Zobrazeno 1 - 3
of 3
pro vyhledávání: '"April Joy Baral"'
Autor:
Peter Laslo, David G. Kent, Edwin Chen, Joanna Baxter, Jeanne F Rivera, Hershna Patel, Emma L Burman, Sally A Boxall, Brian R. Jackson, Ann Mullally, Grace Boyd, Rachael Smyth, Ghadah Alameer, April Joy Baral, Anthony R. Green, Fatima Nadat
Publikováno v:
Blood Adv
Calreticulin (CALR) is mutated in the majority of JAK2/MPL-unmutated myeloproliferative neoplasms (MPNs). Mutant CALR (CALRdel52) exerts its effect by binding to the thrombopoietin receptor MPL to cause constitutive activation of JAK-STAT signaling.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c88bd78a01d6c569428b7041878c47a
https://www.repository.cam.ac.uk/handle/1810/319699
https://www.repository.cam.ac.uk/handle/1810/319699
Autor:
Natalie Florescu, Danielle Beeson, Jeanne F Rivera, April Joy Baral, Gabriel Birrane, Shannon Elf, Edwin Chen, Amy Ko, Ann Mullally, Nouran S. Abdelfattah
Publikováno v:
Blood. 131:782-786
Mutations in calreticulin (CALR) are phenotypic drivers in the pathogenesis of myeloproliferative neoplasms. Mechanistic studies have demonstrated that mutant CALR binds to the thrombopoietin receptor MPL, and that the positive electrostatic charge o
Autor:
Sally A Boxall, Rachael Smyth, Fatima Nadat, Edwin Chen, Ann Mullally, Jeanne F Rivera, Brian R. Jackson, Ghadah Alameer, April Joy Baral, Emma L Burman
Publikováno v:
Blood. 134:312-312
Recurrent mutations in the ER chaperone calreticulin (CALR) are found in ~30% of MPNs. All known CALR mutations result in a +1-frameshift of the CALR reading frame that retains the N-domain and P-arm of wild-type CALR and generates a novel mutant-spe