Results 41 to 50 of about 136,712 (243)

A Novel High-Content Immunofluorescence Assay as a Tool to Identify at the Single Cell Level γ-Globin Inducing Compounds. [PDF]

open access: yesPLoS ONE, 2015
The identification of drugs capable of reactivating γ-globin to ameliorate β-thalassemia and Sickle Cell anemia is still a challenge, as available γ-globin inducers still have limited clinical indications.
Marta Durlak   +14 more
doaj   +1 more source

Physiological and Aberrant γ-Globin Transcription During Development

open access: yesFrontiers in Cell and Developmental Biology, 2021
The expression of the fetal Gγ- and Aγ-globin genes in normal development is confined to the fetal period, where two γ-globin chains assemble with two α-globin chains to form α2γ2 tetramers (HbF). HbF sustains oxygen delivery to tissues until birth, when
Gloria Barbarani   +4 more
doaj   +1 more source

Globin-based redox signaling [PDF]

open access: yesWorm, 2016
In recent years, moderate levels of reactive oxygen species (ROS) have become recognized as signaling cues that participate at all levels of cellular organization. Globins, with their redox-active heme iron and ubiquitous presence, seem ideally suited to participate in ROS metabolism.
De Henau, Sasha, Braeckman, Bart
openaire   +3 more sources

Introduction and Expression of a Rabbit β-globin Gene in Mouse Fibroblasts [PDF]

open access: yes, 1979
The cloned chromosomal rabbit ß-globin gene has been introduced into mouse fibroblasts by DNA-mediated gene transfer (transformation). In this report, we examine the expression of the rabbit gene in six independent transformants that contain from 1 to 20
Axel, R.   +5 more
core  

Post-transcriptional regulation of satellite cell quiescence by TTP-mediated mRNA decay. [PDF]

open access: yes, 2015
Skeletal muscle satellite cells in their niche are quiescent and upon muscle injury, exit quiescence, proliferate to repair muscle tissue, and self-renew to replenish the satellite cell population.
Blackshear, Perry J   +7 more
core   +2 more sources

A Cryoprotectant‐Compatible Nanoporous Platform for Stable and Scalable Delivery of Biopharmaceuticals

open access: yesAdvanced Materials, EarlyView.
A cryoprotectant‐compatible nanoporous platform enables ambient‐stable and scalable delivery of gene editing therapeutics. By combining hierarchical pore architecture with optimized lyophilization chemistry, the system preserves Cas9‐RNP activity post‐freeze‐drying.
Sian Lee   +8 more
wiley   +1 more source

POGZ Is Required for Silencing Mouse Embryonic β-like Hemoglobin and Human Fetal Hemoglobin Expression

open access: yesCell Reports, 2018
Summary: Fetal globin genes are transcriptionally silenced during embryogenesis through hemoglobin switching. Strategies to derepress fetal globin expression in the adult could alleviate symptoms in sickle cell disease and β-thalassemia.
Bjorg Gudmundsdottir   +16 more
doaj   +1 more source

Cotranslational Folding of Globin [PDF]

open access: yesJournal of Biological Chemistry, 1997
Globin synthesis in a wheat germ cell-free translation system was performed in the presence of [3H]hemin and [35S]methionine to determine the minimal length of the nascent ribosome-bound globin chain capable of heme binding. Nascent polypeptides of predetermined size were synthesized on ribosomes by translation of truncated mRNA molecules.
A A, Komar   +3 more
openaire   +2 more sources

A Central Somatic Transmission Mediates Proprioceptive Facilitation of Muscle Pain

open access: yesAdvanced Science, EarlyView.
Zhang et al. uncover a novel central mechanism for persistent muscle pain, in which TRPA1 sensitization in MeV proprioceptive neurons enhances somatic secretion. This, in turn, disinhibits descending pain control from neighboring noradrenergic locus coeruleus neurons via local GABAergic circuits, thereby promoting inflammatory muscle pain.
Xiaoyu Zhang   +15 more
wiley   +1 more source

Differences in cattle globins [PDF]

open access: yesBiochemical Journal, 1965
1. Comparisons have been made between electrophoretic mobilities of the cattle haemoglobins, HbA, HbB, HbC, HbD and HbF, at pH8.9. The fastest was HbB, then came in decreasing order HbF, HbC, HbA and HbD. 2. Globins were prepared from the main fractions of the five haemoglobins by CM-cellulose chromatography and investigated by starch-gel ...
G, Efremov, M, Braend
openaire   +2 more sources

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