a proper presentation of pharmacology to students and physicians. Updated to reflect all critical new developments in drug action and drug-disease interaction
Molecular basis of paralytic neurotoxin action on voltage-sensitive sodium channels : annual summary report by William A Catterall( )

7 editions published between 1985 and 1989 in English and held by 7 WorldCat member libraries worldwide

In years 1 - 5 of this project, progress was made on several objectives: A. The sites and mechanisms of action on the sodium channel were examined and further defined for three new classes of neurotoxins: Goniopora toxins, Brevetoxins, and Conotoxins. B. Monoclonal antibodies with high affinity for the mammalian neuronal sodium channel were developed and methods to screen them for activity at neurotoxin binding sites were established. C. Site-directed antibodies against defined regions of the amino acid sequence of the sodium channel were prepared and shown to bind at discrete negatively charged subsites on the extracellular surface of the channel that may form part of neurotoxin receptor sites. Keywords: Ion transport; Sodium channels; Action potentials; Electrical excitability; Neurotoxins; RA 1. (kt)
Structural and catalytic properties of mitochnodrial ATPase by William A Catterall( )

4 editions published in 1972 in English and held by 5 WorldCat member libraries worldwide

The IUPHAR compendium of voltage-gated ion channels( Book )

1 edition published in 2002 in English and held by 5 WorldCat member libraries worldwide

Characterizing the role of sodium channels in mouse models of Dravet Syndrome by Christine Cheah( )

1 edition published in 2012 in English and held by 3 WorldCat member libraries worldwide

Voltage-gated sodium channels (Nav) are responsible for the initiation and propagation of action potentials in excitable cells. The channels isoforms Nav1.1, Nav1.2, Nav1.3 and Nav1.6 are dynamically expressed in the developing central nervous system and are essential for proper network function. Heterozygous loss-of-function mutations in SCN1A, the gene encoding Nav1.1, leads to Dravet Syndrome (DS), a pharmacoresistant infantile-onset epilepsy syndrome with co-morbidities of cognitive impairment and premature death. Previous studies using a mouse model of DS heterozygous for a global deletion of Scn1a (Scn1a+/- ), revealed reduced sodium currents and impaired excitability in GABAergic interneurons. We generated a floxed Scn1a mouse line and used the Cre-Lox method driven by an enhancer from the DLX1,2 locus to conditionally delete one or both copies of Scn1a in forebrain GABAergic neurons. Mice with this specific deletion had selective loss of NaV1.1 channels in GABAergic interneurons of the cerebral cortex and hippocampus, died prematurely following generalized tonic-clonic seizures, were equally susceptible to thermal induction of seizures as global Scn1a+/- mice, and demonstrated impaired cognitive function. Evidently, loss of NaV1.1 channels in forebrain GABAergic neurons is sufficient to cause epilepsy, premature death, and cognitive impairments in DS. Initial characterization of the DS mouse revealed a striking strain difference with respect to survival and seizure susceptibility. Studies also found an interneuron-specific increase in Nav1.3 with complete loss of Nav1.1, suggesting Nav1.3 as a possible precipitating factor or genetic modifier in DS. To evaluate the role of Nav1.3 in DS progression, we measured channel expression in non-epileptic mouse and human cortical tissue. We found Nav1.3 was expressed at high levels in embryonic life and declined after birth coincident with increased NaV1.1 channel expression in both species. The onset of seizures in mouse and human follows the developmental decrease in Nav1.3 to less than half of its maximal level suggesting that its loss, coupled with failure of normal expression of NaV1.1 channels, may contribute to the time of onset of seizures in DS. We tested whether genetic deletion of NaV1.3 channels would exacerbate the early phase of DS in mice and found that heterozygous loss of Nav1.3 does not lead to impaired survival or increased sensitivity to thermally induced seizures in DS mice. Our results support the hypothesis that declining expression of NaV1.3 channels to below 50% of maximum, in the face of heterozygous loss-of-function mutation of the NaV1.1 channel, may be one of the precipitating factors contributing to the time of onset of DS
Special issue on voltage-gated ion channels( Book )

2 editions published in 2005 in English and held by 2 WorldCat member libraries worldwide

Learning from nature how to design anti-insect selective pesticides : clarification of the interacting face between insecticidal toxins and sodium channel receptors, final report, project no. IS-3928-06 by United States-Israel Binational Agricultural Research and Development Fund( Book )

2 editions published in 2010 in English and held by 2 WorldCat member libraries worldwide

The concise guide to pharmacology 2013/14( )

1 edition published in 2013 in English and held by 1 WorldCat member library worldwide

The Concise Guide to PHARMACOLOGY 2013/14 provides concise overviews of the key properties of over 2000 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (, which provides more detailed views of target and ligand properties from the IUPHAR database. This compilation of the major pharmacological targets is divided into seven areas of focus: G protein-coupled receptors, ligand-gated ion channels, ion channels, catalytic receptors, nuclear hormone receptors, transporters 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. A new landscape format has easy to use tables comparing related targets. It is a condensed version of material contemporary to late 2013, which is presented in greater detail and constantly updated on the website, superseding data presented in previous Guides to Receptors & Channels. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates
Na+ channel function, regulation, structure, trafficking and sequestration( )

1 edition published in 2015 in English and held by 1 WorldCat member library worldwide

Abstract Abstract This paper is the second of a series of three reviews published in this issue resulting from the University of California Davis Cardiovascular Symposium 2014: Systems approach to understanding cardiac excitation-contraction coupling and arrhythmias: Na+ channel and Na+ transport. The goal of the symposium was to bring together experts in the field to discuss points of consensus and controversy on the topic of sodium in the heart. The present review focuses on Na+ channel function and regulation, Na+ channel structure and function, and Na+ channel trafficking, sequestration and complexing
Molecular studies of alpha-scorpion toxin interactions with voltage-gated sodium channels by Jinti Wang( )

1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

Voltage-gated sodium channels are responsible for initiation and propagation of the action potential in vertebrate nerve and muscle. They are also the molecular targets for a large number of paralytic neurotoxins. Alpha-scorpion toxins, including LqhII (Leiurus quinquestriatus hebraeus, type II), bind to the extracellular domain on the sodium channel and inhibit channel fast inactivation. Their binding prolongs sodium channel opening, leading to repetitive firing, depolarization and conduction block. As a consequence, these toxins can kill organisms by inducing paralysis and cardiac arrhythmia. Using site-directed mutagenesis, we have identified residues that constitute the functional interaction surfaces of alpha-scorpion toxin and its receptor site on the voltage-gated sodium channel. Mutants T1560A, F1610A, and E1613A in domain IV had lower affinities for LqhII, and mutant E1613R had ~73-fold lower affinity. Toxin dissociation was accelerated by depolarization and increased by these mutations, whereas association rates at negative membrane potentials were not changed. These results indicate that Thr1560 in the S1-S2 loop, Phe1610 in the S3 segment, and Glu1613 in the S3-S4 loop in domain IV participate in toxin binding. T393A in the SS2-S6 loop in domain I also had lower affinity for LqhII, indicating that this extracellular loop may form a secondary component of the receptor site. Analysis with the Rosetta-Membrane algorithm resulted in a model of LqhII binding to the voltage sensor in a resting state, in which amino acid residues in an extracellular cleft formed by the S1-S2 and S3-S4 loops in domain IV interact with two faces of the wedge-shaped LqhII molecule. The conserved gating charges in the S4 segment are in an inward position and form ion pairs with negatively charged amino acid residues in the S2 and S3 segments of the voltage sensor. This model defines the structure of the resting state of a voltage sensor of sodium channels and reveals its mode of interaction with a gating modifier toxin. The bioactive surface of LqhII has recently been shown to be made of a conserved core domain (Phe-15, Arg-18, Trp-38, and Asn-44) and a variable NC domain (Lys-2, Thr-57, Lys-58). In this work, possible interactions on surfaces of alpha-scorpion toxin and its receptor site on the voltage-gated sodium channel were tested by thermodynamic mutant cycle analysis. Single mutations at key amino acid residues important for activity on toxin and sodium channel were constructed by mutagenesis. We have identified an intermolecular interaction between extracellular loop of sodium channel and alpha-scorpion toxins. We demonstrated a specific aromatic-aromatic interaction between amino acid residue Phe1610 and Trp38 of LqhII, a residue that is conserved among many alpha-scorpion toxins. Toxin dissociation was accelerated by depolarization and increased by mutations at both sites, whereas association rates at negative membrane potentials were not changed for mutation at Phe1610, but slightly increased for mutation at Trp38. These results constrain the possible orientation of alpha-scorpion toxin with respect to the gating-module of DIV in sodium channel and suggest that upon interaction, the core-domain of LqhII is in close proximity to the sodium channel. We found that an antianginal and anti-ischemic drug, ranolazine, attenuated sustained Na+ current induced by alpha-scorpion toxin, with a 50% inhibitory concentration (IC50) of 102 ± 10.7 uM. It also attenuated the peak Na+ currents, with an IC50 of 334 ± 2.6 uM. The results demonstrate that ranolazine has antagonist effect against alpha-scorpion toxin. Consistent with this effect on sodium channels, ranolazine reduces the lethal paralytic effects of LqhII in mice
The IUPHAR compendium of voltage-gated ion channels( )

1 edition published in 2002 in English and held by 1 WorldCat member library worldwide

Structure and function of voltage‐gated sodium channels at atomic resolution( )

1 edition published in 2013 in English and held by 1 WorldCat member library worldwide

New Findings   What is the topic of this review? The central goal of the research reviewed here is to understand the functional properties of voltage‐gated sodium channels at the level of high‐resolution structure of the channel protein.   What advances does it highlight? The key functional properties of voltage‐gated sodium channels, including voltage‐dependent activation. Sodium conductance and selectivity, block by local anesthetics and related drugs, and both fast and slow inactivation, are now understood at the level of protein structure with high resolution. These emerging high‐resolution structural models may lead to development of safer and more efficacious drugs for treatment of epilepsy, chronic pain, and cardiac arrhythmia through structure‐based drug design. Voltage‐gated sodium channels initiate action potentials in nerve, muscle and other excitable cells. Early physiological studies described sodium selectivity, voltage‐dependent activation and fast inactivation, and developed conceptual models for sodium channel function. This review article follows the topics of my 2013 Sharpey‐Schafer Prize Lecture and gives an overview of research using a combination of biochemical, molecular biological, physiological and structural biological approaches that have elucidated the structure and function of sodium channels at the atomic level. Structural models for voltage‐dependent activation, sodium selectivity and conductance, drug block and both fast and slow inactivation are discussed. A perspective for the future envisions new advances in understanding the structural basis for sodium channel function and the opportunity for structure‐based discovery of novel therapeutics
Structural analysis of CavAb, a prokaryotic voltage-gated calcium channel by Teresa Mae Swanson( )

1 edition published in 2016 in English and held by 1 WorldCat member library worldwide

Voltage--gated calcium channels are large membrane proteins that coordinate the movement of calcium into and out of the cell in response to changes in membrane potential, mediating signaling processes such as muscle contraction and synaptic transmission. We used CavAb, a bacterial calcium channel, as a structural model for three Cav channel characteristics; ion selectivity, drug binding, and disease mutations. First, CavAb reveals three binding sites for hydrated calcium within the selectivity filter of the channel, confirming the theory of a "knock-off" mechanism of calcium selectivity. Second, CavAb mimics mammalian Cav antagonist binding properties, providing visualization of bound drug molecules and potential direction for structure based drug design. Finally, the addition of Timothy Syndrome disease mutations into CavAb shows small conformational changes, highlighting the potential importance of channel regulation by lipids. Even though CavAb is a distant ancestor to the mammalian calcium channels, it has proven to be a valuable tool for answering classic calcium channel questions
Prevention of Paralytic Neurotoxin Action on Voltage-Sensitive Sodium Channels( )

1 edition published in 1992 in English and held by 1 WorldCat member library worldwide

Fine-tuning synaptic plasticity by modulation of presynaptic Cav2.1 channels with Ca² sensor proteins by Karina Leal( )

1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

Short-term plasticity of synaptic transmission is recognized as an important component of information processing in neuronal networks. Repetitive firing in neurons either leads to an increase, or to a decrease in synaptic transmission, processes referred to as facilitation and depression. This short-term plasticity behavior of synaptic transmission is specifically regulated at each given synaptic connection. P/Q-type and N-type Ca2+ currents through Cav2.1 and Cav2.2 channels, respectively, are responsible for the Ca2+ entry that initiates neurotransmitter release at most conventional synapses. However, it remains not well understood to what extent regulation of Cav2.1 channels play a role in short-term plasticity. Recent work has shown Ca2+-dependent regulation of Cav2.1 channels to be mediated by calmodulin (CaM) and neuronal Ca sensors (CaS), which include calcium binding protein 1 (CaBP1) and visinin-like protein 2 (VILIP-2). Mutations of the CaS binding sites in the carboxyl terminal of Cav2.1 affect short-term synaptic plasticity. Although it is clear that CaS-dependent regulation of Cav2.1 channels induces synaptic plasticity, it remains unknown which CaS proteins are responsible for these changes. Candidate proteins include, CaM, CaBP1, and VILIP-2, which show differential modulation of Cav2.1 channels in heterologous expression systems; yet, their role in synaptic transmission has not been studied. Here, we show that activity-dependent modulation of presynaptic CaV2.1 channels by CaBP1 and VILIP-2 has opposing effects on short-term synaptic plasticity in superior cervical ganglion (SCG) neurons. Expression of CaBP1, which blocks Ca2+-dependent facilitation of P/Q-type Ca2+ current, markedly reduced facilitation of synaptic transmission. VILIP-2, which blocks Ca2+-dependent inactivation of P/Q-type Ca2+ current, reduced synaptic depression and increased facilitation under conditions of high release probability. These results demonstrate that activity-dependent regulation of presynaptic CaV2.1 channels by differentially expressed CaS proteins can fine-tune synaptic responses to trains of action potentials and thereby contribute to the diversity of short-term synaptic plasticity
Physiology : a one-domain voltage-gated sodium channel in bacteria by William A Catterall( )

1 edition published in 2001 in English and held by 0 WorldCat member libraries worldwide

Ion channels in plasma membrane signal transduction( Book )

1 edition published in 1996 in English and held by 0 WorldCat member libraries worldwide

A 3D view of sodium channels by William A Catterall( )

1 edition published in 2001 in English and held by 0 WorldCat member libraries worldwide

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Goodman & Gilman's the pharmacological basis of therapeutics
English (31)