Hypoxia-inducible factor prolyl hydroxylase domain inhibitor may maintain hemoglobin synthesis at lower serum ferritin and transferrin saturation levels than darbepoetin alfa.
<h4>Background</h4>Hypoxia-inducible factor (HIF) prolyl hydroxylase domain inhibitors, which have recently become clinically available for treating renal anemia, are attracting attention for their novel mechanisms of action.<h4>Methods</h4>Relationships of reticulocyte hemog...
Guardado en:
Autores principales: | Chie Ogawa, Ken Tsuchiya, Naohisa Tomosugi, Kunimi Maeda |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/b997f3f707444cd4a6f422da27d4cb91 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases
por: Rasheduzzaman Chowdhury, et al.
Publicado: (2016) -
Cryo-EM structure of the human ferritin–transferrin receptor 1 complex
por: Linda Celeste Montemiglio, et al.
Publicado: (2019) -
Managing chemotherapy induced anemia with darbepoetin alfa and other erythropoiesis stimulating agents: a nurse's perspective
por: Derbyshire L, et al.
Publicado: (2013) -
Prolyl hydroxylase substrate adenylosuccinate lyase is an oncogenic driver in triple negative breast cancer
por: Giada Zurlo, et al.
Publicado: (2019) -
Use of cyclic peptides to induce crystallization: case study with prolyl hydroxylase domain 2
por: Rasheduzzaman Chowdhury, et al.
Publicado: (2020)