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Total: 15 results
  • Wheat germ agglutinin-conjugated fluorescent pH sensors for visualizing proton fluxes

    Author(s): Lejie Zhang,Mei Zhang,Karl Bellve,Kevin E Fogarty,Maite A Castro,Sebastian Brauchi,William R Kobertz
    Small-molecule fluorescent wheat germ agglutinin (WGA) conjugates are routinely used to demarcate mammalian plasma membranes, because they bind to the cell's glycocalyx. Here, we describe the derivatization of WGA with a pH-sensitive rhodamine fluorophore (pHRho; pKa = 7) to detect proton channel fl...
  • Oddballs in the Shaker family: Kv2-related regulatory subunits

    Author(s): William R Kobertz
    Kobertz comments on the family of “silent” Kv2-related regulatory subunits and a new study investigating their assembly idiosyncrasies.
  • The Proton-Coupled Monocarboxylate Transporter Hermes Is Necessary for Autophagy during Cell Death

    Author(s): Panagiotis D Velentzas,Lejie Zhang,Gautam Das,Tsun-Kai Chang,Charles Nelson,William R Kobertz,Eric H Baehrecke
    Nutrient availability influences the production and degradation of materials that are required for cell growth and survival. Autophagy is a nutrient-regulated process that is used to degrade cytoplasmic materials and has been associated with human diseases. Solute transporters influence nutrient ava...
  • Palladium-Mediated Synthesis of a Near-Infrared Fluorescent K+ Sensor

    Author(s): H M Dhammika Bandara,Zhengmao Hua,Mei Zhang,Steven M Pauff,Stephen C Miller,Elizabeth A Colby Davie,William R Kobertz
    Potassium (K^(+)) exits electrically excitable cells during normal and pathophysiological activity. Currently, K^(+)-sensitive electrodes and electrical measurements are the primary tools to detect K^(+) fluxes. Here, we describe the synthesis of a near-IR, oxazine fluorescent K^(+) sensor (K(NIR)-1...
  • Fluorescent Visualization of Cellular Proton Fluxes

    Author(s): Lejie Zhang,Karl Bellve,Kevin Fogarty,William R Kobertz
    Cells use plasma membrane proton fluxes to maintain cytoplasmic and extracellular pH and to mediate the co-transport of metabolites and ions. Because proton-coupled transport often involves movement of multiple substrates, traditional electrical measurements provide limited information about proton ...
  • Erratum to: Mutant SOD1 protein increases Nav1.3 channel excitability

    Author(s): Elif Kubat Öktem,Karen Mruk,Joshua Chang,Ata Akin,William R Kobertz,Robert H Brown
    No abstract
  • Mutant SOD1 protein increases Nav1.3 channel excitability

    Author(s): Elif Kubat Öktem,Karen Mruk,Joshua Chang,Ata Akin,William R Kobertz,Robert H Brown
    Amyotrophic lateral sclerosis (ALS) is a lethal paralytic disease caused by the degeneration of motor neurons in the spinal cord, brain stem, and motor cortex. Mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) are present in ~20% of familial ALS and ~2% of all ALS cases. The mos...
  • Bioreactive Tethers

    Author(s): Karen Mruk,William R Kobertz
    Ion channel complexes are challenging to study by traditional biochemical methods due to their membranous lipid environment and large size. Bioreactive tethers are specialized chemical probes that have been used in electrophysiological experiments to provide unique insight into ion channel structure...
  • LQT1 mutations in KCNQ1 C-terminus assembly domain suppress IKs using different mechanisms

    Author(s): Ademuyiwa S Aromolaran,Prakash Subramanyam,Donald D Chang,William R Kobertz,Henry M Colecraft
    CONCLUSION: Distinct LQT1 mutations in KCNQ1 assembly domain decrease IKs using unique combinations of biophysical and trafficking mechanisms. Functional deficits in IKs observed in heterologous cells are mostly, but not completely, recapitulated in adult rat cardiomyocytes. A 'methodological chain'...
  • The middle X residue influences cotranslational N-glycosylation consensus site skipping

    Author(s): Heidi L H Malaby,William R Kobertz
    Asparagine (N)-linked glycosylation is essential for efficient protein folding in the endoplasmic reticulum (ER) and anterograde trafficking through the secretory pathway. N-Glycans are attached to nascent polypeptides at consensus sites, N-X-T/S (X ≠ P), by one of two enzymatic isoforms of the olig...
  • Calmodulation meta-analysis: predicting calmodulin binding via canonical motif clustering

    Author(s): Karen Mruk,Brian M Farley,Alan W Ritacco,William R Kobertz
    The calcium-binding protein calmodulin (CaM) directly binds to membrane transport proteins to modulate their function in response to changes in intracellular calcium concentrations. Because CaM recognizes and binds to a wide variety of target sequences, identifying CaM-binding sites is difficult, re...
  • Stoichiometry of the cardiac IKs complex

    Author(s): William R Kobertz
    No abstract
  • Molecular determinants of co- and post-translational N-glycosylation of type I transmembrane peptides

    Author(s): Heidi L H Malaby,William R Kobertz
    Type I transmembrane peptides acquire N-linked glycans during and after protein synthesis to facilitate anterograde trafficking through the secretory pathway. Mutations in N-glycosylation consensus sites (NXT and NXS, where X≠P) that alter the kinetics of the initial N-glycan attachment have been as...
  • Chemical derivatization and purification of peptide-toxins for probing ion channel complexes

    Author(s): Zhengmao Hua,William R Kobertz
    Ion channels function as multi-protein complexes made up of ion-conducting α-subunits and regulatory β-subunits. To detect, identify, and quantitate the regulatory β-subunits in functioning K(+) channel complexes, we have chemically derivatized peptide-toxins that specifically react with strategical...
  • Structural insights into neuronal K+ channel-calmodulin complexes

    Author(s): Karen Mruk,Shiven M D Shandilya,Robert O Blaustein,Celia A Schiffer,William R Kobertz
    Calmodulin (CaM) is a ubiquitous intracellular calcium sensor that directly binds to and modulates a wide variety of ion channels. Despite the large repository of high-resolution structures of CaM bound to peptide fragments derived from ion channels, there is no structural information about CaM boun...

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