Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Ashley Vanderbeck"'
Autor:
Janina Sprenger, Anda Trifan, Neal Patel, Ashley Vanderbeck, Jenny Bredfelt, Emad Tajkhorshid, Roger Rowlett, Leila Lo Leggio, Karin S. Åkerfeldt, Sara Linse
Publikováno v:
Current Research in Structural Biology, Vol 3, Iss , Pp 121-132 (2021)
Calmodulin (CaM) is a ubiquitous Ca2+ sensing protein that binds to and modulates numerous target proteins and enzymes during cellular signaling processes. A large number of CaM-target complexes have been identified and structurally characterized, re
Externí odkaz:
https://doaj.org/article/ca9bbe845bb241dc86a94af47d5c09fb
Autor:
Lyndsay Avery, Tanner F. Robertson, Christine F. Wu, Nathan H. Roy, Samuel D. Chauvin, Eric Perkey, Ashley Vanderbeck, Ivan Maillard, Janis K. Burkhardt
Publikováno v:
Frontiers in Immunology, Vol 12 (2022)
X-linked moesin associated immunodeficiency (X-MAID) is a primary immunodeficiency disease in which patients suffer from profound lymphopenia leading to recurrent infections. The disease is caused by a single point mutation leading to a R171W amino a
Externí odkaz:
https://doaj.org/article/5d9b6894ef484ac99865935e08f454e1
Autor:
Leolene Carrington, Shovik Bandyopadhyay, Katlyn Lederer, Samantha Kelly, Ashley Vanderbeck, Gloria Jih, Frederick Allen, Daniela Gómez Atria, Anneka Allman, Eric Perkey, Kai Tan, Norbert Pardi, Burkhard Ludewig, Ronjon Chakraverty, Ivan Maillard
Publikováno v:
Blood. 140:7334-7335
Autor:
Leila Lo Leggio, J. Sprenger, Emad Tajkhorshid, Ashley Vanderbeck, Jenny Bredfelt, Neal Patel, Sara Linse, Karin S. Åkerfeldt, Roger S. Rowlett, Anda Trifan
Publikováno v:
'Current Research in Structural Biology ', vol: 3, pages: 121-132 (2021)
Current Research in Structural Biology, Vol 3, Iss, Pp 121-132 (2021)
Current research in structural biology 3, 121-132 (2021). doi:10.1016/j.crstbi.2021.05.001
Current Research in Structural Biology
Sprenger, J, Trifan, A, Patel, N, Vanderbeck, A, Bredfelt, J, Tajkhorshid, E, Rowlett, R, Lo Leggio, L, Åkerfeldt, K S & Linse, S 2021, ' Calmodulin complexes with brain and muscle creatine kinase peptides ', Current Research in Structural Biology, vol. 3, pp. 121-132 . https://doi.org/10.1016/j.crstbi.2021.05.001
Current Research in Structural Biology, Vol 3, Iss, Pp 121-132 (2021)
Current research in structural biology 3, 121-132 (2021). doi:10.1016/j.crstbi.2021.05.001
Current Research in Structural Biology
Sprenger, J, Trifan, A, Patel, N, Vanderbeck, A, Bredfelt, J, Tajkhorshid, E, Rowlett, R, Lo Leggio, L, Åkerfeldt, K S & Linse, S 2021, ' Calmodulin complexes with brain and muscle creatine kinase peptides ', Current Research in Structural Biology, vol. 3, pp. 121-132 . https://doi.org/10.1016/j.crstbi.2021.05.001
Current research in structural biology 3, 121-132 (2021). doi:10.1016/j.crstbi.2021.05.001
Calmodulin (CaM) is a ubiquitous Ca$^{2+}$ sensing protein that binds to and modulates numerous target proteins and enzymes during cellular signaling proc
Calmodulin (CaM) is a ubiquitous Ca$^{2+}$ sensing protein that binds to and modulates numerous target proteins and enzymes during cellular signaling proc
Autor:
Victor Tkachev, Ashley Vanderbeck, Eric Perkey, Scott N. Furlan, Connor McGuckin, Daniela Gómez Atria, Ulrike Gerdemann, Xianliang Rui, Jennifer Lane, Daniel J. Hunt, Hengqi Zheng, Lucrezia Colonna, Michelle Hoffman, Alison Yu, Samantha Kelly, Anneka Allman, Brandon Burbach, Yoji Shimizu, Angela Panoskaltsis-Mortari, Guoying Chen, Stephen M. Carpenter, Olivier Harari, Frank Kuhnert, Gavin Thurston, Bruce R. Blazar, Leslie S. Kean, Ivan Maillard
Notch signaling promotes T-cell pathogenicity and graft-versus-host disease (GVHD) after allogeneic hematopoietic cell transplantation (allo-HCT) in mice, with a dominant role for the Delta-like ligand DLL4. To assess if Notch’s effects are evoluti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d7537e5f3939cb946abc2aed68e7ba97
https://doi.org/10.1101/2022.04.23.488844
https://doi.org/10.1101/2022.04.23.488844
Autor:
Ashley Vanderbeck, Samantha Kelly, Leolene Carrington, Eric Perkey, Anneka Allman, Frederick Allen, Joshua D Brandstadter, Burkhard Ludewig, Chris Siebel
Publikováno v:
Blood. 140:7363-7363
Differential impact of a dyskeratosis congenita mutation in TPP1 on mouse hematopoiesis and germline
Autor:
Saher Sue Hammoud, Aniela Crayton, Jacqueline Graniel, Peedikayil E. Thomas, Leolene J Carrington, Catherine E. Keegan, Joshua D Brandstadter, Jayakrishnan Nandakumar, Adrienne Niederriter Shami, James J. White, Kamlesh Bisht, Alina Moroz, Jennifer Chase, Frederick Allen, Ann Friedman, Eric Perkey, Ivan Maillard, Anna Mychalowych, Mariel Manzor, Ashley Vanderbeck
Publikováno v:
Life Science Alliance
A TPP1 mutation known to cause telomere shortening and bone marrow failure in humans recapitulates telomere loss but results in severe germline defects in mice without impacting murine hematopoiesis.
Telomerase extends chromosome ends in somatic
Telomerase extends chromosome ends in somatic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31f399ba0af60580eccc81bcad6af3e0
https://doi.org/10.1101/2021.07.29.454392
https://doi.org/10.1101/2021.07.29.454392
Autor:
Ivan Maillard, Ashley Vanderbeck
Publikováno v:
Journal of leukocyte biologyREFERENCES. 109(3)
Notch signaling is an evolutionarily conserved cell-to-cell signaling pathway that regulates cellular differentiation and function across multiple tissue types and developmental stages. In this review, we discuss our current understanding of Notch si
Autor:
Ashley Vanderbeck, Ivan Maillard
Publikováno v:
Haematologica
Loss-of-function studies have determined that Notch signaling is essential for hematopoietic and endothelial development. By deleting a single allele of the Notch1 transcriptional activation domain we generated viable, post-natal mice exhibiting hypo
Autor:
Karin S. Åkerfeldt, Leila Lo Leggio, Sara Linse, Ann-Victoria Isaak, Janina Sprenger, Ashley Vanderbeck, Neal Patel, Jenny Bredtfelt
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 74:e213-e213