Results 21 to 30 of about 75,793 (264)

CD71 (Transferrin Receptor) [PDF]

open access: yesAmerican Journal of Clinical Pathology, 2010
Abstract Accurate analysis of the erythroid lineage is essential in evaluating bone marrow biopsy specimens and can be particularly challenging in the setting of dyserythropoiesis. Transferrin receptor (CD71) mediates the uptake of transferrin-iron complexes and is highly expressed on the surface of cells of the erythroid lineage ...
Derek K. Marsee   +2 more
openaire   +1 more source

Transferrin Receptor Functionally Marks Thermogenic Adipocytes

open access: yesFrontiers in Cell and Developmental Biology, 2020
BackgroundThermogenic adipocytes, including beige and brown adipocytes, are critical for thermogenesis and energy homeostasis. Identification of functional cell surface markers of thermogenic adipocytes is of significance for potential application in ...
Jin Qiu   +18 more
doaj   +1 more source

Iron metabolism and type 2 diabetes mellitus: A meta‐analysis and systematic review

open access: yesJournal of Diabetes Investigation, 2020
Aims/Introduction Iron metabolism can directly or indirectly affect the occurrence and development of type 2 diabetes. This meta‐analysis and systematic review aimed to analyze the association between serum iron metabolism indicators and type 2 diabetes.
Jingfang Liu   +3 more
doaj   +1 more source

The extrahepatic role of TFR2 in iron homeostasis

open access: yesFrontiers in Pharmacology, 2014
Transferrin receptor 2 (TFR2), a protein homologous to the cell iron importer transferrin receptor 1 (TFR1), is expressed in the liver and erythroid cells and is reported to bind diferric transferrin, although at lower affinity than TFR1.
Laura eSilvestri   +3 more
doaj   +1 more source

Role of the clathrin adaptor PICALM in normal hematopoiesis and polycythemia vera pathophysiology

open access: yesHaematologica, 2015
Clathrin-dependent endocytosis is an essential cellular process shared by all cell types. Despite this, precisely how endocytosis is regulated in a cell-type-specific manner and how this key pathway functions physiologically or pathophysiologically ...
Yuichi Ishikawa   +14 more
doaj   +1 more source

H-Ferritin Is Preferentially Incorporated by Human Erythroid Cells through Transferrin Receptor 1 in a Threshold-Dependent Manner. [PDF]

open access: yesPLoS ONE, 2015
Ferritin is an iron-storage protein composed of different ratios of 24 light (L) and heavy (H) subunits. The serum level of ferritin is a clinical marker of the body's iron level.
Soichiro Sakamoto   +8 more
doaj   +1 more source

Modeling of the N-glycosylated transferrin receptor suggests how transferrin binding can occur within the surface coat of Trypanosoma brucei.

open access: yesPLoS Pathogens, 2012
The transferrin receptor of bloodstream form Trypanosoma brucei is a heterodimer encoded by expression site associated genes 6 and 7. This low-abundance glycoprotein with a single glycosylphosphatidylinositol membrane anchor and eight potential N ...
Angela Mehlert   +2 more
doaj   +1 more source

Transferrin receptor in primary and metastatic breast cancer: Evaluation of expression and experimental modulation to improve molecular targeting.

open access: yesPLoS ONE, 2023
BackgroundConjugation of transferrin (Tf) to imaging or nanotherapeutic agents is a promising strategy to target breast cancer. Since the efficacy of these biomaterials often depends on the overexpression of the targeted receptor, we set out to survey ...
Francesca Fontana   +17 more
doaj   +1 more source

Influence of Protein Carbonylation on Human Adipose Tissue Dysfunction in Obesity and Insulin Resistance

open access: yesBiomedicines, 2022
Background: Obesity is characterized by adipose tissue dysregulation and predisposes individuals to insulin resistance and type 2 diabetes. At the molecular level, adipocyte dysfunction has been linked to obesity-triggered oxidative stress and protein ...
M. Carmen Navarro-Ruiz   +12 more
doaj   +1 more source

Structural biology of ferritin nanocages

open access: yesFEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

Home - About - Disclaimer - Privacy