Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Kenneth M. Blumenthal"'
Autor:
Reiko Teshima, Lars K. Poulsen, Kathleen M. Schegg, Jean-Baptiste Rascle, Laura Privalle, Rod A. Herman, David Rouquié, Corinne Herouet-Guicheney, Nancy G. Doerrer, Jason M. Ward, Scott McClain, Kazumi Kitta, Rie Satoh, Kenneth M. Blumenthal, Leslie M. Hicks, Gregory S. Ladics, Gang-hua Lang, Bénédicte Labory-Carcenac
Publikováno v:
SC10201706260015
Bioscience, Biotechnology, and Biochemistry
Biosci Biotechnol Biochem
Bioscience, Biotechnology, and Biochemistry
Biosci Biotechnol Biochem
In rice, several allergens have been identified such as the non-specific lipid transfer protein-1, the α-amylase/trypsin-inhibitors, the α-globulin, the 33 kDa glyoxalase I (Gly I), the 52–63 kDa globulin, and the granule-bound starch synthetase.
Publikováno v:
Molecular Pharmacology. 86:159-167
Voltage-gated sodium channels are critical determinants of nerve and muscle excitability. Although numerous toxins and small molecules target sodium channels, identifying the mechanisms of action is challenging. Here we used gating-pore currents sele
Publikováno v:
Toxicon. 52:489-500
The peptide toxin ProTxII, recently isolated from the venom of the tarantula spider Thrixopelma pruriens, modifies gating in voltage-gated Na+ and Ca2+ channels. ProTxII is distinct from other known Na+ channel gating modifier toxins in that it affec
Autor:
Kenneth M. Blumenthal, James A. Fallavollita, Rebeccah F. Young, Maciej Lis, Mulchand S. Patel, Brian Page, Lioubov G. Korotchkina, Vijay Iyer, John M. Canty, Gen Suzuki
Publikováno v:
Circulation Research. 102:103-112
Hibernating myocardium is accompanied by a downregulation in energy utilization that prevents the immediate development of ischemia during stress at the expense of an attenuated level of regional contractile function. We used a discovery based proteo
Publikováno v:
Journal of Biological Chemistry. 282:12687-12697
Voltage-gated Na+ channels are critical components in the generation of action potentials in excitable cells, but despite numerous structure-function studies on these proteins, their gating mechanism remains unclear. Peptide toxins often modify chann
Autor:
Rebeccah F. Young, Kenneth M. Blumenthal, Richard Salvi, Donald E. Coling, Dalian Ding, Maciej Lis, Elizabeth Stofko
Publikováno v:
Hearing Research. 226:140-156
To identify early changes in protein expression associated with cisplatin ototoxicity, we used two dimensional-difference gel electrophoresis (2D-DIGE) and matrix-assisted laser desorption-time-of-flight (MALDI-TOF) mass spectrometry to analyze prote
Autor:
Kenneth M. Blumenthal, Jaime J. Smith
Publikováno v:
Toxicon. 49:159-170
Sea anemone toxins, whose biological function is the capture of marine prey, are invaluable tools for studying the structure and function of mammalian voltage-gated sodium channels. Their high degree of specificity and selectivity have allowed for de
Publikováno v:
Journal of Biological Chemistry. 280:11127-11133
It has been shown recently that polypeptide toxins that modulate the gating properties of voltage-sensitive cation channels are able to bind to phospholipid membranes, leading to the suggestion that these toxins are able to access a channel-binding s
Publikováno v:
Biochemistry. 43:7082-7089
Anthopleurin B (ApB) is a type 1 sea anemone toxin, which binds to voltage-sensitive sodium channels (Na(V)'s), thereby delaying channel inactivation. Previous work from our laboratories has demonstrated that the structurally unconstrained region inv
Autor:
Anna L. Seibert, Kenneth M. Blumenthal
Publikováno v:
Cell Biochemistry and Biophysics. 38:215-238
Neurotoxins have served as invaluable agents for identification, purification, and functional characterization of voltage-gated ion channels. Multiple classes of these toxins, which target voltage- gated Na+ channels via high-affinity binding to dist