Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Tzur Paldi"'
Publikováno v:
Nordic Pulp & Paper Research Journal. 18:421-428
Autor:
Tzur Paldi
Publikováno v:
Frontiers in Pharmacology
Frontiers in Pharmacology, Vol 3 (2012)
Frontiers in Pharmacology, Vol 3 (2012)
In PNAS, Capes et al. (2012) showed that the voltage sensor of domain IV in the skeletal muscle voltage-dependent sodium channel is energetically coupled to the channel gate located at the outer side of the pore. For this, the authors elicited gating
Autor:
Michael Gurevitz, Tzur Paldi
The voltage sensor is a four-transmembrane helix bundle (S1–S4) that couples changes in membrane potential to conformational alterations in voltage-gated ion channels leading to pore opening and ion conductance. Although the structure of the voltag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b891e1546c15a0a82bb83e8379bbbeb1
https://europepmc.org/articles/PMC2905116/
https://europepmc.org/articles/PMC2905116/
Publikováno v:
Biomaterials. 25(10)
Biodegradable starch- and cellulose-based polymers have a range of properties which make them suitable for use in a wide array of biomedical applications ranging from bone replacement to engineering of tissue scaffolds and drug delivery systems. A no
Publikováno v:
The Biochemical journal. 372(Pt 3)
Carbohydrate-binding modules (CBMs) are protein domains located within a carbohydrate-active enzyme, with a discrete fold that can be separated from the catalytic domain. Starch-binding domains (SBDs) are CBMs that are usually found at the C-terminus
Publikováno v:
XXIst International Carbohydrate Symposium 2002.
Autor:
Tzur Paldi
Publikováno v:
The Journal of Membrane Biology. 245:761-761
Autor:
Paldi, Tzur
Publikováno v:
Journal of Membrane Biology; Nov2012, Vol. 245 Issue 11, p761-761, 1p