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pro vyhledávání: '"Novandy K, Lim"'
Autor:
Carolina Alvadia, Novandy K Lim, Vanessa Clerico Mosina, Gert T Oostergetel, Raimund Dutzler, Cristina Paulino
Publikováno v:
eLife, Vol 8 (2019)
The lipid scramblase TMEM16F initiates blood coagulation by catalyzing the exposure of phosphatidylserine in platelets. The protein is part of a family of membrane proteins, which encompasses calcium-activated channels for ions and lipids. Here, we r
Externí odkaz:
https://doaj.org/article/1d8af90c04cc474fb58f8be2bcce36f1
Autor:
Ália, Dos Santos, Andreas, Hadjivasiliou, Felipe, Ossa, Novandy K, Lim, Aylin, Turgut, Maureen E, Taylor, Kurt, Drickamer
Publikováno v:
Protein Science
Protein Science : A Publication of the Protein Society
Protein Science : A Publication of the Protein Society
Human dendritic cell-specific intercellular adhesion molecule-1 grabbing nonintegrin, DC-SIGN, and the sinusoidal endothelial cell receptor DC-SIGNR or L-SIGN, are closely related sugar-binding receptors. DC-SIGN acts both as a pathogen-binding endoc
Autor:
Vanessa Clerico Mosina, Carolina Alvadia, Gert T. Oostergetel, Novandy K. Lim, Cristina Paulino, Raimund Dutzler
SUMMARYThe lipid scramblase TMEM16F initiates blood coagulation by catalyzing the exposure of phosphatidylserine in platelets. The protein is part of a family of membrane proteins, which encompasses calcium-activated channels for ions and lipids. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31b72ed28230da2a39068d50946750fa
https://doi.org/10.1101/455261
https://doi.org/10.1101/455261
Publikováno v:
Biophysical Journal. 110(3)
The TMEM16/Anoctamin family of membrane proteins is broadly expressed in eukaryotes and features a remarkable functional diversity. The family contains the long sought-after Ca2+-activated chloride channels but also lipid scramblases or cation channe
Publikováno v:
The Journal of General Physiology
The TMEM16 family contains dimeric membrane proteins activated by intracellular Ca2+. Realizing that lipid scramblase family members contain two independently activated subunits, Lim et al. use concatenated TMEM16A subunits to show that ion channel m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::839907f639699ba30318ccb5b807cd5d
https://doi.org/10.5167/uzh-127231
https://doi.org/10.5167/uzh-127231
Publikováno v:
Biophysical Journal. 112:421a-422a
Publikováno v:
Nature
The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional diversity. This family contains the long sought-after Ca(2+)-activated chloride channels as well as lipid scramblases and cation channels. Here we present the c
Publikováno v:
Biophysical Journal. 108:382a
TMEM16A is a Ca2+-activated chloride channel that is involved in various physiological processes. The functional behavior of the murine ion channel mTMEM16A has been characterized by electrophysiology. mTMEM16A forms anion-selective channels that are
Publikováno v:
Biophysical Journal. (2):343a
The TMEM16s or anoctamins constitute a class of eukaryotic membrane proteins that in mammals contain ten members with high sequence conservation. Despite their close relationship these proteins are characterized by a remarkable functional diversity.