Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Hadassa Shaked"'
Autor:
Dror Eliaz, Sriram Kannan, Hadassa Shaked, Gil Arvatz, Itai Dov Tkacz, Lior Binder, Hiba Waldman Ben-Asher, Uthman Okalang, Vaibhav Chikne, Smadar Cohen-Chalamish, Shulamit Michaeli
Publikováno v:
PLoS Pathogens, Vol 13, Iss 3, p e1006245 (2017)
Extracellular vesicles (EV) secreted by pathogens function in a variety of biological processes. Here, we demonstrate that in the protozoan parasite Trypanosoma brucei, exosome secretion is induced by stress that affects trans-splicing. Following per
Externí odkaz:
https://doaj.org/article/6d5be7b6dfff4aee9b63fbe6eef425a2
Autor:
Chen Guttman, Geula Davidov, Hadassa Shaked, Sofiya Kolusheva, Ronit Bitton, Atish Ganguly, Jeff F Miller, Jordan H Chill, Raz Zarivach
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e55650 (2013)
BteA, a 69-kDa cytotoxic protein, is a type III secretion system (T3SS) effector in the classical Bordetella, the etiological agents of pertussis and related mammalian respiratory diseases. Currently there is limited information regarding the structu
Externí odkaz:
https://doaj.org/article/ea0787a531724d9a85fcfb9dd8c0de3d
Autor:
Chen Guttman, Geula Davidov, Adi Yahalom, Hadassa Shaked, Sofiya Kolusheva, Ronit Bitton, Shiran Barber-Zucker, Jordan H Chill, Raz Zarivach
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e81557 (2013)
Bordetella pertussis, the etiological agent of "whooping cough" disease, utilizes the type III secretion system (T3SS) to deliver a 69 kDa cytotoxic effector protein, BteA, directly into the host cells. As with other T3SS effectors, prior to its secr
Externí odkaz:
https://doaj.org/article/170ed984def44f2d8f50b288c5223983
Publikováno v:
Journal of the American Chemical Society. 144(26)
The pathogen
Autor:
Sofiya Kolusheva, Raz Zarivach, Hadassa Shaked, Geula Davidov, Jordan H. Chill, Shiran Barber-Zucker, Adi Yahalom
Publikováno v:
Biochimica et biophysica acta. Biomembranes. 1861(12)
BteA, a 69-kDa cytotoxic protein, is a type III secretion system (T3SS) effector in the classical Bordetella, the etiological agents of pertussis and related mammalian respiratory diseases. Like other cytotoxicity-mediating effectors, BteA uses its m
Autor:
Zena Qasem, Arwa Qasim, Hadassa Shaked, Orel Hirschhorn, Inbal Sher, Jordan H. Chill, Sharon Ruthstein
Publikováno v:
Chembiochem : a European journal of chemical biology. 20(6)
The bacterial potassium channel KcsA is gated by pH, opening for conduction under acidic conditions. Molecular determinants responsible for this effect have been identified at the extracellular selectivity filter, at the membrane-cytoplasm interface
Autor:
Eva Rozentur-Shkop, Jordan H. Chill, Adi Halle-Bikovski, Mira Barda-Saad, Noah Joseph, Sophia Fried, Hadassa Shaked, Guy Biber
Publikováno v:
ACS chemical biology. 13(1)
Wiskott-Aldrich syndrome protein (WASp) is exclusively expressed in hematopoietic cells and responsible for actin-dependent processes, including cellular activation, migration, and invasiveness. The C-terminal domain of WASp-Interacting Protein (WIP)
Autor:
Hiba Waldman Ben-Asher, Lior Binder, Shulamit Michaeli, Gil Arvatz, Vaibhav Chikne, Uthman Okalang, Dror Eliaz, Sriram Kannan, Hadassa Shaked, Smadar Cohen-Chalamish, Itai Dov Tkacz
Publikováno v:
PLoS Pathogens, Vol 13, Iss 3, p e1006245 (2017)
PLoS Pathogens
PLoS Pathogens
Extracellular vesicles (EV) secreted by pathogens function in a variety of biological processes. Here, we demonstrate that in the protozoan parasite Trypanosoma brucei, exosome secretion is induced by stress that affects trans-splicing. Following per
Publikováno v:
Protein Science. 23:1403-1416
The cytoplasmic C-terminal domain (CTD) of KcsA, a bacterial homotetrameric potassium channel, is an amphiphilic domain that forms a helical bundle with four-fold symmetry mediated by hydrophobic and electrostatic interactions. Previously we have est
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838(3):784-792
Oligomerization of hepatitis C viral envelope proteins E1 and E2 is essential to virus fusion and assembly. Although interactions within the transmembrane (TM) domains of these glycoproteins have proven contributions to the E1/E2 heterodimerization p