Thomas D. Helton

Works (3)

Updated: June 12th, 2023 23:52

2002 journal article

Alternative splicing of a beta(4) subunit proline-rich motif regulates voltage-dependent gating and toxin block of Ca(v)2.1 Ca2+ channels

Journal of Neuroscience, 22(21), 9331–9339.

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
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 journal article

C-terminal alternative splicing changes the gating properties of a human spinal cord calcium channel alpha 1A subunit

Journal of Neuroscience, 20(20), 7564–7570.

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
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

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