Thomas D. Helton

Works (3)

Updated: June 12th, 2023 23:52

2002 article

Alternative Splicing of a β4Subunit Proline-Rich Motif Regulates Voltage-Dependent Gating and Toxin Block of Cav2.1 Ca2+Channels

Helton, T. D., Kojetin, D. J., Cavanagh, J., & Horne, W. A. (2002, November 1). Journal of Neuroscience.

By: T. Helton*, D. Kojetin n, J. Cavanagh n & W. Horne*

MeSH headings : Alternative Splicing / physiology; Amino Acid Motifs / physiology; Animals; Brain / metabolism; Calcium Channel Blockers / pharmacology; Calcium Channels, N-Type / drug effects; Calcium Channels, N-Type / genetics; Calcium Channels, N-Type / metabolism; Humans; Ion Channel Gating / drug effects; Ion Channel Gating / physiology; Membrane Potentials / physiology; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nerve Tissue Proteins / genetics; Oocytes / metabolism; Organ Specificity; Patch-Clamp Techniques; Protein Structure, Tertiary / physiology; Protein Subunits / drug effects; Protein Subunits / genetics; Protein Subunits / metabolism; RNA, Messenger / metabolism; Sequence Deletion; Sequence Homology, Amino Acid; Spinal Cord / metabolism; Structure-Activity Relationship; Xenopus laevis; omega-Conotoxins / pharmacology
topics (OpenAlex): Ion channel regulation and function; Cardiac electrophysiology and arrhythmias; Neuroscience and Neuropharmacology Research
TL;DR: The models reveal that alternative splicing of the β4 N terminus results in dramatic differences in surface charge distribution and localize the proline-rich motif of β4b to an extended arm structure that flanks what would be the equivalent of a highly modified PSD-95 carboxylate binding loop. (via Semantic Scholar)
Source: NC State University Libraries
Added: August 6, 2018

2002 journal article

Alternative splicing of the beta(4) subunit has alpha(1) subunit subtype-specific effects on Ca2+ channel gating

Journal of Neuroscience, 22(5), 1573–1582.

By: T. Helton & W. Horne

Source: NC State University Libraries
Added: August 6, 2018

2000 article

C-Terminal Alternative Splicing Changes the Gating Properties of a Human Spinal Cord Calcium Channel α1A Subunit

Krovetz, H. S., Helton, T. D., Crews, A. L., & Horne, W. A. (2000, October 15). Journal of Neuroscience.

By: H. Krovetz n, T. Helton n, A. Crews n & W. Horne n

MeSH headings : Alternative Splicing; Amino Acid Substitution; Animals; Calcium Channels / genetics; Calcium Channels / metabolism; Cells, Cultured; Cerebellum / metabolism; Exons; Gene Expression; Humans; Ion Channel Gating / genetics; Membrane Potentials / physiology; Microinjections; Molecular Sequence Data; Nerve Tissue Proteins / genetics; Nerve Tissue Proteins / metabolism; Oocytes / metabolism; Patch-Clamp Techniques; Protein Isoforms / genetics; Protein Isoforms / metabolism; Recombinant Fusion Proteins / genetics; Recombinant Fusion Proteins / metabolism; Spinal Cord / metabolism; Xenopus
topics (OpenAlex): Ion channel regulation and function; Neuroscience and Neuropharmacology Research; Nicotinic Acetylcholine Receptors Study
TL;DR: It is demonstrated that C-terminal structural changes alone can influence the way in which α1A subunits respond to a depolarizing stimulus and add to the developing picture of the C terminus as a critical domain in the regulation of Ca2+ channel function. (via Semantic Scholar)
Source: NC State University Libraries
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2026) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.